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Conserved domains on  [gi|6319951|ref|NP_010032|]
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putative aryl-alcohol dehydrogenase [Saccharomyces cerevisiae S288C]

Protein Classification

aldo/keto reductase( domain architecture ID 14442742)

aldo/keto reductase is a soluble NAD(P)(H) oxidoreductase that catalyzes the reduction of aldehydes and ketones to their corresponding primary and secondary alcohols

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AKR_AKR9A3_9B1-4 cd19147
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ...
17-335 0e+00

Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.


:

Pssm-ID: 381373 [Multi-domain]  Cd Length: 319  Bit Score: 639.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   17 FLSETAAIKVSPLILGEVSYDGARSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRLRDQIV 96
Cdd:cd19147   1 VLSKTAGIRVSPLILGAMSIGDAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRDQIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   97 IATKFIKSDKKYKAGESNTANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLG 176
Cdd:cd19147  81 IATKFTTDYKAYEVGKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  177 VSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGI 256
Cdd:cd19147 161 VSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKKAVEERKKNGEGL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319951  257 RSFVGASEQTDAEIKISEALAKIAEEHGTESVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19147 241 RSFVGGTEQTPEEVKISEALEKVAEEHGTESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
 
Name Accession Description Interval E-value
AKR_AKR9A3_9B1-4 cd19147
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ...
17-335 0e+00

Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.


Pssm-ID: 381373 [Multi-domain]  Cd Length: 319  Bit Score: 639.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   17 FLSETAAIKVSPLILGEVSYDGARSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRLRDQIV 96
Cdd:cd19147   1 VLSKTAGIRVSPLILGAMSIGDAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRDQIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   97 IATKFIKSDKKYKAGESNTANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLG 176
Cdd:cd19147  81 IATKFTTDYKAYEVGKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  177 VSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGI 256
Cdd:cd19147 161 VSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKKAVEERKKNGEGL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319951  257 RSFVGASEQTDAEIKISEALAKIAEEHGTESVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19147 241 RSFVGGTEQTPEEVKISEALEKVAEEHGTESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
24-339 1.50e-72

Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440431 [Multi-domain]  Cd Length: 316  Bit Score: 228.14  E-value: 1.50e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   24 IKVSPLILGEVSYdgarSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlRDQIVIATKFIk 103
Cdd:COG0667  11 LKVSRLGLGTMTF----GGPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRP-RDDVVIATKVG- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  104 sdkkYKAGESntANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAW 183
Cdd:COG0667  85 ----RRMGPG--PNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  184 VVSAANyyATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGIRSFVGAS 263
Cdd:COG0667 159 QLRRAL--AIAEGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRAATNFVQG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  264 EQTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKaknffPSVEG-----GKIEDLKENIKALSIDLTPDNIKYLESIV 338
Cdd:COG0667 237 YLTERNLALVDALRAIAAEHGV-TPAQLALAWLLAQ-----PGVTSvipgaRSPEQLEENLAAADLELSAEDLAALDAAL 310

                .
gi 6319951  339 P 339
Cdd:COG0667 311 A 311
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
46-338 2.25e-70

Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.


Pssm-ID: 425554 [Multi-domain]  Cd Length: 290  Bit Score: 221.80  E-value: 2.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951     46 SMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRL-RDQIVIATKFIKSDKKYKAGesntanycgNHKR 124
Cdd:pfam00248  14 PISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVkRDKVVIATKVPDGDGPWPSG---------GSKE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    125 SLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSaanyYATSYGKTPFSIYQ 204
Cdd:pfam00248  85 NIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIE----KALTKGKIPIVAVQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    205 GKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGIRSFVgasEQTDAEIKISEALAKIAEEHG 284
Cdd:pfam00248 161 VEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLK---KGTPLNLEALEALEEIAKEHG 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6319951    285 tESVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLESIV 338
Cdd:pfam00248 238 -VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
tas PRK10625
putative aldo-keto reductase; Provisional
22-337 1.73e-20

putative aldo-keto reductase; Provisional


Pssm-ID: 236727 [Multi-domain]  Cd Length: 346  Bit Score: 91.07  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    22 AAIKVSPLILGEVSYDGARSDflksmnkNRAFELLDTFYEAGGNFIDAAN--------NCQNeQSEEWIGEWIQSRRLRD 93
Cdd:PRK10625   9 SSLEVSTLGLGTMTFGEQNSE-------ADAHAQLDYAVAQGINLIDVAEmypvpprpETQG-LTETYIGNWLAKRGSRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    94 QIVIATKFIKSDKKYKAG-ESNTANYCGNHKRSLHvsvrDSLRKLQTDWIDILYVHW--------------WDYMSSIEE 158
Cdd:PRK10625  81 KLIIASKVSGPSRNNDKGiRPNQALDRKNIREALH----DSLKRLQTDYLDLYQVHWpqrptncfgklgysWTDSAPAVS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   159 FMDSLHILVQQ---GKVLYLGVSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVM 235
Cdd:PRK10625 157 LLETLDALAEQqraGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   236 GGGRFQSK---KAMEERRKNGEGIRSFVGASEQTDAEIKiseALAKIAEEHGTESvTAIAIAYVRSKAknFFPSVEGG-- 310
Cdd:PRK10625 237 AFGTLTGKylnGAKPAGARNTLFSRFTRYSGEQTQKAVA---AYVDIAKRHGLDP-AQMALAFVRRQP--FVASTLLGat 310
                        330       340
                 ....*....|....*....|....*..
gi 6319951   311 KIEDLKENIKALSIDLTPDNIKYLESI 337
Cdd:PRK10625 311 TMEQLKTNIESLHLTLSEEVLAEIEAV 337
 
Name Accession Description Interval E-value
AKR_AKR9A3_9B1-4 cd19147
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ...
17-335 0e+00

Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.


Pssm-ID: 381373 [Multi-domain]  Cd Length: 319  Bit Score: 639.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   17 FLSETAAIKVSPLILGEVSYDGARSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRLRDQIV 96
Cdd:cd19147   1 VLSKTAGIRVSPLILGAMSIGDAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRDQIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   97 IATKFIKSDKKYKAGESNTANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLG 176
Cdd:cd19147  81 IATKFTTDYKAYEVGKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  177 VSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGI 256
Cdd:cd19147 161 VSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKKAVEERKKNGEGL 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319951  257 RSFVGASEQTDAEIKISEALAKIAEEHGTESVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19147 241 RSFVGGTEQTPEEVKISEALEKVAEEHGTESVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYLE 319
AKR_AKR9A1-2 cd19146
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ...
16-349 5.21e-158

Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.


Pssm-ID: 381372 [Multi-domain]  Cd Length: 326  Bit Score: 446.10  E-value: 5.21e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   16 RFLSETAAIKVSPLILGEVSYDGARSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRLRDQI 95
Cdd:cd19146   1 RQLSPTAGVRVSPLCLGAMSFGEAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNRDEM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   96 VIATKFIKSdkkYKAGESN--TANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVL 173
Cdd:cd19146  81 VLATKYTTG---YRRGGPIkiKSNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  174 YLGVSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSkkamEERRKNG 253
Cdd:cd19146 158 YLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQFRT----EEEFKRR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  254 EGIRSFVGAseQTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKY 333
Cdd:cd19146 234 GRSGRKGGP--QTEKERKVSEKLEKVAEEKGT-AITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQE 310
                       330
                ....*....|....*.
gi 6319951  334 LESIVPFDIGFPNNFI 349
Cdd:cd19146 311 IEDAYPFDVGFPMNFL 326
AKR_AKR9A_9B cd19080
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ...
17-335 2.38e-157

AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.


Pssm-ID: 381306 [Multi-domain]  Cd Length: 307  Bit Score: 443.58  E-value: 2.38e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   17 FLSETAAIKVSPLILGEVSYDGARSdflKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlrDQIV 96
Cdd:cd19080   1 RLLGRSGLRVSPLALGTMTFGTEWG---WGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNR--DRIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   97 IATKFIKSDKKykagesNTANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLG 176
Cdd:cd19080  76 LATKYTMNRRP------GDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  177 VSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGI 256
Cdd:cd19080 150 ISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAK 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319951  257 RSFVGASEQTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19080 230 GVTVGFGKLTERNWAIVDVVAAVAEELGR-SAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
24-339 1.50e-72

Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440431 [Multi-domain]  Cd Length: 316  Bit Score: 228.14  E-value: 1.50e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   24 IKVSPLILGEVSYdgarSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlRDQIVIATKFIk 103
Cdd:COG0667  11 LKVSRLGLGTMTF----GGPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRP-RDDVVIATKVG- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  104 sdkkYKAGESntANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAW 183
Cdd:COG0667  85 ----RRMGPG--PNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  184 VVSAANyyATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGIRSFVGAS 263
Cdd:COG0667 159 QLRRAL--AIAEGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRAATNFVQG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  264 EQTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKaknffPSVEG-----GKIEDLKENIKALSIDLTPDNIKYLESIV 338
Cdd:COG0667 237 YLTERNLALVDALRAIAAEHGV-TPAQLALAWLLAQ-----PGVTSvipgaRSPEQLEENLAAADLELSAEDLAALDAAL 310

                .
gi 6319951  339 P 339
Cdd:COG0667 311 A 311
AKR_EcYajO-like cd19079
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ...
24-335 9.86e-72

Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.


Pssm-ID: 381305 [Multi-domain]  Cd Length: 312  Bit Score: 225.93  E-value: 9.86e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   24 IKVSPLILGEVSYdGARSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRLRDQIVIATKFik 103
Cdd:cd19079  10 LKVSRLCLGCMSF-GDPKWRPWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFAPRDEVVIATKV-- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  104 sdkkyKAGESNTANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAW 183
Cdd:cd19079  87 -----YFPMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAW 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  184 VVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGIRSFVGAS 263
Cdd:cd19079 162 QFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDTAKLKYD 241
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319951  264 EQTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19079 242 YFTEADKEIVDRVEEVAKERGV-SMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
46-338 2.25e-70

Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.


Pssm-ID: 425554 [Multi-domain]  Cd Length: 290  Bit Score: 221.80  E-value: 2.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951     46 SMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRL-RDQIVIATKFIKSDKKYKAGesntanycgNHKR 124
Cdd:pfam00248  14 PISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVkRDKVVIATKVPDGDGPWPSG---------GSKE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    125 SLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSaanyYATSYGKTPFSIYQ 204
Cdd:pfam00248  85 NIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIE----KALTKGKIPIVAVQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    205 GKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGIRSFVgasEQTDAEIKISEALAKIAEEHG 284
Cdd:pfam00248 161 VEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLK---KGTPLNLEALEALEEIAKEHG 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6319951    285 tESVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLESIV 338
Cdd:pfam00248 238 -VSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
AKR_SF cd06660
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ...
27-320 5.94e-68

Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.


Pssm-ID: 381296 [Multi-domain]  Cd Length: 232  Bit Score: 213.53  E-value: 5.94e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   27 SPLILGEVSYDGARSDflksmnkNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRLRDQIVIATKFIKSDK 106
Cdd:cd06660   1 SRLGLGTMTFGGDGDE-------EEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRDDVVIATKGGHPPG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  107 kykagesNTANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVS 186
Cdd:cd06660  74 -------GDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  187 AANYYATSYGKTPFSIYQGKWNVLNRDF-ERDIIPMARHFGMALAPWDVMGGGrfqskkameerrkngegirsfvgaseq 265
Cdd:cd06660 147 EALAYAKAHGLPGFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG--------------------------- 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6319951  266 tdaeikisealakiaeehgtesVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIK 320
Cdd:cd06660 200 ----------------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
AKR_AKR9C1 cd19081
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ...
24-334 1.30e-66

AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).


Pssm-ID: 381307 [Multi-domain]  Cd Length: 308  Bit Score: 212.84  E-value: 1.30e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   24 IKVSPLILGEvsydgarSDFLKSMNKNRAFELLDTFYEAGGNFIDAAN-------NCQNEQSEEWIGEWIQSRRLRDQIV 96
Cdd:cd19081   7 LSVSPLCLGT-------MVFGWTADEETSFALLDAFVDAGGNFIDTADvysawvpGNAGGESETIIGRWLKSRGKRDRVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   97 IATKfiksdkkykAGESNTANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLG 176
Cdd:cd19081  80 IATK---------VGFPMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  177 VSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRD-FERDIIPMARHFGMALAPWDVMGG----GRFQSKKAMEERRK 251
Cdd:cd19081 151 ASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGgfltGKYRSEADLPGSTR 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  252 NGEGIRSFVgaseqTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNI 331
Cdd:cd19081 231 RGEAAKRYL-----NERGLRILDALDEVAAEHGA-TPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLTDEEV 304

                ...
gi 6319951  332 KYL 334
Cdd:cd19081 305 ARL 307
AKR_AKR12A1_B1_C1 cd19087
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ...
16-339 6.55e-63

AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.


Pssm-ID: 381313 [Multi-domain]  Cd Length: 310  Bit Score: 203.19  E-value: 6.55e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   16 RFLSETAaIKVSPLILGEVSYdGARSDflksmnKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlrDQI 95
Cdd:cd19087   4 RTLGRTG-LKVSRLCLGTMNF-GGRTD------EETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRR--DDI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   96 VIATKFIksdkkYKAGESNTANycGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYL 175
Cdd:cd19087  74 VLATKVF-----GPMGDDPNDR--GLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  176 GVSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEG 255
Cdd:cd19087 147 GVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  256 IRSFVG-ASEQTDAEIKISEALAKIAEEHGtESVTAIAIAYVRSKaknffPSVEG---G--KIEDLKENIKALSIDLTPD 329
Cdd:cd19087 227 VERARYqARYGLEEYRDIAERFEALAAEAG-LTPASLALAWVLSH-----PAVTSpiiGprTLEQLEDSLAALEITLTPE 300
                       330
                ....*....|
gi 6319951  330 NIKYLESIVP 339
Cdd:cd19087 301 LLAEIDELFP 310
AKR_PsAKR cd19091
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ...
14-337 1.27e-62

Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.


Pssm-ID: 381317 [Multi-domain]  Cd Length: 319  Bit Score: 202.84  E-value: 1.27e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   14 RLRFLSETAaIKVSPLILGEVSYDGARSDFLK--SMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRl 91
Cdd:cd19091   2 EYRTLGRSG-LKVSELALGTMTFGGGGGFFGAwgGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRR- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   92 rDQIVIATKFiksdkKYKAGESntANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGK 171
Cdd:cd19091  80 -DDVLIATKV-----RGRMGEG--PNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  172 VLYLGVSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRK 251
Cdd:cd19091 152 VRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPAP 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  252 NGEGIRSFVGASEQTDAE--IKISEALAKIAEEHGTeSVTAIAIAYVRSKAknFFPSVEGG--KIEDLKENIKALSIDLT 327
Cdd:cd19091 232 EGSRLRRTGFDFPPVDRErgYDVVDALREIAKETGA-TPAQVALAWLLSRP--TVSSVIIGarNEEQLEDNLGAAGLSLT 308
                       330
                ....*....|
gi 6319951  328 PDNIKYLESI 337
Cdd:cd19091 309 PEEIARLDKV 318
AKR_AKR10A1_2 cd19082
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ...
27-323 2.73e-50

AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.


Pssm-ID: 381308 [Multi-domain]  Cd Length: 291  Bit Score: 170.04  E-value: 2.73e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   27 SPLILGevsydgaRSDFLKSMNKNRAFELLDTFYEAGGNFIDAA----NNCQNEQSEEWIGEWIQSRRLRDQIVIATKfi 102
Cdd:cd19082   1 SRIVLG-------TADFGTRIDEEEAFALLDAFVELGGNFIDTArvygDWVERGASERVIGEWLKSRGNRDKVVIATK-- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  103 ksdkkykaG-----ESNTANYCgnHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGV 177
Cdd:cd19082  72 --------GghpdlEDMSRSRL--SPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  178 SDtpaWV---VSAANYYATSYGKTPFSIYQGKWN--VLNRDFERD--IIPM---ARHF----GMALAPWDVMGGGRFqSK 243
Cdd:cd19082 142 SN---WSterIAEANAYAKAHGLPGFAASSPQWSlaRPNEPPWPGptLVAMdeeMRAWheenQLPVFAYSSQARGFF-SK 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  244 KAMEERRKNGEGIRSFvgaseQTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALS 323
Cdd:cd19082 218 RAAGGAEDDSELRRVY-----YSEENFERLERAKELAEEKGV-SPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
AKR_Tas-like cd19094
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ...
47-329 1.35e-45

Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.


Pssm-ID: 381320 [Multi-domain]  Cd Length: 328  Bit Score: 158.88  E-value: 1.35e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   47 MNKNRAFELLDTFYEAGGNFIDAAnncqnEQ------------SEEWIGEWIQSRRLRDQIVIATKFiksdkkykAGESN 114
Cdd:cd19094  15 NTEAEAHEQLDYAFDEGVNFIDTA-----EMypvppspetqgrTEEIIGSWLKKKGNRDKVVLATKV--------AGPGE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  115 TANYCGNHKRSL---HV--SVRDSLRKLQTDWIDILYVHWWD-----------------YMS-SIEEFMDSLHILVQQGK 171
Cdd:cd19094  82 GITWPRGGGTRLdreNIreAVEGSLKRLGTDYIDLYQLHWPDrytplfgggyytepseeEDSvSFEEQLEALGELVKAGK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  172 VLYLGVSDTPAWVVSAANYYATSYGKTPF-SIyQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERR 250
Cdd:cd19094 162 IRHIGLSNETPWGVMKFLELAEQLGLPRIvSI-QNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGG-VLTGKYLDGAA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  251 KNGEGIRS-FVG-----ASEQTDAEIKiseALAKIAEEHGTeSVTAIAIAYVRSKAknFFPSVEGG--KIEDLKENIKAL 322
Cdd:cd19094 240 RPEGGRLNlFPGymaryRSPQALEAVA---EYVKLARKHGL-SPAQLALAWVRSRP--FVTSTIIGatTLEQLKENIDAF 313

                ....*..
gi 6319951  323 SIDLTPD 329
Cdd:cd19094 314 DVPLSDE 320
AKR_AKR11B1-like cd19084
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ...
24-335 1.77e-45

AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.


Pssm-ID: 381310 [Multi-domain]  Cd Length: 296  Bit Score: 157.30  E-value: 1.77e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   24 IKVSPLILGEVSYDGARSDflkSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlrDQIVIATKF-I 102
Cdd:cd19084   2 LKVSRIGLGTWAIGGTWWG---EVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRR--DDVVIATKCgL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  103 KSDKKYKAGESNTANYcgnhkrsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPA 182
Cdd:cd19084  77 RWDGGKGVTKDLSPES-------IRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  183 WVVSAANYYAtsygktPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGG----RFQSK---KAMEERRKNgeg 255
Cdd:cd19084 150 EQLEEARKYG------PIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGlltgKYKKEptfPPDDRRSRF--- 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  256 iRSFVGasEQTDAEIKISEALAKIAEEHGtESVTAIAIAYVRSK---------AKNffpsveggkIEDLKENIKALSIDL 326
Cdd:cd19084 221 -PFFRG--ENFEKNLEIVDKLKEIAEKYG-KSLAQLAIAWTLAQpgvtsaivgAKN---------PEQLEENAGALDWEL 287

                ....*....
gi 6319951  327 TPDNIKYLE 335
Cdd:cd19084 288 TEEELKEID 296
Aldo_ket_red_shaker-like cd19074
Shaker potassium channel beta subunit family and similar proteins; This family includes ...
29-329 8.01e-40

Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.


Pssm-ID: 381300 [Multi-domain]  Cd Length: 297  Bit Score: 142.73  E-value: 8.01e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   29 LILGEVSYDGARSdFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlRDQIVIATK--FIKSDK 106
Cdd:cd19074   2 LKVSELSLGTWLT-FGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWP-RESYVISTKvfWPTGPG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  107 KYKAGESntanycgnhKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVS 186
Cdd:cd19074  80 PNDRGLS---------RKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  187 AANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGG----RFQSKKAMEER-RKNGEGIRSFVG 261
Cdd:cd19074 151 EAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGlltgKYRDGIPPPSRsRATDEDNRDKKR 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6319951  262 aSEQTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPD 329
Cdd:cd19074 231 -RLLTDENLEKVKKLKPIADELGL-TLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSPE 296
AKR_AKR13A_13D cd19076
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ...
21-334 8.07e-37

AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.


Pssm-ID: 381302 [Multi-domain]  Cd Length: 303  Bit Score: 135.04  E-value: 8.07e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   21 TAAIKVSPLILGEVSYdgarSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIqsRRLRDQIVIATK 100
Cdd:cd19076   7 TQGLEVSALGLGCMGM----SAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKAL--KDRRDEVVIATK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  101 F--IKSDKKYKAGESNTANYCgnhkRSlhvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVS 178
Cdd:cd19076  81 FgiVRDPGSGFRGVDGRPEYV----RA---ACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  179 D-TPAWVVSAANYYatsygktPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMG----GGRFQSKKAMEE---RR 250
Cdd:cd19076 154 EaSADTIRRAHAVH-------PITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGrgflTGAIKSPEDLPEddfRR 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  251 KNGEgirsFVGasEQTDAEIKISEALAKIAEEHGtesVTA--IAIAYVRSKAKNFFPsVEGGK-IEDLKENIKALSIDLT 327
Cdd:cd19076 227 NNPR----FQG--ENFDKNLKLVEKLEAIAAEKG---CTPaqLALAWVLAQGDDIVP-IPGTKrIKYLEENVGALDVVLT 296

                ....*..
gi 6319951  328 PDNIKYL 334
Cdd:cd19076 297 PEELAEI 303
AKR_unchar cd19752
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
27-323 2.41e-36

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381391 [Multi-domain]  Cd Length: 291  Bit Score: 133.23  E-value: 2.41e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   27 SPLILGEVsYDGARSDflksmnKNRAFELLDTFYEAGGNFIDAANN-------CQNEQSEEWIGEWIQSRRLRDQIVIAT 99
Cdd:cd19752   1 SELCLGTM-YFGTRTD------EETSFAILDRYVAAGGNFLDTANNyafwtegGVGGESERLIGRWLKDRGNRDDVVIAT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  100 KFiksDKKYKAGESNTANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSD 179
Cdd:cd19752  74 KV---GAGPRDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASN 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  180 TPAWVVSAANYYATSYGKTPFSIYQGKWNVL----NRDF------ERDIIPMAR-HFGMALAPWDVMGGGRFqSKKAMEE 248
Cdd:cd19752 151 FAAWRLERARQIARQQGWAEFSAIQQRHSYLrprpGADFgvqrivTDELLDYASsRPDLTLLAYSPLLSGAY-TRPDRPL 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6319951  249 RrkngegirsfvGASEQTDAEIKISeALAKIAEEHGtesVTA--IAIAYVRSKAKNFFPSVEGGKIEDLKENIKALS 323
Cdd:cd19752 230 P-----------EQYDGPDSDARLA-VLEEVAGELG---ATPnqVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
AKR_AKR11B3 cd19085
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ...
56-337 1.50e-34

Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.


Pssm-ID: 381311 [Multi-domain]  Cd Length: 292  Bit Score: 128.47  E-value: 1.50e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   56 LDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlrDQIVIATKFiksdkkykagesntaNYCGNHKRSLHVSVRDSLR 135
Cdd:cd19085  29 IHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRR--DDVVIATKV---------------SPDNLTPEDVRKSCERSLK 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  136 KLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYyatsygkTPFSIYQGKWNVLNRDF 214
Cdd:cd19085  92 RLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNfGPAQLEEALDA-------GRIDSNQLPYNLLWRAI 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  215 ERDIIPMARHFGMALAPWDVMG----GGRFQSKKAMEERRKNGEGIRSFvgaseQTDAEIKISEALAK---IAEEHGTeS 287
Cdd:cd19085 165 EYEILPFCREHGIGVLAYSPLAqgllTGKFSSAEDFPPGDARTRLFRHF-----EPGAEEETFEALEKlkeIADELGV-T 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 6319951  288 VTAIAIAYVRSkaKNFFPSVEGG--KIEDLKENIKALSIDLTPDNIKYLESI 337
Cdd:cd19085 239 MAQLALAWVLQ--QPGVTSVIVGarNPEQLEENAAAVDLELSPSVLERLDEI 288
AKR_AKR11B2 cd19149
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ...
11-336 2.45e-33

Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.


Pssm-ID: 381375 [Multi-domain]  Cd Length: 315  Bit Score: 125.85  E-value: 2.45e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   11 KLGRlrflsetAAIKVSPLILGEVSYDGArsDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIqsRR 90
Cdd:cd19149   3 KLGK-------SGIEASVIGLGTWAIGGG--PWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAI--KG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   91 LRDQIVIATKF-----IKSDKKYKAGESNTANYCGNhKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHI 165
Cdd:cd19149  72 RRDKVVLATKCglrwdREGGSFFFVRDGVTVYKNLS-PESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  166 LVQQGKVLYLGVSDTPAWVVSAanyyATSYGktPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKA 245
Cdd:cd19149 151 LKRQGKIRAIGASNVSVEQIKE----YVKAG--QLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQG-LLTGKI 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  246 MEERRKNGEGIRS----FVGASEQTDAEIKisEALAKIAEEHGTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKA 321
Cdd:cd19149 224 TPDREFDAGDARSgipwFSPENREKVLALL--EKWKPLCEKYGC-TLAQLVIAWTLAQPGITSALCGARKPEQAEENAKA 300
                       330
                ....*....|....*
gi 6319951  322 LSIDLTPDNIKYLES 336
Cdd:cd19149 301 GDIRLSAEDIATMRS 315
AKR_AKR6C1_2 cd19143
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ...
16-337 4.47e-31

AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.


Pssm-ID: 381369 [Multi-domain]  Cd Length: 319  Bit Score: 120.01  E-value: 4.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   16 RFLSETAaIKVSPLilgevSYdGARSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIqsRRL---R 92
Cdd:cd19143   4 RRLGRSG-LKVSAL-----SF-GSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAI--KELgwpR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   93 DQIVIATKFiksdkkYKAGESNTANYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKV 172
Cdd:cd19143  75 SDYVVSTKI------FWGGGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  173 LYLGVSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRD-FERDIIPMARHFGMALAPWDVMGGGRFQSK---KAMEE 248
Cdd:cd19143 149 FYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKynnGIPEG 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  249 RR---KNGEGIRSFVgaSEQTDAEIKISEALAKIAEEHGTeSVTAIAIAYVrskAKNffPSVE-----GGKIEDLKENIK 320
Cdd:cd19143 229 SRlalPGYEWLKDRK--EELGQEKIEKVRKLKPIAEELGC-SLAQLAIAWC---LKN--PNVStvitgATKVEQLEENLK 300
                       330
                ....*....|....*....
gi 6319951  321 ALSI--DLTPDNIKYLESI 337
Cdd:cd19143 301 ALEVlpKLTPEVMEKIEAI 319
AKR_AKR13D1 cd19145
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ...
52-334 1.16e-30

AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.


Pssm-ID: 381371 [Multi-domain]  Cd Length: 304  Bit Score: 118.30  E-value: 1.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   52 AFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlRDQIVIATKF-IKSDKKYKAGESNTANYcgnhkrslhvsV 130
Cdd:cd19145  35 GIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGP-REKVQLATKFgIHEIGGSGVEVRGDPAY-----------V 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  131 R----DSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAAnyyatsYGKTPFSIYQGK 206
Cdd:cd19145 103 RaaceASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRA------HAVHPITAVQLE 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  207 WNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGIRS---FVGasEQTDAEIKISEALAKIAEEH 283
Cdd:cd19145 177 WSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRKShprFQG--ENLEKNKVLYERVEALAKKK 254
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6319951  284 GTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYL 334
Cdd:cd19145 255 GC-TPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
AKR_AKR11A1_11D1 cd19083
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ...
11-338 7.55e-30

AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).


Pssm-ID: 381309 [Multi-domain]  Cd Length: 307  Bit Score: 116.36  E-value: 7.55e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   11 KLGRlrflsetAAIKVSPLILGEVSYDGarSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRR 90
Cdd:cd19083   3 KLGK-------SDIDVNPIGLGTNAVGG--HNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   91 lRDQIVIATKFIKSDKKYKAGESNTANYcgnhkrsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQG 170
Cdd:cd19083  74 -RNEVVIATKGAHKFGGDGSVLNNSPEF-------LRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  171 KVLYLGVSDTPAWVVSAANyyATSYgktpFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERR 250
Cdd:cd19083 146 KIRAIGVSNFSLEQLKEAN--KDGY----VDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASG-LLAGKYTKDTK 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  251 KNGEGIRSFVG--ASEQTDAEIKISEALAKIAEEHGTEsVTAIAIAYVRSKaknffPSVE----GGK-IEDLKENIKALS 323
Cdd:cd19083 219 FPDNDLRNDKPlfKGERFSENLDKVDKLKSIADEKGVT-VAHLALAWYLTR-----PAIDvvipGAKrAEQVIDNLKALD 292
                       330
                ....*....|....*
gi 6319951  324 IDLTPDNIKYLESIV 338
Cdd:cd19083 293 VTLTEEEIAFIDALF 307
AKR_AKR3F1-like cd19072
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ...
24-335 3.09e-29

Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381298 [Multi-domain]  Cd Length: 263  Bit Score: 113.48  E-value: 3.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   24 IKVSPLILGeVSYDGARSDFLKSmNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIqSRRLRDQIVIATKFIK 103
Cdd:cd19072   2 EEVPVLGLG-TWGIGGGMSKDYS-DDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI-KGFDREDLFITTKVSP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  104 SDKKYKAgesntanycgnhkrsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAW 183
Cdd:cd19072  79 DHLKYDD---------------VIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLE 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  184 VVSAANYYAtsyGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAmeerrkngegirsfvgas 263
Cdd:cd19072 144 ELEEAQSYL---KKGPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG------------------ 202
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319951  264 eqtdaeikiSEALAKIAEEHGtESVTAIAIAYVRSKaKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19072 203 ---------SPLLDEIAKKYG-KTPAQIALNWLISK-PNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
AKR_AKR13C1_2 cd19078
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ...
23-336 3.84e-29

AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.


Pssm-ID: 381304 [Multi-domain]  Cd Length: 301  Bit Score: 114.25  E-value: 3.84e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   23 AIKVSPLILGEVSYDGARSDFlksMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlrDQIVIATKF- 101
Cdd:cd19078   1 GLEVSAIGLGCMGMSHGYGPP---PDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFR--DQVVIATKFg 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  102 --IKSDKKYKAGESNTANycgnHKRSlhvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSD 179
Cdd:cd19078  76 fkIDGGKPGPLGLDSRPE----HIRK---AVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSE 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  180 TpawvvsAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERRKNGEGIRSF 259
Cdd:cd19078 149 A------GVETIRRAHAVCPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKG-FLTGKIDENTKFDEGDDRAS 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319951  260 VG--ASEQTDAEIKISEALAKIAEEHGTESVtAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLES 336
Cdd:cd19078 222 LPrfTPEALEANQALVDLLKEFAEEKGATPA-QIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIED 299
AKR_AtPLR-like cd19093
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ...
25-335 7.92e-29

Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.


Pssm-ID: 381319 [Multi-domain]  Cd Length: 293  Bit Score: 113.09  E-value: 7.92e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   25 KVSPLILGEVSYDGARSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRLRDQIVIATKFiks 104
Cdd:cd19093   1 EVSPLGLGTWQWGDRLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRDEVVIATKF--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  105 dkkykAGESNTANycgnhKRSLHVSVRDSLRKLQTDWIDILYVHW-WDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAW 183
Cdd:cd19093  78 -----APLPWRLT-----RRSVVKALKASLERLGLDSIDLYQLHWpGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSAD 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  184 VVSAANYYATSYGKTPFSIyQGKWNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGIRSFVGA 262
Cdd:cd19093 148 QLRRAHKALKERGVPLASN-QVEYSLLYRDPEQNgLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKN 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  263 SEQTDAeikISEALAKIAEEHGtESVTAIAIAYVRSK-------AKNffpsveggkIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19093 227 LEKVQP---LLDALEEIAEKYG-KTPAQVALNWLIAKgvvpipgAKN---------AEQAEENAGALGWRLSEEEVAELD 293
AKR_BsYcsN_EcYdhF-like cd19092
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ...
23-327 5.93e-28

Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.


Pssm-ID: 381318 [Multi-domain]  Cd Length: 287  Bit Score: 110.72  E-value: 5.93e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   23 AIKVSPLILGevsydgarsdFLKSMNKN----RAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRR-LRDQIVI 97
Cdd:cd19092   3 GLEVSRLVLG----------CMRLADWGesaeELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPgLREKIEI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   98 ATKF-IKSDKKYKAGESNTANYCGNHKRSlhvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLG 176
Cdd:cd19092  73 QTKCgIRLGDDPRPGRIKHYDTSKEHILA---SVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  177 VSDTPAWVVSAANyyatSYGKTPFSIYQGKWNVLNRDF----------ERDIIPMArhfgmalapWDVMGGGRFqskkam 246
Cdd:cd19092 150 VSNFTPSQIELLQ----SYLDQPLVTNQIELSLLHTEAiddgtldycqLLDITPMA---------WSPLGGGRL------ 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  247 eerrkngegirsfvgASEQTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDL 326
Cdd:cd19092 211 ---------------FGGFDERFQRLRAALEELAEEYGV-TIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIEL 274

                .
gi 6319951  327 T 327
Cdd:cd19092 275 T 275
AKR_AKR13A1 cd19144
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ...
35-338 1.22e-26

AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.


Pssm-ID: 381370 [Multi-domain]  Cd Length: 323  Bit Score: 107.91  E-value: 1.22e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   35 SYDGARSDflksmnkNRAFELLDTFYEAGGNFIDAANNCQNeqSEEWIGEWI-QSRRLRDQIVIATKF-IKSDKKYKAGE 112
Cdd:cd19144  26 FYGPPKPD-------EERFAVLDAAFELGCTFWDTADIYGD--SEELIGRWFkQNPGKREKIFLATKFgIEKNVETGEYS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  113 -SNTANYCGNhkrslhvSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAAnyy 191
Cdd:cd19144  97 vDGSPEYVKK-------ACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRA--- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  192 atsYGKTPFSIYQGKWNVLNRDFER---DIIPMARHFGMALAPWDVMG----GGRFQSKKAMEE---RRKNGEgirsFvg 261
Cdd:cd19144 167 ---HAVHPIAAVQIEYSPFSLDIERpeiGVLDTCRELGVAIVAYSPLGrgflTGAIRSPDDFEEgdfRRMAPR----F-- 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319951  262 ASEQTDAEIKISEALAKIAEEHGtesVTA--IAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLESIV 338
Cdd:cd19144 238 QAENFPKNLELVDKIKAIAKKKN---VTAgqLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIA 313
YdhF COG4989
Predicted oxidoreductase YdhF [General function prediction only];
24-327 3.40e-26

Predicted oxidoreductase YdhF [General function prediction only];


Pssm-ID: 444013 [Multi-domain]  Cd Length: 299  Bit Score: 106.00  E-value: 3.40e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   24 IKVSPLILGEVSYDGARsdflksMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRR-LRDQIVIATKFi 102
Cdd:COG4989  11 LSVSRIVLGCMRLGEWD------LSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPsLREKIELQTKC- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  103 ksDKKYKAGESNTA----NYCGNHkrsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVS 178
Cdd:COG4989  84 --GIRLPSEARDNRvkhyDTSKEH---IIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  179 DTPAWVVSAANyyatSYGKTPFSIYQGKWNVLNRD-FERDIIPMARHFGMALAPWDVMGGGRFqskkameerrkngegir 257
Cdd:COG4989 159 NFTPSQFELLQ----SALDQPLVTNQIELSLLHTDaFDDGTLDYCQLNGITPMAWSPLAGGRL----------------- 217
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  258 sfvgASEQTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLT 327
Cdd:COG4989 218 ----FGGFDEQFPRLRAALDELAEKYGV-SPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELT 282
AKR_AKR14A1_2 cd19089
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ...
52-332 3.67e-26

AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.


Pssm-ID: 381315 [Multi-domain]  Cd Length: 308  Bit Score: 106.19  E-value: 3.67e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   52 AFELLDTFYEAGGNFIDAANNC-QNEQS-EEWIGEWIQS--RRLRDQIVIATK--FIKSDKKYKAGESntanycgnhKRS 125
Cdd:cd19089  31 ARELLRTAFDLGITHFDLANNYgPPPGSaEENFGRILKRdlRPYRDELVISTKagYGMWPGPYGDGGS---------RKY 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  126 LHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSYGkTPFSIYQG 205
Cdd:cd19089 102 LLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQP 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  206 KWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSK-----KAMEERRKNGegirSFVGASEQTDAEIKISEALAKIA 280
Cdd:cd19089 181 RYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKylngiPPDSRRAAES----KFLTEEALTPEKLEQLRKLNKIA 256
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 6319951  281 EEHGtESVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKAL-SIDLTPDNIK 332
Cdd:cd19089 257 AKRG-QSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALkNLDFSEEELA 308
AKR_AKR7A1-5 cd19075
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ...
54-323 1.08e-25

AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.


Pssm-ID: 381301 [Multi-domain]  Cd Length: 304  Bit Score: 104.95  E-value: 1.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   54 ELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlrdQIVIATKFiksdkkykagesNTANYCGNHKRSLHVSVRDS 133
Cdd:cd19075  24 ELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGER---GFKIDTKA------------NPGVGGGLSPENVRKQLETS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  134 LRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRD 213
Cdd:cd19075  89 LKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITRQ 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  214 FERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERRKNGEG---IRSFVGASEQT----DAEIKISEALAKIAEEHGtE 286
Cdd:cd19075 169 VETELFPCLRKLGIRFYAYSPLAGG-FLTGKYKYSEDKAGGGrfdPNNALGKLYRDrywkPSYFEALEKVEEAAEKEG-I 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 6319951  287 SVTAIAIAYVR--SKAKnffpsVEGG--------KIEDLKENIKALS 323
Cdd:cd19075 247 SLAEAALRWLYhhSALD-----GEKGdgvilgasSLEQLEENLAALE 288
AKR_AKR11C1 cd19086
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ...
41-229 2.59e-24

AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.


Pssm-ID: 381312 [Multi-domain]  Cd Length: 238  Bit Score: 99.47  E-value: 2.59e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   41 SDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRrlRDQIVIATKFIKSDKKYKAGESNTAnycg 120
Cdd:cd19086  15 GDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGR--RDKVVIATKFGNRFDGGPERPQDFS---- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  121 nhKRSLHVSVRDSLRKLQTDWIDILYVH-WWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAANyyatSYGKtp 199
Cdd:cd19086  89 --PEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAAL----RRGG-- 160
                       170       180       190
                ....*....|....*....|....*....|
gi 6319951  200 FSIYQGKWNVLNRDFERDIIPMARHFGMAL 229
Cdd:cd19086 161 IDVVQVIYNLLDQRPEEELFPLAEEHGVGV 190
AKR_unchar cd19102
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
60-338 2.82e-24

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381328 [Multi-domain]  Cd Length: 302  Bit Score: 100.83  E-value: 2.82e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   60 YEAGGNFIDAANNCQNEQSEEWIGEWIqsRRLRDQIVIATKF-IKSDKKYKAGESNTANycgnhkrSLHVSVRDSLRKLQ 138
Cdd:cd19102  36 LDLGINWIDTAAVYGLGHSEEVVGRAL--KGLRDRPIVATKCgLLWDEEGRIRRSLKPA-------SIRAECEASLRRLG 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  139 TDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYAT-SYGKTPFSIyqgkwnvLNRDFERD 217
Cdd:cd19102 107 VDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPiASLQPPYSL-------LRRGIEAE 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  218 IIPMARHFGMALAPWDVMGGGRFqSKKAMEERRK----NGEGIRSFVGASEQTDAEIKISEALAKIAEEHGTeSVTAIAI 293
Cdd:cd19102 180 ILPFCAEHGIGVIVYSPMQSGLL-TGKMTPERVAslpaDDWRRRSPFFQEPNLARNLALVDALRPIAERHGR-TVAQLAI 257
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 6319951  294 AYVRSKaknffPSVEGG-----KIEDLKENIKALSIDLTPDNIKYLESIV 338
Cdd:cd19102 258 AWVLRR-----PEVTSAivgarRPDQIDETVGAADLRLTPEELAEIEALL 302
AKR_unchar cd19105
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
24-251 3.25e-24

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381331 [Multi-domain]  Cd Length: 250  Bit Score: 99.58  E-value: 3.25e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   24 IKVSPLILGEVSYDGARSDFLKsmnknRAfelldtfYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlRDQIVIATKFIK 103
Cdd:cd19105  11 LKVSRLGFGGGGLPRESPELLR-----RA-------LDLGINYFDTAEGYGNGNSEEIIGEALKGLR-RDKVFLATKASP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  104 SDKKYKAGEsntanycgnhkrsLHVSVRDSLRKLQTDWIDILYVHWWDYMSSI---EEFMDSLHILVQQGKVLYLGVS-- 178
Cdd:cd19105  78 RLDKKDKAE-------------LLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFSth 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319951  179 DTPAWVVSAAnyyATSYgktPFSIYQGKWNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSKKAMEERRK 251
Cdd:cd19105 145 DNMAEVLQAA---IESG---WFDVIMVAYNFLNQPAELEeALAAAAEKGIGVVAMKTLAGGYLQPALLSVLKAK 212
AKR_AKR11B1 cd19148
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ...
61-296 1.70e-22

Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381374 [Multi-domain]  Cd Length: 302  Bit Score: 95.84  E-value: 1.70e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEQSEEWIGEWIQSRRLRDQIVIATKF--IKSDKKYKAGESNTANycgnhkrsLHVSVRDSLRKLQ 138
Cdd:cd19148  36 DLGINLIDTAPVYGFGLSEEIVGKALKEYGKRDRVVIATKVglEWDEGGEVVRNSSPAR--------IRKEVEDSLRRLQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  139 TDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSdtpawvvsaaNY----YATSYGKTPFSIYQGKWNVLNRDF 214
Cdd:cd19148 108 TDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVS----------NFspeqMETFRKVAPLHTVQPPYNLFEREI 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  215 ERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEERRKNGEGIRSFVG--ASEQTDAEIKISEALAKIAEEHGTESVTAIA 292
Cdd:cd19148 178 EKDVLPYARKHNIVTLAYGALCRG-LLSGKMTKDTKFEGDDLRRTDPkfQEPRFSQYLAAVEELDKLAQERYGKSVIHLA 256

                ....
gi 6319951  293 IAYV 296
Cdd:cd19148 257 VRWL 260
AKR_unchar cd19100
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
24-247 6.10e-21

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381326 [Multi-domain]  Cd Length: 238  Bit Score: 90.23  E-value: 6.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   24 IKVSPLILGevsydGARsdfLKSMNKNRAFELLDTFYEAGGNFIDAANNcqNEQSEEWIGEWIQSRRlrDQIVIATKFIK 103
Cdd:cd19100   9 LKVSRLGFG-----GGP---LGRLSQEEAAAIIRRALDLGINYFDTAPS--YGDSEEKIGKALKGRR--DKVFLATKTGA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  104 SDKKyKAgesntanycgnhKRSLHvsvrDSLRKLQTDWIDILYVHwwdYMSSIEEF---------MDSLHILVQQGKVLY 174
Cdd:cd19100  77 RDYE-GA------------KRDLE----RSLKRLGTDYIDLYQLH---AVDTEEDLdqvfgpggaLEALLEAKEEGKIRF 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6319951  175 LGVSD-TPAWVVSAANYYatsygktPFSIYQGKWNVL---NRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAME 247
Cdd:cd19100 137 IGISGhSPEVLLRALETG-------EFDVVLFPINPAgdhIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLD 206
tas PRK10625
putative aldo-keto reductase; Provisional
22-337 1.73e-20

putative aldo-keto reductase; Provisional


Pssm-ID: 236727 [Multi-domain]  Cd Length: 346  Bit Score: 91.07  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    22 AAIKVSPLILGEVSYDGARSDflksmnkNRAFELLDTFYEAGGNFIDAAN--------NCQNeQSEEWIGEWIQSRRLRD 93
Cdd:PRK10625   9 SSLEVSTLGLGTMTFGEQNSE-------ADAHAQLDYAVAQGINLIDVAEmypvpprpETQG-LTETYIGNWLAKRGSRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    94 QIVIATKFIKSDKKYKAG-ESNTANYCGNHKRSLHvsvrDSLRKLQTDWIDILYVHW--------------WDYMSSIEE 158
Cdd:PRK10625  81 KLIIASKVSGPSRNNDKGiRPNQALDRKNIREALH----DSLKRLQTDYLDLYQVHWpqrptncfgklgysWTDSAPAVS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   159 FMDSLHILVQQ---GKVLYLGVSDTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARHFGMALAPWDVM 235
Cdd:PRK10625 157 LLETLDALAEQqraGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   236 GGGRFQSK---KAMEERRKNGEGIRSFVGASEQTDAEIKiseALAKIAEEHGTESvTAIAIAYVRSKAknFFPSVEGG-- 310
Cdd:PRK10625 237 AFGTLTGKylnGAKPAGARNTLFSRFTRYSGEQTQKAVA---AYVDIAKRHGLDP-AQMALAFVRRQP--FVASTLLGat 310
                        330       340
                 ....*....|....*....|....*..
gi 6319951   311 KIEDLKENIKALSIDLTPDNIKYLESI 337
Cdd:PRK10625 311 TMEQLKTNIESLHLTLSEEVLAEIEAV 337
AKR_PA4992-like cd19095
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ...
51-228 5.73e-20

Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381321 [Multi-domain]  Cd Length: 253  Bit Score: 88.06  E-value: 5.73e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   51 RAFELLDTFYEAGGNFIDAANNCQNeqSEEWIGEWIQSRRlRDQIVIATKfiksdkkykAGESNtaNYCGNHKRSL--HV 128
Cdd:cd19095  21 EAARLLNTALDLGINLIDTAPAYGR--SEERLGRALAGLR-RDDLFIATK---------VGTHG--EGGRDRKDFSpaAI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  129 --SVRDSLRKLQTDWIDILYVHwwdyMSSIEEF----MDSLHILVQQGKVLYLGVS-DTPawvvsAANYYATSygkTPFS 201
Cdd:cd19095  87 raSIERSLRRLGTDYIDLLQLH----GPSDDELtgevLETLEDLKAAGKVRYIGVSgDGE-----ELEAAIAS---GVFD 154
                       170       180
                ....*....|....*....|....*..
gi 6319951  202 IYQGKWNVLNRDfERDIIPMARHFGMA 228
Cdd:cd19095 155 VVQLPYNVLDRE-EEELLPLAAEAGLG 180
AKR_YeaE cd19138
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ...
54-335 6.77e-20

Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381364 [Multi-domain]  Cd Length: 266  Bit Score: 88.07  E-value: 6.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   54 ELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlrDQIVIATKFIKSDkkykAGESNTANYCGNhkrslhvsvrdS 133
Cdd:cd19138  33 EALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRR--DKVFLVSKVLPSN----ASRQGTVRACER-----------S 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  134 LRKLQTDWIDILYVHWwdyMSSI--EEFMDSLHILVQQGKVLYLGVS--DTP----AWVVSAANYYATSygktpfsiyQG 205
Cdd:cd19138  96 LRRLGTDYLDLYLLHW---RGGVplAETVAAMEELKKEGKIRAWGVSnfDTDdmeeLWAVPGGGNCAAN---------QV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  206 KWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEerrkngegirsfvgaseqtdaeikiSEALAKIAEEHGT 285
Cdd:cd19138 164 LYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGLLRRGLLE-------------------------NPTLKEIAARHGA 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6319951  286 eSVTAIAIAYV-RSkaKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19138 219 -TPAQVALAWVlRD--GNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
AKR_AKR13B1 cd19088
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ...
47-327 2.67e-19

AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.


Pssm-ID: 381314 [Multi-domain]  Cd Length: 256  Bit Score: 86.12  E-value: 2.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   47 MNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlrDQIVIATK--FIKSDkkykaGESNTANycgNHKR 124
Cdd:cd19088  21 ADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYP--DDVVIATKggLVRTG-----PGWWGPD---GSPE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  125 SLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYyatsygkTPFSIY 203
Cdd:cd19088  91 YLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNvTVAQIEEARAI-------VRIVSV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  204 QGKWNVLNRDFErDIIPMARHFGMALAPWDVMGGGRFqskkameerRKNGegirsfvgaseqtdaeikisEALAKIAEEH 283
Cdd:cd19088 164 QNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDL---------AQPG--------------------GLLAEVAARL 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 6319951  284 GTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLT 327
Cdd:cd19088 214 GA-TPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
AKR_AKR3F1 cd19137
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ...
52-335 2.76e-19

Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.


Pssm-ID: 381363 [Multi-domain]  Cd Length: 260  Bit Score: 86.09  E-value: 2.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   52 AFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlRDQIVIATKFIKSDKKYKagesntanycgnhkrSLHVSVR 131
Cdd:cd19137  28 MVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFP-REDLFIVTKVWPTNLRYD---------------DLLRSLQ 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  132 DSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAanyyATSYGKTPFSIYQGKWNVLN 211
Cdd:cd19137  92 NSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEE----AISKSQTPIVCNQVKYNLED 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  212 RDFERD-IIPMARHFG---MALAPWDvmgggrfqskkameerrkngEGIrsfvgaseqtdaeIKISEALAKIAEEHGtES 287
Cdd:cd19137 168 RDPERDgLLEYCQKNGitvVAYSPLR--------------------RGL-------------EKTNRTLEEIAKNYG-KT 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 6319951  288 VTAIAIAYVRSKaKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19137 214 IAQIALAWLIQK-PNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
AKR_AKR14A2 cd19151
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ...
54-323 5.89e-18

Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).


Pssm-ID: 381377 [Multi-domain]  Cd Length: 309  Bit Score: 83.22  E-value: 5.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   54 ELLDTFYEAGGNFIDAANNCQNE--QSEEWIGEWIQS--RRLRDQIVIATKfiksdkkykAGESNTANYCGNH--KRSLH 127
Cdd:cd19151  34 AMLRRAFDLGITHFDLANNYGPPpgSAEENFGRILKEdlKPYRDELIISTK---------AGYTMWPGPYGDWgsKKYLI 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  128 VSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATSYGkTPFSIYQGKW 207
Cdd:cd19151 105 ASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLG-TPCLIHQPKY 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  208 NVLNRDFERDIIPMARHFGMALAPWDVMGGGRFQSK--KAMEERRKNGEGiRSFVGASEQTDAEIKISEALAKIAEEHGt 285
Cdd:cd19151 184 SMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRylNGIPEDSRAAKG-SSFLKPEQITEEKLAKVRRLNEIAQARG- 261
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 6319951  286 ESVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALS 323
Cdd:cd19151 262 QKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
AKR_AKR15A-like cd19090
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ...
51-329 2.21e-17

AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).


Pssm-ID: 381316 [Multi-domain]  Cd Length: 278  Bit Score: 81.06  E-value: 2.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   51 RAFELLDTFYEAGGNFIDAANNCQNeqSEEWIGEWIQSRRlRDQIVIATKfiksdkkykagesntanyCGNHKR------ 124
Cdd:cd19090  21 EAVATIRAALDLGINYIDTAPAYGD--SEERLGLALAELP-REPLVLSTK------------------VGRLPEdtadys 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  125 --SLHVSVRDSLRKLQTDWIDILYVH------WWDYMsSIEEFMDSLHILVQQGKVLYLGVSDTPAWVvsAANYYATsyG 196
Cdd:cd19090  80 adRVRRSVEESLERLGRDRIDLLMIHdpervpWVDIL-APGGALEALLELKEEGLIKHIGLGGGPPDL--LRRAIET--G 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  197 KTPFSIYQGKWNVLNRDFERDIIPMARHFGMAlapwdVMGGGRFQ----SKKAMEERRKNGEGIrsfvgaseqTDAEIKI 272
Cdd:cd19090 155 DFDVVLTANRYTLLDQSAADELLPAAARHGVG-----VINASPLGmgllAGRPPERVRYTYRWL---------SPELLDR 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319951  273 SEALAKIAEEHGtESVTAIAIAYVRSkaknfFPSVEG-----GKIEDLKENIKALSIDLTPD 329
Cdd:cd19090 221 AKRLYELCDEHG-VPLPALALRFLLR-----DPRISTvlvgaSSPEELEQNVAAAEGPLPEE 276
AKR_AKR3F2_3 cd19073
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ...
60-332 2.76e-16

Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.


Pssm-ID: 381299 [Multi-domain]  Cd Length: 243  Bit Score: 77.31  E-value: 2.76e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   60 YEAGGNFIDAANNCQNEqseEWIGEWIQ-SRRLRDQIVIATKFIKSDKKYKagesntanycgnhkrSLHVSVRDSLRKLQ 138
Cdd:cd19073  24 LELGYRHIDTAEIYNNE---AEVGEAIAeSGVPREDLFITTKVWRDHLRPE---------------DLKKSVDRSLEKLG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  139 TDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYYAT--SYGKTPFSIYQGKWNVLNRDFE 215
Cdd:cd19073  86 TDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNfTIELLEEALDISPLpiAVNQVEFHPFLYQAELLEYCRE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  216 RDIIPMARhfgMALApwdvmgggrfqskkameerrkNGEGIRsfvgaseqtdaeikiSEALAKIAEEHGTESVTaIAIAY 295
Cdd:cd19073 166 NDIVITAY---SPLA---------------------RGEVLR---------------DPVIQEIAEKYDKTPAQ-VALRW 205
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 6319951  296 VRSKAKNFFPSveGGKIEDLKENIKALSIDLTPDNIK 332
Cdd:cd19073 206 LVQKGIVVIPK--ASSEDHLKENLAIFDWELTSEDVA 240
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
54-240 6.91e-16

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 77.94  E-value: 6.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   54 ELLDTFYEAGGNFIDAANNcqNEQSEEWIGEWIQSRRlrDQIVIATKFiksdkkykAGESNTANycgNHKRSLHvsvrDS 133
Cdd:COG1453  33 ALIRRAIDNGINYIDTARG--YGDSEEFLGKALKGPR--DKVILATKL--------PPWVRDPE---DMRKDLE----ES 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  134 LRKLQTDWIDILYVHWWDYMSSIEEFMDSLHIL------VQQGKVLYLGVS--DTPAWVVSAANYYatsygktPFSIYQG 205
Cdd:COG1453  94 LKRLQTDYIDLYLIHGLNTEEDLEKVLKPGGALealekaKAEGKIRHIGFSthGSLEVIKEAIDTG-------DFDFVQL 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 6319951  206 KWNVLNRDF--ERDIIPMARHFGMALApwdVM---GGGRF 240
Cdd:COG1453 167 QYNYLDQDNqaGEEALEAAAEKGIGVI---IMkplKGGRL 203
AKR_AKR6B1 cd19142
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ...
38-178 5.86e-15

AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.


Pssm-ID: 381368 [Multi-domain]  Cd Length: 325  Bit Score: 74.81  E-value: 5.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   38 GARSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRL-RDQIVIATKFIksdkkYKAGESNta 116
Cdd:cd19142  19 GTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWkRSSYIVSTKIY-----WSYGSEE-- 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319951  117 nyCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVS 178
Cdd:cd19142  92 --RGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTS 151
AKR_KCAB3B_AKR6A9-like cd19160
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ...
22-338 1.26e-13

voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.


Pssm-ID: 381386 [Multi-domain]  Cd Length: 325  Bit Score: 70.78  E-value: 1.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   22 AAIKVSPLILGE-VSYDGARSDflksmnkNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRLRdqiviATK 100
Cdd:cd19160  11 SGLRVSCLGLGTwVTFGSQISD-------ETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWR-----RSS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  101 FIKSDKKYKAGESNTANycGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDT 180
Cdd:cd19160  79 YVVTTKIYWGGQAETER--GLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRW 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  181 PAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARH-FGMALAPWDVMGGGRFQSK---KAMEERRKNGEG- 255
Cdd:cd19160 157 SAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHkIGVGSVTWSPLACGLITGKydgRVPDTCRAAVKGy 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  256 --IRSFVGASEQTDAEIKISEaLAKIAEEHGTeSVTAIAIAY-VRSKAknfFPSVEGG--KIEDLKENIKALSI--DLTP 328
Cdd:cd19160 237 qwLKEKVQSEEGKKQQAKVKE-LHPIADRLGC-TVAQLAIAWcLRSEG---VSSVLLGvsSAEQLIENLGSIQVlsQLTP 311
                       330
                ....*....|
gi 6319951  329 DNIKYLESIV 338
Cdd:cd19160 312 QTVMEIDALL 321
AKR_unchar cd19101
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
45-338 3.20e-13

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381327 [Multi-domain]  Cd Length: 304  Bit Score: 69.55  E-value: 3.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   45 KSMNKNRAFELLDTFYEAGGNFIDAANNCQNeqSEEWIGE----WIQSRRLRDQIVIATKFIKSDKKYKAGESNTANYcg 120
Cdd:cd19101  18 GIRDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEfrkrLRRERDAADDVQIHTKWVPDPGELTMTRAYVEAA-- 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  121 nhkrslhvsVRDSLRKLQTDWIDILYVHWWDY-MSSIEEFMDSLHILVQQGKVLYLGVS--DTP--AWVVSAanyyatsy 195
Cdd:cd19101  94 ---------IDRSLKRLGVDRLDLVQFHWWDYsDPGYLDAAKHLAELQEEGKIRHLGLTnfDTErlREILDA-------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  196 GKTPFSiYQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGrFQSKKAMEER------------RKNGEGIRSFVGas 263
Cdd:cd19101 157 GVPIVS-NQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGG-LLSEKYLGVPeptgpaletrslQKYKLMIDEWGG-- 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  264 eqTDAEIKISEALAKIAEEHGTeSVTAIAIAYVRSKaknffPSVeGGKI------EDLKENIKALSIDLTPDNIKYLESI 337
Cdd:cd19101 233 --WDLFQELLRTLKAIADKHGV-SIANVAVRWVLDQ-----PGV-AGVIvgarnsEHIDDNVRAFSFRLDDEDRAAIDAV 303

                .
gi 6319951  338 V 338
Cdd:cd19101 304 L 304
AKR_AKR14A1 cd19150
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ...
54-332 4.67e-13

Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.


Pssm-ID: 381376 [Multi-domain]  Cd Length: 309  Bit Score: 69.02  E-value: 4.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   54 ELLDTFYEAGGNFIDAANNCQNE--QSEEWIGEWIQS--RRLRDQIVIATKfiksdkkykAGESNTANYCGN--HKRSLH 127
Cdd:cd19150  34 AILRTAFDLGITHFDLANNYGPPpgSAEENFGRILREdfAGYRDELIISTK---------AGYDMWPGPYGEwgSRKYLL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  128 VSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYYATSygKTPFSIYQGK 206
Cdd:cd19150 105 ASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSySPERTREAAAILREL--GTPLLIHQPS 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  207 WNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSK--KAMEERRKNGEGiRSFvGASEQTDAEIKISEALAKIAEEH 283
Cdd:cd19150 183 YNMLNRWVEESgLLDTLQELGVGCIAFTPLAQGLLTDKylNGIPEGSRASKE-RSL-SPKMLTEANLNSIRALNEIAQKR 260
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 6319951  284 GtESVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKAL-SIDLTPDNIK 332
Cdd:cd19150 261 G-QSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALdNLTFSADELA 309
AKR_unchar cd19097
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
48-324 9.20e-13

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381323 [Multi-domain]  Cd Length: 267  Bit Score: 67.55  E-value: 9.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   48 NKNRAFELLDTFYEAGGNFIDAANNCQNeqSEEWIGEWIQSRrlrDQIVIATKFiksdkkykageSNTANYCGNHKRSLH 127
Cdd:cd19097  24 SEKEAKKILEYALKAGINTLDTAPAYGD--SEKVLGKFLKRL---DKFKIITKL-----------PPLKEDKKEDEAAIE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  128 VSVRDSLRKLQTDWIDILYVHWWDYMSSI-EEFMDSLHILVQQGKVLYLGVS-DTPAWVVSAANYYatsygktPFSIYQG 205
Cdd:cd19097  88 ASVEASLKRLKVDSLDGLLLHNPDDLLKHgGKLVEALLELKKEGLIRKIGVSvYSPEELEKALESF-------KIDIIQL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  206 KWNVLNRdferdiipmarhfgmalapwdvmgggRFQSKKAMEERRKNGEGI--RS-------FVGASEQTD--AEIK-IS 273
Cdd:cd19097 161 PFNILDQ--------------------------RFLKSGLLAKLKKKGIEIhaRSvflqgllLMEPDKLPAkfAPAKpLL 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6319951  274 EALAKIAEEHGTeSVTAIAIAYVRSkaknfFPSVEG---G--KIEDLKENIKALSI 324
Cdd:cd19097 215 KKLHELAKKLGL-SPLELALGFVLS-----LPEIDKivvGvdSLEQLKEIIAAFKK 264
PRK09912 PRK09912
L-glyceraldehyde 3-phosphate reductase; Provisional
43-323 1.33e-12

L-glyceraldehyde 3-phosphate reductase; Provisional


Pssm-ID: 182140 [Multi-domain]  Cd Length: 346  Bit Score: 68.09  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    43 FLKSMNKNRAfeLLDTFYEAGGNFIDAANNCQNE--QSEEWIGEWIQS--RRLRDQIVIATK--FIKSDKKYKAGESnta 116
Cdd:PRK09912  38 HVNALESQRA--ILRKAFDLGITHFDLANNYGPPpgSAEENFGRLLREdfAAYRDELIISTKagYDMWPGPYGSGGS--- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   117 nycgnhKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSD-TPAWVVSAANYYATsy 195
Cdd:PRK09912 113 ------RKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSySPERTQKMVELLRE-- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   196 GKTPFSIYQGKWNVLNRDFERD-IIPMARHFGMALAPWDVMGGGRFQSK---KAMEERRKNGEGiRSFVGASEQ--TDAE 269
Cdd:PRK09912 185 WKIPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGKylnGIPQDSRMHREG-NKVRGLTPKmlTEAN 263
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6319951   270 IKISEALAKIAEEHGtESVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALS 323
Cdd:PRK09912 264 LNSLRLLNEMAQQRG-QSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALN 316
ARA1 COG0656
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ...
61-337 6.27e-12

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440421 [Multi-domain]  Cd Length: 259  Bit Score: 65.08  E-value: 6.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEqseEWIGEWI-QSRRLRDQIVIATKFIKSDKKYkagesntanycgnhkRSLHVSVRDSLRKLQT 139
Cdd:COG0656  29 EAGYRHIDTAAMYGNE---EGVGEAIaASGVPREELFVTTKVWNDNHGY---------------DDTLAAFEESLERLGL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  140 DWIDILYVHW---WDYMSSIEEFMDslhiLVQQGKVLYLGVSD-TPA---WVVSAAnyyatsyGKTP------FSIYQGK 206
Cdd:COG0656  91 DYLDLYLIHWpgpGPYVETWRALEE----LYEEGLIRAIGVSNfDPEhleELLAET-------GVKPavnqveLHPYLQQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  207 WNVLNRDFERDIIPMArhfgmalapWDVMGGGrfqskKAMEErrkngegirsfvgaseqtdaeikisEALAKIAEEHGTe 286
Cdd:COG0656 160 RELLAFCREHGIVVEA---------YSPLGRG-----KLLDD-------------------------PVLAEIAEKHGK- 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 6319951  287 SVTAIAIAYVRskAKNFFP---SVeggKIEDLKENIKALSIDLTPDNIKYLESI 337
Cdd:COG0656 200 TPAQVVLRWHL--QRGVVVipkSV---TPERIRENLDAFDFELSDEDMAAIDAL 248
AKR_AKR1-5-like cd19071
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ...
61-335 7.68e-12

AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.


Pssm-ID: 381297 [Multi-domain]  Cd Length: 251  Bit Score: 64.81  E-value: 7.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEQSeewIGEWIQSRRL-RDQIVIATKFIKSDKKYKagesNTANycgnhkrslhvSVRDSLRKLQT 139
Cdd:cd19071  25 EAGYRHIDTAAAYGNEAE---VGEAIRESGVpREELFITTKLWPTDHGYE----RVRE-----------ALEESLKDLGL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  140 DWIDILYVHW---WDYMSSIEEFMDS---LHILVQQGKVLYLGVSdtpawvvsaaNYYAT------SYGKTPFSIYQGKW 207
Cdd:cd19071  87 DYLDLYLIHWpvpGKEGGSKEARLETwraLEELVDEGLVRSIGVS----------NFNVEhleellAAARIKPAVNQIEL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  208 NVLN-----RDF--ERDIIPMArhfgmalapWDVMGGGRFQSKKameerrkngegirsfvgaseqtdaeikiSEALAKIA 280
Cdd:cd19071 157 HPYLqqkelVEFckEHGIVVQA---------YSPLGRGRRPLLD----------------------------DPVLKEIA 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6319951  281 EEHGTeSVTAIAIAYVRSkaKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19071 200 KKYGK-TPAQVLLRWALQ--RGVVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
Aldo_ket_red_shaker cd19141
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ...
21-330 9.16e-12

Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.


Pssm-ID: 381367 [Multi-domain]  Cd Length: 310  Bit Score: 65.16  E-value: 9.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   21 TAAIKVSPLILGE-VSYDGARSDFLksmnknrAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRL-RDQIVIA 98
Cdd:cd19141   7 KSGLRVSCLGLGTwVTFGSQISDEV-------AEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWrRSSYVIT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   99 TKFiksdkkYKAGESNTANycGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVS 178
Cdd:cd19141  80 TKI------FWGGKAETER--GLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  179 DTPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARH-FGMALAPWDVMGGG----------RFQSKKAME 247
Cdd:cd19141 152 RWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHkIGVGAMTWSPLACGilsgkyddgvPEYSRASLK 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  248 ERRKNGEGIRSFVGASEQTdaeiKISEaLAKIAEEHGTeSVTAIAIAY-VRSKAKNffpSVEGG--KIEDLKENIKALSI 324
Cdd:cd19141 232 GYQWLKEKILSEEGRRQQA----KLKE-LQIIADRLGC-TLPQLAIAWcLKNEGVS---SVLLGasSTEQLYENLQAIQV 302

                ....*...
gi 6319951  325 --DLTPDN 330
Cdd:cd19141 303 lpKLTPNI 310
AKR_galDH-like cd19153
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ...
20-185 3.71e-11

L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).


Pssm-ID: 381379 [Multi-domain]  Cd Length: 294  Bit Score: 63.32  E-value: 3.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   20 ETAAIKVSPLILGEVSYDGARSDFLKSMnknrafELLDTFYEA---GGNFIDAANNCQNEQSEEWIGEWIQSRRL-RDQI 95
Cdd:cd19153   6 EIALGNVSPVGLGTAALGGVYGDGLEQD------EAVAIVAEAfaaGINHFDTSPYYGAESSEAVLGKALAALQVpRSSY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   96 VIATKFiksdKKYKAGESNTAnycgnhKRSLHVSVRDSLRKLQTDWIDILYVH---WWDYMSSIEEFMDSLHILVQQGKV 172
Cdd:cd19153  80 TVATKV----GRYRDSEFDYS------AERVRASVATSLERLHTTYLDVVYLHdieFVDYDTLVDEALPALRTLKDEGVI 149
                       170
                ....*....|....*..
gi 6319951  173 LYLGVS----DTPAWVV 185
Cdd:cd19153 150 KRIGIAgyplDTLTRAT 166
AKR_unchar cd19099
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
25-178 4.74e-11

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381325 [Multi-domain]  Cd Length: 316  Bit Score: 63.11  E-value: 4.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   25 KVSPLILGevSYDGARSDFLKSmnknRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIG----EWIQSRRL-RDQIVIAT 99
Cdd:cd19099   2 TLSSLGLG--TYRGDSDDETDE----EYREALKAALDSGINVIDTAINYRGGRSERLIGkalrELIEKGGIkRDEVVIVT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  100 K--FIKSD------------KKYKAGESNTANYCGN----HKRSLHVSVRDSLRKLQTDWIDILYVH----------WWD 151
Cdd:cd19099  76 KagYIPGDgdeplrplkyleEKLGRGLIDVADSAGLrhciSPAYLEDQIERSLKRLGLDTIDLYLLHnpeeqllelgEEE 155
                       170       180
                ....*....|....*....|....*..
gi 6319951  152 YMSSIEEFMDSLHILVQQGKVLYLGVS 178
Cdd:cd19099 156 FYDRLEEAFEALEEAVAEGKIRYYGIS 182
AKR_galDH cd19163
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ...
24-178 5.95e-11

L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).


Pssm-ID: 381389 [Multi-domain]  Cd Length: 293  Bit Score: 62.57  E-value: 5.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   24 IKVSPLILGEvsydGARSDFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRlRDQIVIATKFik 103
Cdd:cd19163  11 LKVSKLGFGA----SPLGGVFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIP-RDSYYLATKV-- 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319951  104 sdKKYKAGESNTANYcgNHKRSLHvSVRDSLRKLQTDWIDILYVHWWDYMSS----IEEFMDSLHILVQQGKVLYLGVS 178
Cdd:cd19163  84 --GRYGLDPDKMFDF--SAERITK-SVEESLKRLGLDYIDIIQVHDIEFAPSldqiLNETLPALQKLKEEGKVRFIGIT 157
AKR_unchar cd19103
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
57-336 7.38e-11

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381329 [Multi-domain]  Cd Length: 299  Bit Score: 62.35  E-value: 7.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   57 DTFYEAGGNFIDAANNCQNEQSEEWIGEWIQsRRLRDQIVIATKFiksdkkykagesnTANYCGNHKRSLHVSVRDSLRK 136
Cdd:cd19103  39 DKAMAAGLNLWDTAAVYGMGASEKILGEFLK-RYPREDYIISTKF-------------TPQIAGQSADPVADMLEGSLAR 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  137 LQTDWIDILYVHwwdYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYatsYGKTPFSIY--QGKWNVLNRDF 214
Cdd:cd19103 105 LGTDYIDIYWIH---NPADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEI---LAKAGVSLSavQNHYSLLYRSS 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  215 ERD-IIPMARHFGMALAPWDV----MGGGRFQSKKAMEERRKNGEGIRSFVGASEqtdaeiKISEALAKIAEEHGTeSVT 289
Cdd:cd19103 179 EEAgILDYCKENGITFFAYMVleqgALSGKYDTKHPLPEGSGRAETYNPLLPQLE------ELTAVMAEIGAKHGA-SIA 251
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 6319951  290 AIAIAYVRskAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLES 336
Cdd:cd19103 252 QVAIAWAI--AKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQ 296
AKR_AKR3F2 cd19139
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ...
61-332 1.72e-10

Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).


Pssm-ID: 381365 [Multi-domain]  Cd Length: 248  Bit Score: 60.44  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEQSeewIGEWI-QSRRLRDQIVIATKfIKSDkkykagesntaNYcgnHKRSLHVSVRDSLRKLQT 139
Cdd:cd19139  25 ELGYRHIDTAQIYDNEAA---VGQAIaESGVPRDELFITTK-IWID-----------NL---SKDKLLPSLEESLEKLRT 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  140 DWIDILYVHW--WDYMSSIEEFMDSLHILVQQGKVLYLGVSDtpawvvsaanyyatsygktpFSIYQ--------GKWNV 209
Cdd:cd19139  87 DYVDLTLIHWpsPNDEVPVEEYIGALAEAKEQGLTRHIGVSN--------------------FTIALldeaiavvGAGAI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  210 LNRDFErdiipmarhfgmaLAPWdvmgggrFQSKKAMEERRKNGEGIRSFvgaseQTDAEIKI--SEALAKIAEEHGTeS 287
Cdd:cd19139 147 ATNQIE-------------LSPY-------LQNRKLVAHCKQHGIHVTSY-----MTLAYGKVldDPVLAAIAERHGA-T 200
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 6319951  288 VTAIAIAYVRSKAKNFFPSveGGKIEDLKENIKALSIDLTPDNIK 332
Cdd:cd19139 201 PAQIALAWAMARGYAVIPS--STKREHLRSNLLALDLTLDADDMA 243
AKR_AKR3F3 cd19140
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ...
61-337 2.56e-10

Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.


Pssm-ID: 381366 [Multi-domain]  Cd Length: 253  Bit Score: 60.35  E-value: 2.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAAnncQNEQSEEWIGEWI-QSRRLRDQIVIATKFIksdkkykagesnTANYcgnHKRSLHVSVRDSLRKLQT 139
Cdd:cd19140  32 ELGYRHIDTA---QMYGNEAQVGEAIaASGVPRDELFLTTKVW------------PDNY---SPDDFLASVEESLRKLRT 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  140 DWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAanyyATSYGKTPFSIYQGKWNVLNRdfERDII 219
Cdd:cd19140  94 DYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLRE----AVELSEAPLFTNQVEYHPYLD--QRKLL 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  220 PMARHFGMALAPWDVMGGGrfqskkameerrkngegirsfvgaseqtdaEIKISEALAKIAEEHGtESVTAIAIAY---- 295
Cdd:cd19140 168 DAAREHGIALTAYSPLARG------------------------------EVLKDPVLQEIGRKHG-KTPAQVALRWllqq 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 6319951  296 ----VRSKAKNFfpsveggkiEDLKENIKALSIDLTPDNIKYLESI 337
Cdd:cd19140 217 egvaAIPKATNP---------ERLEENLDIFDFTLSDEEMARIAAL 253
AKR_KCAB1B_AKR6A3-like cd19159
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ...
22-324 9.36e-10

voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.


Pssm-ID: 381385 [Multi-domain]  Cd Length: 323  Bit Score: 59.29  E-value: 9.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   22 AAIKVSPLILGE-VSYDGARSDflksmnkNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRLR-DQIVIAT 99
Cdd:cd19159   9 SGLRVSCLGLGTwVTFGGQISD-------EVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRrSSLVITT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  100 KFiksdkkYKAGESNTANycGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSD 179
Cdd:cd19159  82 KL------YWGGKAETER--GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  180 TPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARH-FGMALAPWDVMG----GGRFQ------SKKAMEE 248
Cdd:cd19159 154 WSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHkIGVGAMTWSPLAcgiiSGKYGngvpesSRASLKC 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319951  249 RRKNGEGIRSFVGASEQTdaeiKISEaLAKIAEEHGTeSVTAIAIAY-VRSKAknfFPSVEGG--KIEDLKENIKALSI 324
Cdd:cd19159 234 YQWLKERIVSEEGRKQQN----KLKD-LSPIAERLGC-TLPQLAVAWcLRNEG---VSSVLLGssTPEQLIENLGAIQV 303
AKR_AKR8A1-2 cd19077
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ...
51-335 1.85e-09

AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).


Pssm-ID: 381303 [Multi-domain]  Cd Length: 302  Bit Score: 58.02  E-value: 1.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   51 RAFELLDTFYEAGGNFIDAA---NNCQNEQSEEWIGEWIQSR-RLRDQIVIATKFIKSDKKYKAGESntanycgnhKRSL 126
Cdd:cd19077  26 EAFETMKAALDAGSNLWNGGefyGPPDPHANLKLLARFFRKYpEYADKVVLSVKGGLDPDTLRPDGS---------PEAV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  127 HVSVRDSLRKL-QTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYAtsygktPFSIYQG 205
Cdd:cd19077  97 RKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAVH------PIAAVEV 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  206 KWNVLNRD-FERDIIPMARHFGMALAPWDVMGGGRFQSKKAMEERRKNGEGIRSFVGASEQT-DAEIKISEALAKIAEEH 283
Cdd:cd19077 171 EYSLFSREiEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHLDRFNGENfEKNLKLVDALQELAEKK 250
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 6319951  284 GTeSVTAIAIAYVRSKAKN-FFPSVEGGKIEDLKENIKALSIDLTPDNIKYLE 335
Cdd:cd19077 251 GC-TPAQLALAWILAQSGPkIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
AKR_unchar cd19104
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
61-337 2.17e-09

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381330 [Multi-domain]  Cd Length: 321  Bit Score: 58.05  E-value: 2.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEQSEEWIGEWIQSrrLRDQIVIATKfiksdkkYKAGESNTANYCGNHKRSLHvsvrDSLRKLQTD 140
Cdd:cd19104  43 DLGINFFDTAPSYGDGKSEENLGRALKG--LPAGPYITTK-------VRLDPDDLGDIGGQIERSVE----KSLKRLKRD 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  141 WIDILYVH------------------WWDYMssiEEFMDSLHILVQQGKVLYLGVS------------DTPAWvvSAANY 190
Cdd:cd19104 110 SVDLLQLHnrigderdkpvggtlsttDVLGL---GGVADAFERLRSEGKIRFIGITglgnppairellDSGKF--DAVQV 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  191 YATSYGKTPFSIYQGKWNvlNRDFeRDIIPMARHFGMALAPWDVMGGGrfqskkAMEERRKNGEGIRSFVGASEQTDAEi 270
Cdd:cd19104 185 YYNLLNPSAAEARPRGWS--AQDY-GGIIDAAAEHGVGVMGIRVLAAG------ALTTSLDRGREAPPTSDSDVAIDFR- 254
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  271 kISEALAKIAEEHGtESVTAIAIAYVRSKAKnfFPSVEGG--KIEDLKENIKALSI-DLTPDNIKYLESI 337
Cdd:cd19104 255 -RAAAFRALAREWG-ETLAQLAHRFALSNPG--VSTVLVGvkNREELEEAVAAEAAgPLPAENLARLEAL 320
AKR_Fe-S_oxidoreductase cd19096
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ...
45-240 3.97e-09

Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381322 [Multi-domain]  Cd Length: 255  Bit Score: 56.80  E-value: 3.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   45 KSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIqSRRLRDQIVIATKF-IKSDKKYKAGESNtanycgnhk 123
Cdd:cd19096  16 DSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEAL-KEGPREKFYLATKLpPWSVKSAEDFRRI--------- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  124 rslhvsVRDSLRKLQTDWIDILYVHWWDyMSSIEEFMDSLHIL------VQQGKVLYLGVS--DTPAWVVSAANYYatsy 195
Cdd:cd19096  86 ------LEESLKRLGVDYIDFYLLHGLN-SPEWLEKARKGGLLeflekaKKEGLIRHIGFSfhDSPELLKEILDSY---- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 6319951  196 gktPFSIYQGKWNVLNRDFERDI--IPMARHFGMALApwdVM---GGGRF 240
Cdd:cd19096 155 ---DFDFVQLQYNYLDQENQAGRpgIEYAAKKGMGVI---IMeplKGGGL 198
AKR_KCAB2B_AKR6A1-like cd19158
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ...
22-324 6.41e-08

voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.


Pssm-ID: 381384 [Multi-domain]  Cd Length: 324  Bit Score: 53.55  E-value: 6.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   22 AAIKVSPLILGE-VSYDGARSDFLksmnknrAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQSRRLR-DQIVIAT 99
Cdd:cd19158   9 SGLRVSCLGLGTwVTFGGQITDEM-------AEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRrSSLVITT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  100 KFiksdkkYKAGESNTANycGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYMSSIEEFMDSLHILVQQGKVLYLGVSD 179
Cdd:cd19158  82 KI------FWGGKAETER--GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  180 TPAWVVSAANYYATSYGKTPFSIYQGKWNVLNRDFERDIIPMARH-FGMALAPWDVMG----GGRFQSKKAMEERR--KN 252
Cdd:cd19158 154 WSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHkIGVGAMTWSPLAcgivSGKYDSGIPPYSRAslKG 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6319951  253 GEGIRSFVGASEQTDAEIKISEaLAKIAEEHGTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSI 324
Cdd:cd19158 234 YQWLKDKILSEEGRRQQAKLKE-LQAIAERLGC-TLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 303
AKR_FDH cd19162
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ...
51-296 2.28e-07

D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.


Pssm-ID: 381388 [Multi-domain]  Cd Length: 290  Bit Score: 51.59  E-value: 2.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   51 RAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQsRRLRDQIVIATKfiksdkkykAG---ESNTANYCGNHKRSLH 127
Cdd:cd19162  20 EAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA-RHPRAEYVVSTK---------VGrllEPGAAGRPAGADRRFD 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  128 V-------SVRDSLRKLQTDWIDILYVHWWD--YMSSIEEFMDSLHILVQQGKVLYLGVSDTpawVVSAANYYATSYGKT 198
Cdd:cd19162  90 FsadgirrSIEASLERLGLDRLDLVFLHDPDrhLLQALTDAFPALEELRAEGVVGAIGVGVT---DWAALLRAARRADVD 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  199 PFSIyQGKWNVLNRDFERDIIPMARHFGMALAPWDVMGGGRFqskkAMEERrkngEGIRSFVGASeqTDAEIKISEALAK 278
Cdd:cd19162 167 VVMV-AGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGIL----ATDDP----AGDRYDYRPA--TPEVLARARRLAA 235
                       250
                ....*....|....*...
gi 6319951  279 IAEEHGTESVTAiAIAYV 296
Cdd:cd19162 236 VCRRYGVPLPAA-ALQFP 252
AKR_AKR15A1 cd19161
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ...
27-296 4.51e-07

Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.


Pssm-ID: 381387 [Multi-domain]  Cd Length: 310  Bit Score: 50.79  E-value: 4.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   27 SPLILGEVSYDGarsdFLKSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSEEWIGEWIQsRRLRDQIVIATKFIKsdK 106
Cdd:cd19161   1 SELGLGTAGLGN----LYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLR-EKPRDEFVLSTKVGR--L 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  107 KYKAGESNTANYCGNHK----------------RSlhvsVRDSLRKLQTDWIDILYVHWWDYMSSIEEF--------MDS 162
Cdd:cd19161  74 LKPAREGSVPDPNGFVDplpfeivydysydgimRS----FEDSLQRLGLNRIDILYVHDIGVYTHGDRKerhhfaqlMSG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  163 ----LHILVQQG--KVLYLGVSDTPAwVVSAANYYatsygktPFSIY--QGKWNVLNRDFERDIIPMARHFGMALAPwdv 234
Cdd:cd19161 150 gfkaLEELKKAGviKAFGLGVNEVQI-CLEALDEA-------DLDCFllAGRYSLLDQSAEEEFLPRCEQRGTSLVI--- 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6319951  235 mgGGRFQSkkameerrkngeGIRSFVGASEQT------DAEI-KISEALAKIAEEHGTESVTAiAIAYV 296
Cdd:cd19161 219 --GGVFNS------------GILATGTKSGAKfnygdaPAEIiSRVMEIEKICDAYNVPLAAA-ALQFP 272
AKR_AKR5C2 cd19131
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ...
61-179 1.45e-06

Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.


Pssm-ID: 381357 [Multi-domain]  Cd Length: 256  Bit Score: 48.91  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEqseEWIGEWIQSRRL-RDQIVIATKFIKSDKKYKAGESntanycgnhkrslhvSVRDSLRKLQT 139
Cdd:cd19131  34 EVGYRSIDTAAIYGNE---EGVGKAIRASGVpREELFITTKLWNSDQGYDSTLR---------------AFDESLRKLGL 95
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6319951  140 DWIDILYVHWwdYMSSIEEFMDSLHILVQ---QGKVLYLGVSD 179
Cdd:cd19131  96 DYVDLYLIHW--PVPAQDKYVETWKALIElkkEGRVKSIGVSN 136
PLN02587 PLN02587
L-galactose dehydrogenase
27-181 6.07e-06

L-galactose dehydrogenase


Pssm-ID: 178198 [Multi-domain]  Cd Length: 314  Bit Score: 47.47  E-value: 6.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    27 SPL--ILGEVSYDGARSDFlksmnkNRAFELldtfyeaGGNFIDAANNCQNEQSEEWIGEWIQSRRL-RDQIVIATKFik 103
Cdd:PLN02587  19 SPLgsVFGPVSEEDAIASV------REAFRL-------GINFFDTSPYYGGTLSEKVLGKALKALGIpREKYVVSTKC-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   104 sdKKYKAGESNTAnycgnhKRSLHvSVRDSLRKLQTDWIDILYVHWWDYMS---SIEEFMDSLHILVQQGKVLYLGVSDT 180
Cdd:PLN02587  84 --GRYGEGFDFSA------ERVTK-SVDESLARLQLDYVDILHCHDIEFGSldqIVNETIPALQKLKESGKVRFIGITGL 154

                 .
gi 6319951   181 P 181
Cdd:PLN02587 155 P 155
AKR_AKR5A_5G cd19126
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ...
45-179 7.83e-06

AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.


Pssm-ID: 381352 [Multi-domain]  Cd Length: 254  Bit Score: 46.66  E-value: 7.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   45 KSMNKNRAFELLDTFYEAGGNFIDAANNCQNEQSeewIGEWIQSRRL-RDQIVIATKFIKSDKKYKAGESntanycgnhk 123
Cdd:cd19126  18 QTPDGDETERAVQTALENGYRSIDTAAIYKNEEG---VGEAIRESGVpREELFVTTKLWNDDQRARRTED---------- 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319951  124 rslhvSVRDSLRKLQTDWIDILYVHW---------WDYMssiEEFMDSlhilvqqGKVLYLGVSD 179
Cdd:cd19126  85 -----AFQESLDRLGLDYVDLYLIHWpgkdkfidtWKAL---EKLYAS-------GKVKAIGVSN 134
AKR_AKR3C2-3 cd19120
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ...
61-332 1.54e-05

Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.


Pssm-ID: 381346 [Multi-domain]  Cd Length: 269  Bit Score: 46.07  E-value: 1.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEQSeewIGEWI-QSRRLRDQIVIATKFIKSDKKYKAgesntanycgnhkrslhvSVRDSLRKLQT 139
Cdd:cd19120  36 KAGFRHIDTAEMYGNEKE---VGEALkESGVPREDLFITTKVSPGIKDPRE------------------ALRKSLAKLGV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  140 DWIDILYVH--WWDYMS--SIEEFMDSLHILVQQGKVLYLGVSdtpawvvsaaNYYAT------SYGKTPFSIYQGKWNV 209
Cdd:cd19120  95 DYVDLYLIHspFFAKEGgpTLAEAWAELEALKDAGLVRSIGVS----------NFRIEdleellDTAKIKPAVNQIEFHP 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  210 LNRDFERDIIPMARHFGMALApwdvmgggrfqskkameerrkngegirSFVGASEQT-DAEIKISEALAKIAEEHGtESV 288
Cdd:cd19120 165 YLYPQQPALLEYCREHGIVVS---------------------------AYSPLSPLTrDAGGPLDPVLEKIAEKYG-VTP 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 6319951  289 TAIAIAYVRskAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIK 332
Cdd:cd19120 217 AQVLLRWAL--QKGIVVVTTSSKEERMKEYLEAFDFELTEEEVE 258
dkgB PRK11172
2,5-didehydrogluconate reductase DkgB;
61-179 1.64e-05

2,5-didehydrogluconate reductase DkgB;


Pssm-ID: 183012 [Multi-domain]  Cd Length: 267  Bit Score: 45.79  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    61 EAGGNFIDAANNCQNEQSeewIGEWIQ-SRRLRDQIVIATKFIksdkkykagesnTANYCgnhKRSLHVSVRDSLRKLQT 139
Cdd:PRK11172  27 ELGYRAIDTAQIYDNEAA---VGQAIAeSGVPRDELFITTKIW------------IDNLA---KDKLIPSLKESLQKLRT 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 6319951   140 DWIDILYVHW--WDYMSSIEEFMDSLHILVQQGKVLYLGVSD 179
Cdd:PRK11172  89 DYVDLTLIHWpsPNDEVSVEEFMQALLEAKKQGLTREIGISN 130
AKR_ARA2 cd19164
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ...
127-197 2.61e-05

D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).


Pssm-ID: 381390 [Multi-domain]  Cd Length: 298  Bit Score: 45.35  E-value: 2.61e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6319951  127 HVSVRDSLRKLQTDWIDILYVHWWDYMSSiEEFMDSLHILVQ---QGKVLYLGVSDTPAWV-VSAANYYATSYGK 197
Cdd:cd19164 102 RASVERSLRRLHTDYLDLVYLHDVEFVAD-EEVLEALKELFKlkdEGKIRNVGISGYPLPVlLRLAELARTTAGR 175
AKR_AKR5F1 cd19133
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ...
61-178 3.38e-05

the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).


Pssm-ID: 381359 [Multi-domain]  Cd Length: 255  Bit Score: 44.87  E-value: 3.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEqseEWIGEWI-QSRRLRDQIVIATKFIKSDKKYKagesntanycgNHKRSLHvsvrDSLRKLQT 139
Cdd:cd19133  34 KAGYRLIDTAAAYGNE---EAVGRAIkKSGIPREELFITTKLWIQDAGYE-----------KAKKAFE----RSLKRLGL 95
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6319951  140 DWIDILYVHW--------WDYMssiEEfmdslhiLVQQGKVLYLGVS 178
Cdd:cd19133  96 DYLDLYLIHQpfgdvygaWRAM---EE-------LYKEGKIRAIGVS 132
AKR_AKR1I_CgAKR1 cd19155
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ...
56-148 1.64e-04

Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.


Pssm-ID: 381381 [Multi-domain]  Cd Length: 307  Bit Score: 42.90  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   56 LDTFYEAGGNFIDAANNCQNEQSeewIG----EWIQSRRL-RDQIVIATKFIKSdkkykagesntanycGNHKRSLHVSV 130
Cdd:cd19155  31 VDTALEAGYRHIDTAYVYRNEAA---IGnvlkKWIDSGKVkREELFIVTKLPPG---------------GNRREKVEKFL 92
                        90
                ....*....|....*...
gi 6319951  131 RDSLRKLQTDWIDILYVH 148
Cdd:cd19155  93 LKSLEKLQLDYVDLYLIH 110
AKR_CeZK1290-like cd19135
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ...
79-178 2.56e-04

Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.


Pssm-ID: 381361 [Multi-domain]  Cd Length: 265  Bit Score: 42.31  E-value: 2.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   79 EEWIGEWI-QSRRLRDQIVIATKFIKSDKKYKagesNTANYCgnhkrslhvsvRDSLRKLQTDWIDILYVHWWDYMSS-- 155
Cdd:cd19135  52 EELLGKAIkESGVPREDLFLTTKLWPSDYGYE----STKQAF-----------EASLKRLGVDYLDLYLLHWPDCPSSgk 116
                        90       100
                ....*....|....*....|....*...
gi 6319951  156 -----IEEFMDSLHILVQQGKVLYLGVS 178
Cdd:cd19135 117 nvketRAETWRALEELYDEGLCRAIGVS 144
AKR_AKR5D1_E1 cd19132
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ...
61-178 3.42e-04

AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).


Pssm-ID: 381358 [Multi-domain]  Cd Length: 255  Bit Score: 41.87  E-value: 3.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEQSeewIGEWIQSRRL-RDQIVIATKFIKSDKKYKAGESntanycgnhkrslhvSVRDSLRKLQT 139
Cdd:cd19132  31 QAGYRLLDTAFNYENEGA---VGEAVRRSGVpREELFVTTKLPGRHHGYEEALR---------------TIEESLYRLGL 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6319951  140 DWIDILYVHWWD-----YMSSIEEFMDslhiLVQQGKVLYLGVS 178
Cdd:cd19132  93 DYVDLYLIHWPNpsrdlYVEAWQALIE----AREEGLVRSIGVS 132
AKR_AKR5A1_2 cd19156
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ...
61-179 4.08e-04

AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.


Pssm-ID: 381382 [Multi-domain]  Cd Length: 266  Bit Score: 41.73  E-value: 4.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEQSeewIGEWI-QSRRLRDQIVIATKFIKSDKKYkagESNTANYcgnhkrslhvsvRDSLRKLQT 139
Cdd:cd19156  34 EAGYRHIDTAAIYKNEEG---VGQGIrESGVPREEVFVTTKLWNSDQGY---ESTLAAF------------EESLEKLGL 95
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 6319951  140 DWIDILYVHWwdymSSIEEFMDS---LHILVQQGKVLYLGVSD 179
Cdd:cd19156  96 DYVDLYLIHW----PVKGKFKDTwkaFEKLYKEKKVRAIGVSN 134
dkgA PRK11565
2,5-didehydrogluconate reductase DkgA;
61-179 4.45e-04

2,5-didehydrogluconate reductase DkgA;


Pssm-ID: 183203 [Multi-domain]  Cd Length: 275  Bit Score: 41.60  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951    61 EAGGNFIDAANNCQNEqseEWIGEWIQSRRL-RDQIVIATKFIKSDKKykagesntanycgNHKRSLHvsvrDSLRKLQT 139
Cdd:PRK11565  39 EVGYRSIDTAAIYKNE---EGVGKALKEASVaREELFITTKLWNDDHK-------------RPREALE----ESLKKLQL 98
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 6319951   140 DWIDILYVHWwdYMSSIEEFMDS---LHILVQQGKVLYLGVSD 179
Cdd:PRK11565  99 DYVDLYLMHW--PVPAIDHYVEAwkgMIELQKEGLIKSIGVCN 139
AKR_AKR1G1_CeAKR cd19154
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ...
61-148 5.47e-04

Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381380 [Multi-domain]  Cd Length: 303  Bit Score: 41.24  E-value: 5.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNE-QSEEWIGEWIQSRRL-RDQIVIATKFiksdkkykagesntanYCGNHKRS-LHVSVRDSLRKL 137
Cdd:cd19154  36 KAGYRLIDTAFLYQNEeAIGEALAELLEEGVVkREDLFITTKL----------------WTHEHAPEdVEEALRESLKKL 99
                        90
                ....*....|.
gi 6319951  138 QTDWIDILYVH 148
Cdd:cd19154 100 QLEYVDLYLIH 110
AKR_AKR3A1-2 cd19117
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ...
62-179 6.52e-04

AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.


Pssm-ID: 381343 [Multi-domain]  Cd Length: 284  Bit Score: 40.94  E-value: 6.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   62 AGGNFIDAANNCQNEqseEWIGEWIQSRRL-RDQIVIATKFiksdkkykagesntanYCGNHKRsLHVSVRDSLRKLQTD 140
Cdd:cd19117  39 AGYRHIDTAAIYGNE---EEVGQGIKDSGVpREEIFITTKL----------------WCTWHRR-VEEALDQSLKKLGLD 98
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6319951  141 WIDILYVHW-------------------------WDYMSSIEEFMDslhiLVQQGKVLYLGVSD 179
Cdd:cd19117  99 YVDLYLMHWpvpldpdgndflfkkddgtkdhepdWDFIKTWELMQK----LPATGKVKAIGVSN 158
PRK10376 PRK10376
putative oxidoreductase; Provisional
130-337 7.48e-04

putative oxidoreductase; Provisional


Pssm-ID: 236676 [Multi-domain]  Cd Length: 290  Bit Score: 40.72  E-value: 7.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   130 VRDSLRKLQTDWIDILYVH-WWDYMS----SIEEFMDSLHILVQQGKVLYLGVSD-TPAWVVSAAnyyatsyGKTPFSIY 203
Cdd:PRK10376 112 VHDNLRNLGLDVLDVVNLRlMGDGHGpaegSIEEPLTVLAELQRQGLVRHIGLSNvTPTQVAEAR-------KIAEIVCV 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   204 QGKWNVLNRDFERDIIPMARHfGMALAPWDVMGGgrFQSKKameerrkngegirsfvgaseqtdaeikiSEALAKIAEEH 283
Cdd:PRK10376 185 QNHYNLAHRADDALIDALARD-GIAYVPFFPLGG--FTPLQ----------------------------SSTLSDVAASL 233
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6319951   284 GTeSVTAIAIAYVRSKAKNFFPSVEGGKIEDLKENIKALSIDLTPDNIKYLESI 337
Cdd:PRK10376 234 GA-TPMQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
AKR_AKR1G1_1I cd19111
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ...
54-337 1.34e-03

Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.


Pssm-ID: 381337 [Multi-domain]  Cd Length: 286  Bit Score: 40.17  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   54 ELLDTFYEAGGNFIDAANNCQNEQS-EEWIGEWIQSRRL-RDQIVIATKfiksdkkykagesntANYCGNHKRSLHVSVR 131
Cdd:cd19111  21 AAVDYALFVGYRHIDTALSYQNEKAiGEALKWWLKNGKLkREEVFITTK---------------LPPVYLEFKDTEKSLE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  132 DSLRKLQTDWIDILYVHW-W------------DYMSSIEEFMDSLHILVQQGKVLYLGVSDtpaWVVSAANyYATSYGKT 198
Cdd:cd19111  86 KSLENLKLPYVDLYLIHHpCgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSN---FNPRQIN-KILAYAKV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  199 PFSIYQGKWNVLNRdfERDIIPMARHFGMALAPWDVMGggrfqskkameerrknGEGIRSFVGASEQTDaeIKISEALAK 278
Cdd:cd19111 162 KPSNLQLECHAYLQ--QRELRKFCNKKNIVVTAYAPLG----------------SPGRANQSLWPDQPD--LLEDPTVLA 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951  279 IAEEHGtESVTAIAIAYVRSKAKNFFP-SVEGGKIEdlkENIKALSIDLTPDNIKYLESI 337
Cdd:cd19111 222 IAKELD-KTPAQVLLRFVLQRGTGVLPkSTNKERIE---ENFEVFDFELTEEHFKKLKTL 277
AKR_AKR5B1 cd19127
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ...
62-179 2.26e-03

AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.


Pssm-ID: 381353 [Multi-domain]  Cd Length: 268  Bit Score: 39.31  E-value: 2.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   62 AGGNFIDAANNCQNEQSeewIGEWI-QSRRLRDQIVIATKFIKSDKKYKAGEsntanycgnhkrslhVSVRDSLRKLQTD 140
Cdd:cd19127  34 DGYRLIDTAAAYGNERE---VGEGIrRSGVDRSDIFVTTKLWISDYGYDKAL---------------RGFDASLRRLGLD 95
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 6319951  141 WIDILYVHW-----WDymSSIEEFMDSLHILVqQGKVLYLGVSD 179
Cdd:cd19127  96 YVDLYLLHWpvpndFD--RTIQAYKALEKLLA-EGRVRAIGVSN 136
AKR_AKR5G1-3 cd19157
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ...
61-179 6.47e-03

AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.


Pssm-ID: 381383 [Multi-domain]  Cd Length: 265  Bit Score: 37.76  E-value: 6.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319951   61 EAGGNFIDAANNCQNEqseEWIGEWIQ-SRRLRDQIVIATKFIKSDKKYkagESNTANYcgnhkrslhvsvRDSLRKLQT 139
Cdd:cd19157  35 KNGYRSIDTAAIYGNE---EGVGKGIKeSGIPREELFITSKVWNADQGY---DSTLKAF------------EASLERLGL 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 6319951  140 DWIDILYVHWWDYMSSIEEFmDSLHILVQQGKVLYLGVSD 179
Cdd:cd19157  97 DYLDLYLIHWPVKGKYKETW-KALEKLYKDGRVRAIGVSN 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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