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Conserved domains on  [gi|123179543|sp|Q1BE87|]
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RecName: Full=Glutamyl-tRNA reductase; Short=GluTR

Protein Classification

glutamyl-tRNA reductase( domain architecture ID 11477807)

glutamyl-tRNA reductase catalyzes conversion of glutamyl-tRNA to glutamate-1-semialdehyde

CATH:  3.40.50.720|3.30.460.30|1.10.1200.70
EC:  1.2.1.70
Gene Ontology:  GO:0008883|GO:0050661
SCOP:  4000132

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 1-429 2.21e-175

glutamyl-tRNA reductase; Reviewed


:

Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 497.40  E-value: 2.21e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   1 MSVLLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEHCGMS 80
Cdd:PRK00045   1 MSLLAVGLNHKTAPVELREKLAFSEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAIIRWLAEYHGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  81 LNDLTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETGIDA 160
Cdd:PRK00045  81 LEELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNRLFQKAFSVAKRVRTETGIGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 161 AGASVVSVALDIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLldqgvTADAHTLDD 240
Cdd:PRK00045 161 GAVSVASAAVELAKQIFGDLSGKKVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEF-----GGEAIPLDE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 241 IAHALADADVVITSTGAVRPVVSLADAHRGLTGRpEHRRLVICDLGMPRDVEPAIAGLPGVNVIDMERIQR--EPSARAA 318
Cdd:PRK00045 236 LPEALAEADIVISSTGAPHPIIGKGMVERALKAR-RHRPLLLVDLAVPRDIEPEVGELPGVYLYDVDDLQEivEENLAQR 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 319 ASDADAARSIVAAEVANYLAGQRMAEVTPTVTALRQRAADVVEAELLRLDNRLPElDAAHRAEVAKTVRRVVDKLLHAPT 398
Cdd:PRK00045 315 QEAAEKAEAIVEEEVAEFMEWLRSLEVVPTIRALREQAEEIREEELERALKKLGP-GEDEEEVLEKLARSLVNKLLHAPT 393

                        410       420       430
                 ....*....|....*....|....*....|.
gi 123179543 399 VRVKQlASAPGGDSYAEALRELFELDQQAVD 429
Cdd:PRK00045 394 VRLKE-AAEEGDDEYLEALRELFGLDPESVE 423
 
Name Accession Description Interval E-value
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 1-429 2.21e-175

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 497.40  E-value: 2.21e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   1 MSVLLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEHCGMS 80
Cdd:PRK00045   1 MSLLAVGLNHKTAPVELREKLAFSEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAIIRWLAEYHGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  81 LNDLTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETGIDA 160
Cdd:PRK00045  81 LEELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNRLFQKAFSVAKRVRTETGIGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 161 AGASVVSVALDIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLldqgvTADAHTLDD 240
Cdd:PRK00045 161 GAVSVASAAVELAKQIFGDLSGKKVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEF-----GGEAIPLDE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 241 IAHALADADVVITSTGAVRPVVSLADAHRGLTGRpEHRRLVICDLGMPRDVEPAIAGLPGVNVIDMERIQR--EPSARAA 318
Cdd:PRK00045 236 LPEALAEADIVISSTGAPHPIIGKGMVERALKAR-RHRPLLLVDLAVPRDIEPEVGELPGVYLYDVDDLQEivEENLAQR 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 319 ASDADAARSIVAAEVANYLAGQRMAEVTPTVTALRQRAADVVEAELLRLDNRLPElDAAHRAEVAKTVRRVVDKLLHAPT 398
Cdd:PRK00045 315 QEAAEKAEAIVEEEVAEFMEWLRSLEVVPTIRALREQAEEIREEELERALKKLGP-GEDEEEVLEKLARSLVNKLLHAPT 393

                        410       420       430
                 ....*....|....*....|....*....|.
gi 123179543 399 VRVKQlASAPGGDSYAEALRELFELDQQAVD 429
Cdd:PRK00045 394 VRLKE-AAEEGDDEYLEALRELFGLDPESVE 423
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 1-429 1.18e-165

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 472.67  E-value: 1.18e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   1 MSVLLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEHCGMS 80
Cdd:COG0373    1 MSLLVVGLNHKTAPVEIREKLAFSEEELEEALEELKAQPGVDEAVILSTCNRTEIYAVADDPHAGLEALIEFLAEYHGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  81 LNDLTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETGIDA 160
Cdd:COG0373   81 VEELEPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYELAREAGTTGPVLNRLFQKAFSVAKRVRTETGIGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 161 AGASVVSVALDIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSlldqgVTADAHTLDD 240
Cdd:COG0373  161 GAVSVSSAAVELAKKIFGDLSGKTVLVIGAGEMGELAARHLAAKGVKRITVANRTLERAEELAEE-----FGGEAVPLEE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 241 IAHALADADVVITSTGAVRPVVSLADAHRGLTGRPeHRRLVICDLGMPRDVEPAIAGLPGVNVIDMERIQR--EPSARAA 318
Cdd:COG0373  236 LPEALAEADIVISSTGAPHPVITKEMVERALKKRR-HRPLFLIDLAVPRDIEPEVGELPGVYLYDIDDLQEvvDENLEER 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 319 ASDADAARSIVAAEVANYLAGQRMAEVTPTVTALRQRAADVVEAELLRLDNRLPELDAAHRAEVAKTVRRVVDKLLHAPT 398
Cdd:COG0373  315 QAAAPKAEAIIEEEVEEFLEWLKSREVVPTIRALREKAEAIREEELERALKKLPDLGEDEREVLEKLTRSLVNKLLHAPT 394

                        410       420       430
                 ....*....|....*....|....*....|.
gi 123179543 399 VRVKQLASAPGGDSYAEALRELFELDQQAVD 429
Cdd:COG0373  395 VRLKEAAAEGEDDEYLEALRRLFDLEEEEED 425
hemA TIGR01035
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ...
 3-424 8.64e-158

glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713), leads to the production of delta-amino-levulinic acid from Glu-tRNA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273407 [Multi-domain]  Cd Length: 417  Bit Score: 452.61  E-value: 8.64e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543    3 VLLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEHCGMSLN 82
Cdd:TIGR01035   1 ILVLGVSHKSAPVEVREKLSIDEIKLKKALDTLKAEPSIEEAMVLSTCNRVEIYAVVDNLHEGKSALLQILAENKNMSNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   83 DLTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETGIDAAG 162
Cdd:TIGR01035  81 DLEKYLYILTGESAVEHLFRVASGLDSMVVGETQILGQVKNAYKVAQEEKTVGKVLERLFQKAFSVGKRVRTETDISAGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  163 ASVVSVALDIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLLDQGVtadahTLDDIA 242
Cdd:TIGR01035 161 VSISSAAVELAERIFGSLKGKKALLIGAGEMGELVAKHLLRKGVGKILIANRTYERAEDLAKELGGEAV-----KFEDLE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  243 HALADADVVITSTGAVRPVVSLADAHRGLTGRpeHRRLVICDLGMPRDVEPAIAGLPGVNVIDMERIQREPS--ARAAAS 320
Cdd:TIGR01035 236 EYLAEADIVISSTGAPHPIVSKEDVERALRER--TRPLFIIDIAVPRDVDPAVARLEGVFLYDVDDLQPVVEenLAERRE 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  321 DADAARSIVAAEVANYLAGQRMAEVTPTVTALRQRAADVVEAELLRLDNRLPELDAAHRAEVAKTVRRVVDKLLHAPTVR 400
Cdd:TIGR01035 314 EAEKAEEIVEEETAEFKQWLRSLEVEPTIKALRSLAEIVREKELEKALKKLPGLSKDVEEVLEDLARKLINKLLHAPTVR 393

                         410       420
                  ....*....|....*....|....
gi 123179543  401 VKQLASAPGGDSYAEALRELFELD 424
Cdd:TIGR01035 394 LKQLADKEESEVCLEALKNLFGLE 417
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 4-312 8.05e-98

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 295.71  E-value: 8.05e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   4 LLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEhcGMSLND 83
Cdd:cd05213    2 LVIGLSHKTAPVELREKLAFSEEELKEALRRLLEKPGISEAVLLSTCNRVELYLVGDNFHKLADELEELLAE--LLNEPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  84 LTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETGIDAAGA 163
Cdd:cd05213   80 LREYLYVGRGQDAVRHLFRVASGLDSMVVGETQILGQVKNAYKLAKEAGTSGKLLNRLFQKAIKVGKRVRTETGISRGAV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 164 SVVSVALDIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLLdqgvtADAHTLDDIAH 243
Cdd:cd05213  160 SISSAAVELAEKIFGNLKGKKVLVIGAGEMGELAAKHLAAKGVAEITIANRTYERAEELAKELG-----GNAVPLDELLE 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123179543 244 ALADADVVITSTGAVRPVVSLADAHRGLTGRPehrrLVICDLGMPRDVEPAIAGLPGVNVIDMERIQRE 312
Cdd:cd05213  235 LLNEADVVISATGAPHYAKIVERAMKKRSGKP----RLIVDLAVPRDIEPEVGELEGVRLYTIDDLEEV 299
GlutR_N pfam05201
Glutamyl-tRNAGlu reductase, N-terminal domain;
9-156 2.39e-58

Glutamyl-tRNAGlu reductase, N-terminal domain;


Pssm-ID: 461585  Cd Length: 144  Bit Score: 188.10  E-value: 2.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543    9 SHRSAPVSVLEQLSTDESDQAKIVDQVLQsslVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEHCGmSLNDLTKYA 88
Cdd:pfam05201   1 NHKTAPVEIREKLAFSEEELEEALQELRG---IDEAVILSTCNRTEIYAVADDFHAALEAVIEFLAEHSG-DLEELRPYL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123179543   89 YVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSET 156
Cdd:pfam05201  77 YVYEGEEAVRHLFRVASGLDSMVLGEDQILGQVKDAYELAREAGTTGPVLNRLFQKAITVAKRVRTET 144
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 184-253 3.37e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 40.95  E-value: 3.37e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   184 TAVVIGAGSMGALSAKHLVRAGIErVHVVNRSLPRARRLaQSLLDQGVTADAHTLDDIAHALADADVVIT 253
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAE-VTVLDVRPARLRQL-ESLLGARFTTLYSQAELLEEAVKEADLVIG 89
 
Name Accession Description Interval E-value
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 1-429 2.21e-175

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 497.40  E-value: 2.21e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   1 MSVLLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEHCGMS 80
Cdd:PRK00045   1 MSLLAVGLNHKTAPVELREKLAFSEDELEEALESLLASPSVLEAVILSTCNRTEIYAVVDQFHAGREAIIRWLAEYHGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  81 LNDLTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETGIDA 160
Cdd:PRK00045  81 LEELRPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYALAQEAGTVGTILNRLFQKAFSVAKRVRTETGIGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 161 AGASVVSVALDIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLldqgvTADAHTLDD 240
Cdd:PRK00045 161 GAVSVASAAVELAKQIFGDLSGKKVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEF-----GGEAIPLDE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 241 IAHALADADVVITSTGAVRPVVSLADAHRGLTGRpEHRRLVICDLGMPRDVEPAIAGLPGVNVIDMERIQR--EPSARAA 318
Cdd:PRK00045 236 LPEALAEADIVISSTGAPHPIIGKGMVERALKAR-RHRPLLLVDLAVPRDIEPEVGELPGVYLYDVDDLQEivEENLAQR 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 319 ASDADAARSIVAAEVANYLAGQRMAEVTPTVTALRQRAADVVEAELLRLDNRLPElDAAHRAEVAKTVRRVVDKLLHAPT 398
Cdd:PRK00045 315 QEAAEKAEAIVEEEVAEFMEWLRSLEVVPTIRALREQAEEIREEELERALKKLGP-GEDEEEVLEKLARSLVNKLLHAPT 393

                        410       420       430
                 ....*....|....*....|....*....|.
gi 123179543 399 VRVKQlASAPGGDSYAEALRELFELDQQAVD 429
Cdd:PRK00045 394 VRLKE-AAEEGDDEYLEALRELFGLDPESVE 423
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 1-429 1.18e-165

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 472.67  E-value: 1.18e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   1 MSVLLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEHCGMS 80
Cdd:COG0373    1 MSLLVVGLNHKTAPVEIREKLAFSEEELEEALEELKAQPGVDEAVILSTCNRTEIYAVADDPHAGLEALIEFLAEYHGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  81 LNDLTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETGIDA 160
Cdd:COG0373   81 VEELEPYLYVHEGEEAVRHLFRVASGLDSMVLGEPQILGQVKDAYELAREAGTTGPVLNRLFQKAFSVAKRVRTETGIGE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 161 AGASVVSVALDIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSlldqgVTADAHTLDD 240
Cdd:COG0373  161 GAVSVSSAAVELAKKIFGDLSGKTVLVIGAGEMGELAARHLAAKGVKRITVANRTLERAEELAEE-----FGGEAVPLEE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 241 IAHALADADVVITSTGAVRPVVSLADAHRGLTGRPeHRRLVICDLGMPRDVEPAIAGLPGVNVIDMERIQR--EPSARAA 318
Cdd:COG0373  236 LPEALAEADIVISSTGAPHPVITKEMVERALKKRR-HRPLFLIDLAVPRDIEPEVGELPGVYLYDIDDLQEvvDENLEER 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 319 ASDADAARSIVAAEVANYLAGQRMAEVTPTVTALRQRAADVVEAELLRLDNRLPELDAAHRAEVAKTVRRVVDKLLHAPT 398
Cdd:COG0373  315 QAAAPKAEAIIEEEVEEFLEWLKSREVVPTIRALREKAEAIREEELERALKKLPDLGEDEREVLEKLTRSLVNKLLHAPT 394

                        410       420       430
                 ....*....|....*....|....*....|.
gi 123179543 399 VRVKQLASAPGGDSYAEALRELFELDQQAVD 429
Cdd:COG0373  395 VRLKEAAAEGEDDEYLEALRRLFDLEEEEED 425
hemA TIGR01035
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ...
 3-424 8.64e-158

glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713), leads to the production of delta-amino-levulinic acid from Glu-tRNA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273407 [Multi-domain]  Cd Length: 417  Bit Score: 452.61  E-value: 8.64e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543    3 VLLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEHCGMSLN 82
Cdd:TIGR01035   1 ILVLGVSHKSAPVEVREKLSIDEIKLKKALDTLKAEPSIEEAMVLSTCNRVEIYAVVDNLHEGKSALLQILAENKNMSNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   83 DLTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETGIDAAG 162
Cdd:TIGR01035  81 DLEKYLYILTGESAVEHLFRVASGLDSMVVGETQILGQVKNAYKVAQEEKTVGKVLERLFQKAFSVGKRVRTETDISAGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  163 ASVVSVALDIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLLDQGVtadahTLDDIA 242
Cdd:TIGR01035 161 VSISSAAVELAERIFGSLKGKKALLIGAGEMGELVAKHLLRKGVGKILIANRTYERAEDLAKELGGEAV-----KFEDLE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  243 HALADADVVITSTGAVRPVVSLADAHRGLTGRpeHRRLVICDLGMPRDVEPAIAGLPGVNVIDMERIQREPS--ARAAAS 320
Cdd:TIGR01035 236 EYLAEADIVISSTGAPHPIVSKEDVERALRER--TRPLFIIDIAVPRDVDPAVARLEGVFLYDVDDLQPVVEenLAERRE 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  321 DADAARSIVAAEVANYLAGQRMAEVTPTVTALRQRAADVVEAELLRLDNRLPELDAAHRAEVAKTVRRVVDKLLHAPTVR 400
Cdd:TIGR01035 314 EAEKAEEIVEEETAEFKQWLRSLEVEPTIKALRSLAEIVREKELEKALKKLPGLSKDVEEVLEDLARKLINKLLHAPTVR 393

                         410       420
                  ....*....|....*....|....
gi 123179543  401 VKQLASAPGGDSYAEALRELFELD 424
Cdd:TIGR01035 394 LKQLADKEESEVCLEALKNLFGLE 417
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 4-312 8.05e-98

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 295.71  E-value: 8.05e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   4 LLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEhcGMSLND 83
Cdd:cd05213    2 LVIGLSHKTAPVELREKLAFSEEELKEALRRLLEKPGISEAVLLSTCNRVELYLVGDNFHKLADELEELLAE--LLNEPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  84 LTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETGIDAAGA 163
Cdd:cd05213   80 LREYLYVGRGQDAVRHLFRVASGLDSMVVGETQILGQVKNAYKLAKEAGTSGKLLNRLFQKAIKVGKRVRTETGISRGAV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 164 SVVSVALDIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLLdqgvtADAHTLDDIAH 243
Cdd:cd05213  160 SISSAAVELAEKIFGNLKGKKVLVIGAGEMGELAAKHLAAKGVAEITIANRTYERAEELAKELG-----GNAVPLDELLE 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123179543 244 ALADADVVITSTGAVRPVVSLADAHRGLTGRPehrrLVICDLGMPRDVEPAIAGLPGVNVIDMERIQRE 312
Cdd:cd05213  235 LLNEADVVISATGAPHYAKIVERAMKKRSGKP----RLIVDLAVPRDIEPEVGELEGVRLYTIDDLEEV 299
PLN00203 PLN00203
glutamyl-tRNA reductase
 2-429 1.26e-64

glutamyl-tRNA reductase


Pssm-ID: 215101 [Multi-domain]  Cd Length: 519  Bit Score: 216.54  E-value: 1.26e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   2 SVLLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEHCGMSL 81
Cdd:PLN00203  84 SIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAELCSLNHIEEAAVLSTCNRMEIYVVALSWHRGVKEVTEWMSKTSGIPV 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  82 NDLTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETGIDAA 161
Cdd:PLN00203 164 SELRQHLFLLYDKDATQHLFEVSGGLDSLVLGEGQILAQVKQVVKVGQGVDGFGRNLSGLFKHAITAGKRVRTETNIASG 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 162 GASVVSVALDIAEAKL--GSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLldQGVTADAHTLD 239
Cdd:PLN00203 244 AVSVSSAAVELALMKLpeSSHASARVLVIGAGKMGKLLVKHLVSKGCTKMVVVNRSEERVAALREEF--PDVEIIYKPLD 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 240 DIAHALADADVVITSTGAVRPVVSLADAHRGLTGRPE--HRRLVIcDLGMPRDVEPAIAGLPGV---NVIDMERIQrEPS 314
Cdd:PLN00203 322 EMLACAAEADVVFTSTSSETPLFLKEHVEALPPASDTvgGKRLFV-DISVPRNVGACVSELESArvyNVDDLKEVV-AAN 399

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 315 ARAAASDADAARSIVAAEVANYLAGQRMAEVTPTVTALRQRAADVVEAELLRLDNRLPE-LDAAHRAEVAKTVRRVVDKL 393
Cdd:PLN00203 400 KEDRLRKAMEAQTIIREESKNFEAWRDSLETVPTIKKLRSYAERIRAAELEKCLSKMGDdLTKKQRKAVEDLSRGIVNKL 479

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 123179543 394 LHAPtvrVKQLASApGGDSYA--------EALRELFELDQQAVD 429
Cdd:PLN00203 480 LHGP---MQHLRCD-GSDSRTvsetlenmHALNRMFDLETEIAG 519
GlutR_N pfam05201
Glutamyl-tRNAGlu reductase, N-terminal domain;
9-156 2.39e-58

Glutamyl-tRNAGlu reductase, N-terminal domain;


Pssm-ID: 461585  Cd Length: 144  Bit Score: 188.10  E-value: 2.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543    9 SHRSAPVSVLEQLSTDESDQAKIVDQVLQsslVTEAMVLSTCNRVEVYAVVDAFHGGLSVIGQVLAEHCGmSLNDLTKYA 88
Cdd:pfam05201   1 NHKTAPVEIREKLAFSEEELEEALQELRG---IDEAVILSTCNRTEIYAVADDFHAALEAVIEFLAEHSG-DLEELRPYL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123179543   89 YVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSET 156
Cdd:pfam05201  77 YVYEGEEAVRHLFRVASGLDSMVLGEDQILGQVKDAYELAREAGTTGPVLNRLFQKAITVAKRVRTET 144
PRK13940 PRK13940
glutamyl-tRNA reductase; Provisional
 1-424 6.21e-35

glutamyl-tRNA reductase; Provisional


Pssm-ID: 172450 [Multi-domain]  Cd Length: 414  Bit Score: 134.37  E-value: 6.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   1 MSVLLFGVSHRSAPVSVLEQLSTDESDQAKIVDQVLQSSLVTEAMVLSTCNRVEVYAVVDafhgGLSVIGQVLAEHCGMS 80
Cdd:PRK13940   1 MALISLAIDYKKSPIEVRSEFALSGLDVSMLYRSILAIDNVVHAVILSTCNRTEVYLEIS----DLRVVDDILVWWQGYV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  81 LN---DLTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRVHSETG 157
Cdd:PRK13940  77 RNpnyKIKDYFKLRQGTEVIMHLMKLACGLESMVLGEPQILGQVKDSYTLSKKNHAIGKELDRVFQKVFATAKRVRSETR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 158 IDAAGASVVSVALDIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLLDqgvtADAHT 237
Cdd:PRK13940 157 IGHCPVSVAFSAITLAKRQLDNISSKNVLIIGAGQTGELLFRHVTALAPKQIMLANRTIEKAQKITSAFRN----ASAHY 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 238 LDDIAHALADADVVITSTGAVRPVVSLADAHrgltgrpEHRRLVIcDLGMPRDVEPAIAGLPGVNVIDMERIQR--EPSA 315
Cdd:PRK13940 233 LSELPQLIKKADIIIAAVNVLEYIVTCKYVG-------DKPRVFI-DISIPQALDPKLGELEQNVYYCVDDINAviEDNK 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 316 RAAASDADAARSIVAAEVANYLAGQRMAEVTPTVTALRQRAADVVEaelLRLDNRLPELDAAHRAE--VAKTVRRVVDKL 393
Cdd:PRK13940 305 DKRKYESSKAQKIIVKSLEEYLEKEKAIISNSAIKELFQKADGLVD---LSLEKSLAKIRNGKDAEeiIKRFAYEIKKKV 381

                        410       420       430
                 ....*....|....*....|....*....|.
gi 123179543 394 LHAPTVRVKQlASAPGGDSYAEALRELFELD 424
Cdd:PRK13940 382 LHYPVVGMKE-ASKQGRSDCLVCMKRMFGLN 411
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 171-311 1.13e-33

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 123.07  E-value: 1.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  171 DIAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLLDqgvtADAHTLDDIAHALADADV 250
Cdd:pfam01488   1 ELAKKIFGDLKDKKVLLIGAGEMGELVAKHLLAKGAKEVTIANRTIERAQELAEKFGG----VEALPLDDLKEYLAEADI 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123179543  251 VITSTGAVRPVVSLADAHRGLtgRPEHRRLVICDLGMPRDVEPAIAGLPGVNVIDMERIQR 311
Cdd:pfam01488  77 VISATSSPTPIITKEMVERAL--KPRKKPLLFVDIAVPRDIEPEVGELEGVYLYTVDDLKE 135
GlutR_dimer pfam00745
Glutamyl-tRNAGlu reductase, dimerization domain;
328-420 1.93e-21

Glutamyl-tRNAGlu reductase, dimerization domain;


Pssm-ID: 459922 [Multi-domain]  Cd Length: 95  Bit Score: 88.40  E-value: 1.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  328 IVAAEVANYLAGQRMAEVTPTVTALRQRAADVVEAELLRLDNRLPeLDAAHRAEVAKTVRRVVDKLLHAPTVRVKQlASA 407
Cdd:pfam00745   5 IIEEEVEEFMAWLKSLEVVPTIRALREKAEEIREEELERALKKLG-LDGEDREELEKLTRSLVNKLLHDPTVRLKE-AEE 82

                          90
                  ....*....|...
gi 123179543  408 PGGDSYAEALREL 420
Cdd:pfam00745  83 GDGDEYLEALRRL 95
COG5322 COG5322
Predicted amino acid dehydrogenase [General function prediction only];
169-305 2.37e-14

Predicted amino acid dehydrogenase [General function prediction only];


Pssm-ID: 444114 [Multi-domain]  Cd Length: 362  Bit Score: 74.11  E-value: 2.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 169 ALDIAEAKLG-SLAGRTAVVIGA-GSMGALSAKHLVRAGiERVHVVNRSLPRARRLAQSLLdQGVTADAHTLDDIAHALA 246
Cdd:COG5322  137 ATKQAAERMGiDLKKATVAVVGAtGSIGSVCARLLAREV-KRLTLVARNLERLEELAEEIL-RNPGGKVTITTDIDEALR 214

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 247 DADVVITSTGAVRPVVSLADAHRGltgrpehrrLVICDLGMPRDVEPAIAGL-PGVNVID 305
Cdd:COG5322  215 EADIVVTVTSAVGAIIDPEDLKPG---------AVVCDVARPRDVSRRVAEKrPDVLVIE 265
hemA PRK00676
glutamyl-tRNA reductase; Validated
 1-168 6.79e-13

glutamyl-tRNA reductase; Validated


Pssm-ID: 234810 [Multi-domain]  Cd Length: 338  Bit Score: 69.50  E-value: 6.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   1 MSVLLFGVSHRSAPVSVLEQLstdesdqAKIVDQVLQSSLVTE--------AMVLSTCNRVEVYAVVDAFHgglSVIGQV 72
Cdd:PRK00676   1 MVLGVVGISYREAALKEREQV-------IQILQQFEGSLFFRQrffgeegdFVLLLTCHRAELYYYSVSPA---ELQSSL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  73 LAEhcgmsLNDLTKYAYVRYAEAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAEANHTVGRTLHELSQRALSVGKRV 152
Cdd:PRK00676  71 LSE-----ITSLGVRPYFYRGLDCFTHLFCVTSGMDSLILGETEIQGQVKRAYLKAARERKLPFALHFLFQKALKEGKVF 145

                        170
                 ....*....|....*.
gi 123179543 153 HSETGIDAAGASVVSV 168
Cdd:PRK00676 146 RSKGGAPYAEVTIESV 161
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 174-256 6.86e-12

Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 65.55  E-value: 6.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 174 EAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLldqgvTADAHTLDDIAHALADADVVI- 252
Cdd:COG0169  113 REAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAEALAARL-----GVRAVPLDDLAAALAGADLVIn 187


                 ....*
gi 123179543 253 -TSTG 256
Cdd:COG0169  188 aTPLG 192
OCDMu COG2423
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
 183-270 1.72e-09

Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid transport and metabolism]; Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 441972 [Multi-domain]  Cd Length: 322  Bit Score: 59.00  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 183 RTAVVIGAGSMGALSAKHLVRA-GIERVHVVNRSLPRARRLAQSLLDQGVTADAHtlDDIAHALADADVVITSTGAVRPV 261
Cdd:COG2423  128 RTLGIIGAGVQARTQLRALAAVrPIERVRVWGRDPEKAEAFAARLAAEGLPVEAA--DDLEEAVADADIIVTATPSREPV 205


                 ....*....
gi 123179543 262 VSLADAHRG 270
Cdd:COG2423  206 LRGEWLRPG 214
aroE PRK00258
shikimate 5-dehydrogenase; Reviewed
 138-257 1.12e-08

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 234703 [Multi-domain]  Cd Length: 278  Bit Score: 55.96  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 138 LHELSQRALSVGKR---VHSETGI-----DAAGasvvsVALDIAEAKLGSLAGRTAVVIGAG--SMGALSAkhLVRAGIE 207
Cdd:PRK00258  76 ADELSERARLIGAVntlVLEDGRLigdntDGIG-----FVRALEERLGVDLKGKRILILGAGgaARAVILP--LLDLGVA 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 123179543 208 RVHVVNRSLPRARRLAQSLLDQGVTADAHTLDDiahALADADVVITSTGA 257
Cdd:PRK00258 149 EITIVNRTVERAEELAKLFGALGKAELDLELQE---ELADFDLIINATSA 195
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 156-304 1.51e-08

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 54.32  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 156 TGIDAAGASVVSVALDIAEAKLGSLAGRTAVVIGA-GSMGALSAKHLVRAGiERVHVVNRSLPRARRLAQSL---LDQGV 231
Cdd:cd01078    2 NGSNTTAAAAVAAAGKALELMGKDLKGKTAVVLGGtGPVGQRAAVLLAREG-ARVVLVGRDLERAQKAADSLrarFGEGV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123179543 232 TADAHTLDDIAHALADADVVITSTGA--VRPVVSLADAHRGLtgrpehrrLVICDLGMPRDVEPAIAGLPGVNVI 304
Cdd:cd01078   81 GAVETSDDAARAAAIKGADVVFAAGAagVELLEKLAWAPKPL--------AVAADVNAVPPVGIEGIDVPDKGVD 147
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 174-267 6.10e-08

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 51.89  E-value: 6.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 174 EAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLLDQGVTADAHtldDIAHALADADVVI- 252
Cdd:cd01065   11 EEAGIELKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIAIAYL---DLEELLAEADLIIn 87

                         90
                 ....*....|....*.
gi 123179543 253 -TSTGAVRPVVSLADA 267
Cdd:cd01065   88 tTPVGMKPGDELPLPP 103
PRK08291 PRK08291
cyclodeaminase;
183-271 1.15e-07

cyclodeaminase;


Pssm-ID: 236221 [Multi-domain]  Cd Length: 330  Bit Score: 53.43  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 183 RTAVVIGAGsMGA---LSAKHLVRAgIERVHVVNRSLPRARRLAQSL-LDQGVTADAHtlDDIAHALADADVVITSTGAV 258
Cdd:PRK08291 133 SRAAVIGAG-EQArlqLEALTLVRP-IREVRVWARDAAKAEAYAADLrAELGIPVTVA--RDVHEAVAGADIIVTTTPSE 208

                         90
                 ....*....|...
gi 123179543 259 RPVVSLADAHRGL 271
Cdd:PRK08291 209 EPILKAEWLHPGL 221
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 187-267 1.29e-06

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 49.73  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 187 VIGAGSMGALSAKHLVRAGIErVHVVNRSLPRARRLAQslldqgvtADAHTLDDIAHALADADVVITS---TGAVRPVVS 263
Cdd:COG2084    6 FIGLGAMGAPMARNLLKAGHE-VTVWNRTPAKAEALVA--------AGARVAASPAEAAAAADVVITMlpdDAAVEEVLL 76


                 ....
gi 123179543 264 LADA 267
Cdd:COG2084   77 GEDG 80
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 179-260 2.85e-06

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 48.24  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 179 SLAGRTAVVIGAGS-MGALSAKHLVRAGIeRVHVVNRSLPRARRLAQSLLDQGVTADAHTLD-----DIAHALADA---- 248
Cdd:COG1028    3 RLKGKVALVTGGSSgIGRAIARALAAEGA-RVVITDRDAEALEAAAAELRAAGGRALAVAADvtdeaAVEALVAAAvaaf 81

                         90
                 ....*....|....*
gi 123179543 249 ---DVVITSTGAVRP 260
Cdd:COG1028   82 grlDILVNNAGITPP 96
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 186-260 7.66e-06

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 47.37  E-value: 7.66e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123179543 186 VVIGAGSMGALSAKHLVRAGI--ERVHVVNRSLPRARRLAQSLldqGVtadaHTLDDIAHALADADVVItstGAVRP 260
Cdd:COG0345    6 GFIGAGNMGSAIIKGLLKSGVppEDIIVSDRSPERLEALAERY---GV----RVTTDNAEAAAQADVVV---LAVKP 72
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 187-261 9.23e-06

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 45.54  E-value: 9.23e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123179543  187 VIGAGSMGALSAKHLVRAGIErVHVVNRSLPRARRLAQslldqgvtADAHTLDDIAHALADADVVITSTGAVRPV 261
Cdd:pfam03446   4 FIGLGVMGSPMALNLLKAGYT-VTVYNRTPEKVEELVA--------AGAIAAASPAEFVAGLDVVITMVPAGAAV 69
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 160-257 1.07e-05

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 47.44  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 160 AAGASVVSVALDIAEaKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRaRRLAQSL-LDQGVTADAHTL 238
Cdd:COG1063  141 AALVEPLAVALHAVE-RAGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPER-LELARELgADAVVNPREEDL 218

                         90       100
                 ....*....|....*....|..
gi 123179543 239 DDIAHALAD---ADVVITSTGA 257
Cdd:COG1063  219 VEAVRELTGgrgADVVIEAVGA 240
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 180-255 3.96e-05

thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 45.37  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 180 LAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRS---------------------LPRA----RRLAQslLDQGVTAD 234
Cdd:PRK07688  22 LREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDyvewsnlqrqqlytesdvknnLPKAvaakKRLEE--INSDVRVE 99

                         90       100
                 ....*....|....*....|....*
gi 123179543 235 AHTLDDIAHAL----ADADVVITST 255
Cdd:PRK07688 100 AIVQDVTAEELeelvTGVDLIIDAT 124
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 183-252 5.82e-05

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 44.72  E-value: 5.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 183 RTAVVIGAGSMGALSAKHLVRAGIErVHVVNRS---LPRARRLAQSLLDQGVTADAHTLDDIA------------HALAD 247
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYE-VVLLDISpeaLERARARIAKLLDKLVKKGKLTEEEADaalaritpttdlAALAD 81


                 ....*
gi 123179543 248 ADVVI 252
Cdd:COG1250   82 ADLVI 86
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 160-298 6.11e-05

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 44.92  E-value: 6.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 160 AAGASVVSVALDiAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERV---HVVNRSLPRARRLAQsllDQGVTADAH 236
Cdd:cd08232  145 AALAEPLAVALH-AVNRAGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIvatDLADAPLAVARAMGA---DETVNLARD 220

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123179543 237 TLDDIAHALADADVVITSTGAVRPVVSLADAHRgltgrpehRRLVICDLGM-PRDVEPAIAGL 298
Cdd:cd08232  221 PLAAYAADKGDFDVVFEASGAPAALASALRVVR--------PGGTVVQVGMlGGPVPLPLNAL 275
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 186-259 6.66e-05

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 44.70  E-value: 6.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123179543 186 VVIGAGSMGALSAKhlVRAGIE-RVHVVNRSLPRARRLaQSLLDQGVTADAHTLDDIAHALADADVVItstGAVR 259
Cdd:cd05305  172 VILGAGVVGENAAR--VALGLGaEVTVLDINLERLRYL-DDIFGGRVTTLYSNPANLEEALKEADLVI---GAVL 240
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 157-267 1.09e-04

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 44.03  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 157 GIDAAGASVVSvALDIAEA---KLGSLAGRTAVVIGAGSMGALSAKHLVRAGIErVHVVNRS---LPR-----ARRLAQS 225
Cdd:COG0446   97 GLDLPGVFTLR-TLDDADAlreALKEFKGKRAVVIGGGPIGLELAEALRKRGLK-VTLVERAprlLGVldpemAALLEEE 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 123179543 226 LLDQGVtaDAHTLDDIAHALAD--------------ADVVITSTGaVRPVVSLADA 267
Cdd:COG0446  175 LREHGV--ELRLGETVVAIDGDdkvavtltdgeeipADLVVVAPG-VRPNTELAKD 227
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
181-267 1.15e-04

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 44.36  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 181 AGRTAVVIGAGSMGALSAKHLVRAGIErVHVVNRS---LPR------ARRLAQSLLDQGVT------ADAHTLDDIAHA- 244
Cdd:COG1251  141 PGKRVVVIGGGLIGLEAAAALRKRGLE-VTVVERAprlLPRqldeeaGALLQRLLEALGVEvrlgtgVTEIEGDDRVTGv 219

                         90       100
                 ....*....|....*....|....*....
gi 123179543 245 -LAD-----ADVVITSTGaVRPVVSLADA 267
Cdd:COG1251  220 rLADgeelpADLVVVAIG-VRPNTELARA 247
Glu_dehyd_C pfam16912
Glucose dehydrogenase C-terminus;
164-267 1.17e-04

Glucose dehydrogenase C-terminus;


Pssm-ID: 407146 [Multi-domain]  Cd Length: 211  Bit Score: 43.09  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  164 SVVSVALDIAEAkLGSLAG---RTAVVIGAGSMGALSAKHL-VRAGIERVHVVNRslpRAR-----RLAQSLLDQGVTAD 234
Cdd:pfam16912  11 SIVEKAIEHAEA-SRSRFEwrpRSALVLGNGPLGLLALAMLrVQRGFDRVYCLGR---RDRpdptiDLVEELGATYVDSR 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 123179543  235 AHTLDDIAHALADADVVITSTGAVRPVVSLADA 267
Cdd:pfam16912  87 ETPVDEIPAAHEPMDLVYEATGYAPHAFEAIDA 119
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 159-261 1.22e-04

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 44.14  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 159 DAAGASVVSVALDiAEAKLGSLAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSlPRARRLAQSL-LDQGVTADAHT 237
Cdd:cd08236  138 EAAMIEPAAVALH-AVRLAGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDID-DEKLAVARELgADDTINPKEED 215

                         90       100
                 ....*....|....*....|....*.
gi 123179543 238 LDDIAHAL--ADADVVITSTGAVRPV 261
Cdd:cd08236  216 VEKVRELTegRGADLVIEAAGSPATI 241
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 94-288 1.46e-04

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 44.21  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543  94 EAAVEHLFAVASGLDSAVIGEQQVLGQVRRAYTSAE-ANHTVGRTlHELSQRALSVG---KRVHSETGIDAAGASVVS-- 167
Cdd:PLN02328 129 EVDVEALIAISVGFPVDSLTEEEIEANVVSTIGGTEqANYIVVRN-HILARWRSNVSnwlTRDHALESIRAEHKNLVDsa 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 168 -------------VALDIAEAKLGSLAG---RTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLLDQGV 231
Cdd:PLN02328 208 ynfllehgyinfgVAPVIKEAQLRSFEGvepANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGDGV 287

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 123179543 232 TADAhtldDIAHAladadvVITSTGAvRPVVSLAdahRGLtGRPEHRRLVICDLGMP 288
Cdd:PLN02328 288 VAAA----DLGGS------VLTGING-NPLGVLA---RQL-GLPLHKVRDICPLYLP 329
PRK12549 PRK12549
shikimate 5-dehydrogenase; Reviewed
 185-255 1.70e-04

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 183586 [Multi-domain]  Cd Length: 284  Bit Score: 43.35  E-value: 1.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123179543 185 AVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLLDQGVTADAHTLDDIAHALADADVVITST 255
Cdd:PRK12549 130 VVQLGAGGAGAAVAHALLTLGVERLTIFDVDPARAAALADELNARFPAARATAGSDLAAALAAADGLVHAT 200
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
179-249 1.74e-04

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 42.93  E-value: 1.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123179543 179 SLAGRTAVVIGAGS-MGALSAKHLVRAGIeRVHVVNRSLPRARRLAQSLLDQGVTADAHTLDdiahaLADAD 249
Cdd:COG0300    2 SLTGKTVLITGASSgIGRALARALAARGA-RVVLVARDAERLEALAAELRAAGARVEVVALD-----VTDPD 67
PRK08618 PRK08618
ornithine cyclodeaminase family protein;
183-263 2.08e-04

ornithine cyclodeaminase family protein;


Pssm-ID: 236313 [Multi-domain]  Cd Length: 325  Bit Score: 43.13  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 183 RTAVVIGAG--SMGALSAKHLVRaGIERVHVVNRSLPRARRLAQSLLDQ-GVTADAHTldDIAHALADADVVITSTGAVR 259
Cdd:PRK08618 128 KTLCLIGTGgqAKGQLEAVLAVR-DIERVRVYSRTFEKAYAFAQEIQSKfNTEIYVVN--SADEAIEEADIIVTVTNAKT 204


                 ....
gi 123179543 260 PVVS 263
Cdd:PRK08618 205 PVFS 208
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
187-268 2.61e-04

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 42.08  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 187 VIGAGSMGALSAKHLVRAGIErVHVVNRSLPRARRLAQSLldqGVTADAHTLDDiahALADADVVITST--GAVRPVVSL 264
Cdd:COG2085    3 IIGTGNIGSALARRLAAAGHE-VVIGSRDPEKAAALAAEL---GPGARAGTNAE---AAAAADVVVLAVpyEAVPDVLES 75


                 ....
gi 123179543 265 ADAH 268
Cdd:COG2085   76 LGDA 79
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 184-253 3.37e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 40.95  E-value: 3.37e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543   184 TAVVIGAGSMGALSAKHLVRAGIErVHVVNRSLPRARRLaQSLLDQGVTADAHTLDDIAHALADADVVIT 253
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAE-VTVLDVRPARLRQL-ESLLGARFTTLYSQAELLEEAVKEADLVIG 89
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 131-257 7.41e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.84  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 131 NHTVGRTLHELSQRALSVGKRVHSETGIDAAGASvvsvaLDIAEAKLGSLAGRTavvigaGSMGALSAKHLVRAGIeRVH 210
Cdd:PLN03209  41 KHPHSRKLRSLDIKAQASGATKFSSAAIEAIPKE-----LDTKDEDLAFVAGAT------GKVGSRTVRELLKLGF-RVR 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123179543 211 VVNRSLPRARRLAQS-----LLDQG---------VTADAHTLDDIAHALADADVVITSTGA 257
Cdd:PLN03209 109 AGVRSAQRAESLVQSvkqmkLDVEGtqpvekleiVECDLEKPDQIGPALGNASVVICCIGA 169
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 179-239 7.90e-04

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 41.04  E-value: 7.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123179543 179 SLAGRTAVVIGA-GSMGALSAKHLVRAGIeRVHVVNRSLPRARRLAQSLLDQGVTADAHTLD 239
Cdd:PRK08277   7 SLKGKVAVITGGgGVLGGAMAKELARAGA-KVAILDRNQEKAEAVVAEIKAAGGEALAVKAD 67
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 179-280 9.58e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 41.07  E-value: 9.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 179 SLAGRTAVVIGAGSMGALSAKHLvRAGIERVHVVNRSLPRarrlaqslldQGVTADAHTLDDIAHALADADVVITSTgav 258
Cdd:cd12165  134 ELRGKTVGILGYGHIGREIARLL-KAFGMRVIGVSRSPKE----------DEGADFVGTLSDLDEALEQADVVVVAL--- 199

                         90       100
                 ....*....|....*....|..
gi 123179543 259 rPvvsLADAHRGLTGRPEHRRL 280
Cdd:cd12165  200 -P---LTKQTRGLIGAAELAAM 217
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 180-256 1.02e-03

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 40.80  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 180 LAGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRsLPRARRLAQSL-LDQGVTADAHTLDDIAHALAD---ADVVITST 255
Cdd:cd08269  128 RAGKTVAVIGAGFIGLLFLQLAAAAGARRVIAIDR-RPARLALARELgATEVVTDDSEAIVERVRELTGgagADVVIEAV 206


                 .
gi 123179543 256 G 256
Cdd:cd08269  207 G 207
PRK06141 PRK06141
ornithine cyclodeaminase family protein;
186-263 1.22e-03

ornithine cyclodeaminase family protein;


Pssm-ID: 180421  Cd Length: 314  Bit Score: 40.66  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 186 VVIGAGSMGALSAK-HL-VRAgIERVHVVNRSLPRARRLAQSLLDQGVTADAhtLDDIAHALADADVVITSTGAVRPVVS 263
Cdd:PRK06141 129 LVVGTGRLASLLALaHAsVRP-IKQVRVWGRDPAKAEALAAELRAQGFDAEV--VTDLEAAVRQADIISCATLSTEPLVR 205
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
174-267 1.61e-03

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 40.98  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 174 EAKLG------SLAGRTAVVIGAGS-MGALSAKHLVRAGIERVhVVNRSLPRARRLAQSLLDQ----GVTADAHTLDDIA 242
Cdd:PRK08324 408 QAKLQrmpkpkPLAGKVALVTGAAGgIGKATAKRLAAEGACVV-LADLDEEAAEAAAAELGGPdralGVACDVTDEAAVQ 486

                         90       100
                 ....*....|....*....|....*
gi 123179543 243 HALADAdvvITSTGAVRPVVSLADA 267
Cdd:PRK08324 487 AAFEEA---ALAFGGVDIVVSNAGI 508
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 186-252 1.63e-03

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 40.18  E-value: 1.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123179543 186 VVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLldqgvtaDAHTLDDIAHALADADVVI 252
Cdd:COG5495    7 GIIGAGRVGTALAAALRAAGHEVVGVYSRSPASAERAAALL-------GAVPALDLEELAAEADLVL 66
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 186-252 1.94e-03

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 37.95  E-value: 1.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123179543  186 VVIGAGSMGALSAKHLVRAG-IERVHVVNRSLPRARRLAQSLLDQGVTADAHTLDDIAHALA----DADVVI 252
Cdd:pfam03435   2 LIIGAGSVGQGVAPLLARHFdVDRITVADRTLEKAQALAAKLGGVRFIAVAVDADNYEAVLAallkEGDLVV 73
NAD_binding_10 pfam13460
NAD(P)H-binding;
189-257 2.26e-03

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 39.13  E-value: 2.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123179543  189 GAGSMGALSAKHLVRAGIERVHVVnRSLPRARRLAQSLLDQGVTADAHTLDDIAHALADADVVITSTGA 257
Cdd:pfam13460   2 ATGKIGRLLVKQLLARGHEVTALV-RNPEKLADLEDHPGVEVVDGDVLDPDDLAEALAGQDAVISALGG 69
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 179-239 2.46e-03

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 39.65  E-value: 2.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123179543 179 SLAGRTAVVIGAGS-MGALSAKHLVRAGIErVHVVNRSLPRARRLAQSLLDQGVTADAHTLD 239
Cdd:cd05347    2 SLKGKVALVTGASRgIGFGIASGLAEAGAN-IVINSRNEEKAEEAQQLIEKEGVEATAFTCD 62
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 180-252 2.78e-03

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 39.34  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 180 LAGRTAVVIGAGSMGALSAKHLVRAGIERVHVV----------NRSL---------PRARRLAQSLLDQ--GVTADAH-- 236
Cdd:COG0476   25 LKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVdddvvelsnlQRQIlyteadvgrPKVEAAAERLRALnpDVEVEAIpe 104

                         90
                 ....*....|....*...
gi 123179543 237 --TLDDIAHALADADVVI 252
Cdd:COG0476  105 rlTEENALELLAGADLVL 122
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 186-256 3.03e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 39.28  E-value: 3.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123179543 186 VVIGAGSMGALSAKHLVRAGIErVHVVNRSLPRARRLAQSLLdQGVTADAHTLDDIAHA-LADADVVITSTG 256
Cdd:COG0569   99 IIIGAGRVGRSLARELEEEGHD-VVVIDKDPERVERLAEEDV-LVIVGDATDEEVLEEAgIEDADAVIAATG 168
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
183-252 3.27e-03

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 39.19  E-value: 3.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 183 RTAVVIGAGSMGALSAKHLVRAGiERVHVVNRSLPRARRLAQSLLDQGVTADAHTLDDIAHALADADVVI 252
Cdd:COG0451    1 RILVTGGAGFIGSHLARRLLARG-HEVVGLDRSPPGAANLAALPGVEFVRGDLRDPEALAAALAGVDAVV 69
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 186-260 3.30e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 38.97  E-value: 3.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123179543 186 VVIGAGSMGALSAKHLVRAGI--ERVHVVNRSLPRARRLAQSLldqGVTADAhtldDIAHALADADVVItstGAVRP 260
Cdd:PRK11880   6 GFIGGGNMASAIIGGLLASGVpaKDIIVSDPSPEKRAALAEEY---GVRAAT----DNQEAAQEADVVV---LAVKP 72
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 186-259 4.15e-03

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 39.22  E-value: 4.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123179543 186 VVIGAGSMGALSAKHLVRAGIErVHVVNRSLPRARRLaQSLLDQGV---TADAHTlddIAHALADADVVItstGAVR 259
Cdd:COG0686  172 VILGGGVVGTNAARMALGLGAD-VTVLDINLDRLRRL-DDIFGGRVttlYSNPAN---IEEALKEADLVI---GAVL 240
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 179-252 4.55e-03

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 38.62  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 179 SLAGRTAVVIGAGS-MGALSAKHLVRAGIeRVHVVNRSLPRARRLAQSLldqGVTADAHTLD-----DIAHALADA---- 248
Cdd:COG4221    2 SDKGKVALITGASSgIGAATARALAAAGA-RVVLAARRAERLEALAAEL---GGRALAVPLDvtdeaAVEAAVAAAvaef 77


                 ....*..
gi 123179543 249 ---DVVI 252
Cdd:COG4221   78 grlDVLV 84
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
187-254 4.61e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 36.44  E-value: 4.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123179543  187 VIGAGSMGALSAKHLVRAGIERVHVVN-RSLPRARRLAQSLldqGVTADAHTLDDiahALADADVVITS 254
Cdd:pfam03807   2 FIGAGNMGEALARGLVAAGPHEVVVANsRNPEKAEELAEEY---GVGATAVDNEE---AAEEADVVFLA 64
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 180-256 4.68e-03

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 36.69  E-value: 4.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123179543  180 LAGRTAVVIGAGSMGALSAKHLVRAGiERVHVVNRSLPRARRLAQSLLDQGVTADahtlddiahaLADADVVITSTG 256
Cdd:pfam13241   5 LRGKRVLVVGGGEVAARKARKLLEAG-AKVTVVSPEITPFLEGLLDLIRREFEGD----------LDGADLVIAATD 70
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 181-258 4.91e-03

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 38.73  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 181 AGRTAVVIGAGSMGALSAKHLVRAGIERVHVVNRSLPRARRLAQSLLDQGVTADAHTLDDIAHALAD---ADVVITSTGA 257
Cdd:cd08235  165 PGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGADYTIDAAEEDLVEKVRELTDgrgADVVIVATGS 244


                 .
gi 123179543 258 V 258
Cdd:cd08235  245 P 245
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 178-252 6.65e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.


Pssm-ID: 240625 [Multi-domain]  Cd Length: 313  Bit Score: 38.27  E-value: 6.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123179543 178 GSLAGRTAVVIGAGSMGALSAKhLVRA-GIeRVHVVNRSlPRArrlaqsllDQGVTADAHTLDDIAHALADADVVI 252
Cdd:cd05300  130 RELAGKTVLIVGLGDIGREIAR-RAKAfGM-RVIGVRRS-GRP--------APPVVDEVYTPDELDELLPEADYVV 194
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 187-252 8.58e-03

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 37.91  E-value: 8.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123179543 187 VIGAGSMGALSAKHLVRAGIErVHVVNRSLPRARRLAQ---SLLDQGVTADAHTLDDIAHaLADADVVI 252
Cdd:PRK06522   5 ILGAGAIGGLFGAALAQAGHD-VTLVARRGAHLDALNEnglRLEDGEITVPVLAADDPAE-LGPQDLVI 71
FabG-like PRK07231
SDR family oxidoreductase;
180-269 9.20e-03

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 37.89  E-value: 9.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123179543 180 LAGRTAVVIGAGS-MGALSAKHLVRAGiERVHVVNRSLPRARRLAQSLLDQG----VTADAHTLDDIAHALADA------ 248
Cdd:PRK07231   3 LEGKVAIVTGASSgIGEGIARRFAAEG-ARVVVTDRNEEAAERVAAEILAGGraiaVAADVSDEADVEAAVAAAlerfgs 81

                         90       100
                 ....*....|....*....|....*..
gi 123179543 249 -DVVITSTG---AVRPV--VSLADAHR 269
Cdd:PRK07231  82 vDILVNNAGtthRNGPLldVDEAEFDR 108
 
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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