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Conserved domains on  [gi|663530329|gb|AIF20318|]
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UDP-glucose/GDP-mannose dehydrogenase (wbpO) [uncultured marine thaumarchaeote KM3_89_C12]

Protein Classification

nucleotide sugar dehydrogenase( domain architecture ID 11430796)

nucleotide sugar dehydrogenase such as UDP-N-acetylglucosamine 6-dehydrogenase, which catalyzes the C-6 dehydrogenation of UDP-D-GlcNAc to UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA)

CATH:  3.40.50.720
EC:  1.1.1.-
Gene Ontology:  GO:0051287|GO:0016628

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
20-446 1.13e-160

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 460.30  E-value: 1.13e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKV-VYEYTDILEDVVLKSKKLHVTIEPkEALDNAEIIFV 98
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDpILEPGDELLAEAVAAGRLRATTDP-EALAEADVVII 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  99 CVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTI-ESLCNLKFGIDLGLAYCPERYNPTpmk 177
Cdd:COG0677   80 AVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPIlEKRSGLKAGEDFFLAYSPERINPG--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 178 kytkDVDHTISakgesftvdRISRVVGGIDEKSTKITKTIYSQFVKTDVLELSSIETAEATKLLENIFRDVNIALVNELA 257
Cdd:COG0677  157 ----NKLHELR---------NIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 258 KIYPKFGLNIYEIINAATSKPFaFMPHYPGAGVGGECIPVDTWYLISQAEKLGMDTKILNSARQINDSMPTHMITLLENE 337
Cdd:COG0677  224 LICDRLGIDVWEVIEAANTKPG-FLIFYPGPGVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKA 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 338 LHKHGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVY---EKVDSNVQLTPLSNIFNGSDAILF 414
Cdd:COG0677  303 LNEAGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVdeeEVEGEYGELVDLEEALEGADAVVL 382
                        410       420       430
                 ....*....|....*....|....*....|..
gi 663530329 415 VTDHDIFTTLDFSKIKdEMKTPLIIDGRNFFN 446
Cdd:COG0677  383 AVDHDEFDELDPEELR-LKGAKVVVDTRGVLD 413
 
Name Accession Description Interval E-value
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
20-446 1.13e-160

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 460.30  E-value: 1.13e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKV-VYEYTDILEDVVLKSKKLHVTIEPkEALDNAEIIFV 98
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDpILEPGDELLAEAVAAGRLRATTDP-EALAEADVVII 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  99 CVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTI-ESLCNLKFGIDLGLAYCPERYNPTpmk 177
Cdd:COG0677   80 AVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPIlEKRSGLKAGEDFFLAYSPERINPG--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 178 kytkDVDHTISakgesftvdRISRVVGGIDEKSTKITKTIYSQFVKTDVLELSSIETAEATKLLENIFRDVNIALVNELA 257
Cdd:COG0677  157 ----NKLHELR---------NIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 258 KIYPKFGLNIYEIINAATSKPFaFMPHYPGAGVGGECIPVDTWYLISQAEKLGMDTKILNSARQINDSMPTHMITLLENE 337
Cdd:COG0677  224 LICDRLGIDVWEVIEAANTKPG-FLIFYPGPGVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKA 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 338 LHKHGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVY---EKVDSNVQLTPLSNIFNGSDAILF 414
Cdd:COG0677  303 LNEAGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVdeeEVEGEYGELVDLEEALEGADAVVL 382
                        410       420       430
                 ....*....|....*....|....*....|..
gi 663530329 415 VTDHDIFTTLDFSKIKdEMKTPLIIDGRNFFN 446
Cdd:COG0677  383 AVDHDEFDELDPEELR-LKGAKVVVDTRGVLD 413
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
20-443 4.03e-132

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 387.35  E-value: 4.03e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINsAKVVYEYTDILEDVV---LKSKKLHVTIEPKEALDNAEII 96
Cdd:TIGR03026   2 KIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLN-KGKSPIYEPGLDELLakaLKAGRLRATTDYEEAIRDADVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   97 FVCVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIESLCNLKFGIDLGLAYCPERYNPTPM 176
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYNPEFLREGNA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  177 KkytkdvdhtisakgesFTVDRISRVVGGIDEKSTKITKTIYSQFVKTDVLeLSSIETAEATKLLENIFRDVNIALVNEL 256
Cdd:TIGR03026 161 V----------------HDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVL-VTSIETAEMIKLAENTFRAVKIAFANEL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  257 AKIYPKFGLNIYEIINAATSKPF-AFMPHYPGAGVGGECIPVDTWYLISQAEKLGMDTKILNSARQINDSMPTHMITLLE 335
Cdd:TIGR03026 224 ARICEALGIDVYEVIEAAGTDPRiGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIK 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  336 NELhkhgKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPV--YEKVDSNVQLTPLSNIFNGSDAIL 413
Cdd:TIGR03026 304 DLL----GPLKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLvpEEEVKGLPSIDDLEEALKGADALV 379
                         410       420       430
                  ....*....|....*....|....*....|
gi 663530329  414 FVTDHDIFTTLDFSKIKDEMKTPLIIDGRN 443
Cdd:TIGR03026 380 ILTDHSEFKDLDLEKIKDLMKGKVVVDTRN 409
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
20-440 1.27e-63

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 211.38  E-value: 1.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVvyeytDILE---DVVLKSK----KLHVTIEPKEAldN 92
Cdd:PRK11064   5 TISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEI-----HIVEpdlDMVVKTAveggYLRATTTPEPA--D 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  93 AEIIfvCVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTI-ESLCNLKF------GIDLGLA 165
Cdd:PRK11064  78 AFLI--AVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLaEARPDLTFpqqageQADINIA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 166 YCPERYNPtpmkkytkdvDHTISakgESFTVDrisRVVGGIDEKSTKITKTIYSQFVKTDVLELSSiETAEATKLLENIF 245
Cdd:PRK11064 156 YCPERVLP----------GQVMV---ELIKND---RVIGGMTPVCSARASELYKIFLEGECVVTNS-RTAEMCKLTENSF 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 246 RDVNIALVNELAKIYPKFGLNIYEIINAATSKPFAFMPHyPGAGVGGECIPVDTWYLISQAEKLgmdTKILNSARQINDS 325
Cdd:PRK11064 219 RDVNIAFANELSLICADQGINVWELIRLANRHPRVNILQ-PGPGVGGHCIAVDPWFIVAQNPQQ---ARLIRTAREVNDG 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 326 MPTHMI----TLLENELHKHGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKV-NFLVCDP----VYEKVDSN 396
Cdd:PRK11064 295 KPHWVIdqvkAAVADCLAATDKRASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWHSgETLVVEPnihqLPKKLDGL 374
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 663530329 397 VQLTPLSNIFNGSDAILFVTDHDIFTTLDfskiKDEMKTPLIID 440
Cdd:PRK11064 375 VTLVSLDEALATADVLVMLVDHSQFKAIN----GDNVHQQWVVD 414
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
20-212 6.20e-37

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 133.91  E-value: 6.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKV-VYEYTdiLEDVVLK--SKKLHVTIEPKEALDNAEII 96
Cdd:pfam03721   2 KISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIpIYEPG--LDELVKAnvSGRLSFTTDYSTAIEEADVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   97 FVCVPTPLNIK-KEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIESLCNLKFGIDLGLAYCPERYNP-T 174
Cdd:pfam03721  80 FIAVGTPSKKGgGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFDVASNPEFLREgS 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 663530329  175 PMKkytkdvdhtisakgESFTVDRIsrvVGGIDEKSTK 212
Cdd:pfam03721 160 AVY--------------DLFNPDRV---VIGVTEKCAE 180
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
352-446 4.45e-25

UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 214954 [Multi-domain]  Cd Length: 99  Bit Score: 98.73  E-value: 4.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   352 ILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVYEKVDSNVQLTPLSNI---FNGSDAILFVTDHDIFTTLDFSK 428
Cdd:smart00984   2 VLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYGLTYVSDLeeaLKGADAVVIATEHDEFRSLDPEE 81
                           90
                   ....*....|....*...
gi 663530329   429 IKDEMKTPLIIDGRNFFN 446
Cdd:smart00984  82 LKDLMKKPVVVDGRNILD 99
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
20-53 8.64e-03

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. 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: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 38.02  E-value: 8.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQ-VTGLDIDQKR 53
Cdd:cd08255  100 RVAVVGLGLVGLLAAQLAKAAGAReVVGVDPDAAR 134
 
Name Accession Description Interval E-value
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
20-446 1.13e-160

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 460.30  E-value: 1.13e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKV-VYEYTDILEDVVLKSKKLHVTIEPkEALDNAEIIFV 98
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDpILEPGDELLAEAVAAGRLRATTDP-EALAEADVVII 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  99 CVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTI-ESLCNLKFGIDLGLAYCPERYNPTpmk 177
Cdd:COG0677   80 AVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPIlEKRSGLKAGEDFFLAYSPERINPG--- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 178 kytkDVDHTISakgesftvdRISRVVGGIDEKSTKITKTIYSQFVKTDVLELSSIETAEATKLLENIFRDVNIALVNELA 257
Cdd:COG0677  157 ----NKLHELR---------NIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELA 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 258 KIYPKFGLNIYEIINAATSKPFaFMPHYPGAGVGGECIPVDTWYLISQAEKLGMDTKILNSARQINDSMPTHMITLLENE 337
Cdd:COG0677  224 LICDRLGIDVWEVIEAANTKPG-FLIFYPGPGVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKA 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 338 LHKHGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVY---EKVDSNVQLTPLSNIFNGSDAILF 414
Cdd:COG0677  303 LNEAGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVdeeEVEGEYGELVDLEEALEGADAVVL 382
                        410       420       430
                 ....*....|....*....|....*....|..
gi 663530329 415 VTDHDIFTTLDFSKIKdEMKTPLIIDGRNFFN 446
Cdd:COG0677  383 AVDHDEFDELDPEELR-LKGAKVVVDTRGVLD 413
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
20-443 4.03e-132

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 387.35  E-value: 4.03e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINsAKVVYEYTDILEDVV---LKSKKLHVTIEPKEALDNAEII 96
Cdd:TIGR03026   2 KIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLN-KGKSPIYEPGLDELLakaLKAGRLRATTDYEEAIRDADVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   97 FVCVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIESLCNLKFGIDLGLAYCPERYNPTPM 176
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYNPEFLREGNA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  177 KkytkdvdhtisakgesFTVDRISRVVGGIDEKSTKITKTIYSQFVKTDVLeLSSIETAEATKLLENIFRDVNIALVNEL 256
Cdd:TIGR03026 161 V----------------HDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVL-VTSIETAEMIKLAENTFRAVKIAFANEL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  257 AKIYPKFGLNIYEIINAATSKPF-AFMPHYPGAGVGGECIPVDTWYLISQAEKLGMDTKILNSARQINDSMPTHMITLLE 335
Cdd:TIGR03026 224 ARICEALGIDVYEVIEAAGTDPRiGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIK 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  336 NELhkhgKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPV--YEKVDSNVQLTPLSNIFNGSDAIL 413
Cdd:TIGR03026 304 DLL----GPLKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLvpEEEVKGLPSIDDLEEALKGADALV 379
                         410       420       430
                  ....*....|....*....|....*....|
gi 663530329  414 FVTDHDIFTTLDFSKIKDEMKTPLIIDGRN 443
Cdd:TIGR03026 380 ILTDHSEFKDLDLEKIKDLMKGKVVVDTRN 409
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
20-463 1.57e-84

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 266.50  E-value: 1.57e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKV-VYEYTdiLEDVV---LKSKKLHVTIEPKEALDNAEI 95
Cdd:COG1004    2 KIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIpIYEPG--LEELVarnVAAGRLRFTTDLAEAVAEADV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  96 IFVCVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIESLcNLKFGIDLGLAYCPE--Rynp 173
Cdd:COG1004   80 VFIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEE-LRGAGVDFDVVSNPEflR--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 174 tpmkkytkdvdhtisakgESFTV------DRIsrVVGGIDEKSTKITKTIYSQFVKTDV-LELSSIETAEATKLLENIFR 246
Cdd:COG1004  156 ------------------EGSAVedflrpDRI--VIGVDSERAAEVLRELYAPFVRNGTpIIVTDLRSAELIKYAANAFL 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 247 DVNIALVNELAKIYPKFGLNIYEIINAATSKP---FAFMphYPGAGVGGECIPVDTWYLISQAEKLGMDTKILNSARQIN 323
Cdd:COG1004  216 ATKISFINEIANLCEKVGADVEEVARGIGLDSrigPKFL--YAGIGYGGSCFPKDVRALIATARELGYDLRLLEAVEEVN 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 324 DSMPTHMITLLENELhkhGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPV-----YEKVDSNVQ 398
Cdd:COG1004  294 ERQKRRLVEKIREHL---GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVamenaRRLLPDDIT 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663530329 399 L--TPLSNIfNGSDAILFVTDHDIFTTLDFSKIKDEMKTPLIIDGRNFFNAEKLISLGFYYRAIGKP 463
Cdd:COG1004  371 YadDAYEAL-EGADALVILTEWPEFRALDFARLKALMKGPVIFDGRNLLDPEELRAAGFTYYGIGRP 436
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
20-440 1.27e-63

UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 211.38  E-value: 1.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVvyeytDILE---DVVLKSK----KLHVTIEPKEAldN 92
Cdd:PRK11064   5 TISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEI-----HIVEpdlDMVVKTAveggYLRATTTPEPA--D 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  93 AEIIfvCVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTI-ESLCNLKF------GIDLGLA 165
Cdd:PRK11064  78 AFLI--AVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLaEARPDLTFpqqageQADINIA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 166 YCPERYNPtpmkkytkdvDHTISakgESFTVDrisRVVGGIDEKSTKITKTIYSQFVKTDVLELSSiETAEATKLLENIF 245
Cdd:PRK11064 156 YCPERVLP----------GQVMV---ELIKND---RVIGGMTPVCSARASELYKIFLEGECVVTNS-RTAEMCKLTENSF 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 246 RDVNIALVNELAKIYPKFGLNIYEIINAATSKPFAFMPHyPGAGVGGECIPVDTWYLISQAEKLgmdTKILNSARQINDS 325
Cdd:PRK11064 219 RDVNIAFANELSLICADQGINVWELIRLANRHPRVNILQ-PGPGVGGHCIAVDPWFIVAQNPQQ---ARLIRTAREVNDG 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 326 MPTHMI----TLLENELHKHGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKV-NFLVCDP----VYEKVDSN 396
Cdd:PRK11064 295 KPHWVIdqvkAAVADCLAATDKRASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWHSgETLVVEPnihqLPKKLDGL 374
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 663530329 397 VQLTPLSNIFNGSDAILFVTDHDIFTTLDfskiKDEMKTPLIID 440
Cdd:PRK11064 375 VTLVSLDEALATADVLVMLVDHSQFKAIN----GDNVHQQWVVD 414
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
18-430 8.13e-56

Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 191.44  E-value: 8.13e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  18 DVRVCVIGVGTIGLPLATFLAKvGFQVTGLDIDQKRIDEI-NSAKVVYEYTdilEDVVLKSKKLHVTIEpKEALDNAEII 96
Cdd:PRK15182   6 EVKIAIIGLGYVGLPLAVEFGK-SRQVVGFDVNKKRILELkNGVDVNLETT---EEELREARYLKFTSE-IEKIKECNFY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  97 FVCVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTRE-ISKTIESLCNLKFGIDLGLAYCPERYNPtp 175
Cdd:PRK15182  81 IITVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEeCVPILARMSGMTFNQDFYVGYSPERINP-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 176 mkkytKDVDHTISakgesftvdRISRVVGGIDEKSTKITKTIYSQFVKTDVLELSSIETAEATKLLENIFRDVNIALVNE 255
Cdd:PRK15182 159 -----GDKKHRLT---------NIKKITSGSTAQIAELIDEVYQQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNE 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 256 LAKIYPKFGLNIYEIINAATSKpFAFMPHYPGAgVGGECIPVDTWYLISQAEKLGMDTKILNSARQINDSMPTHMITLLE 335
Cdd:PRK15182 225 LAIIFNRLNIDTEAVLRAAGSK-WNFLPFRPGL-VGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNMGNYVSEQLI 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 336 NELHKHGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVY--EKVDSNVQLTPLSNIFNGS-DAI 412
Cdd:PRK15182 303 KAMIKKGINVEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVdaEEVRREYGIIPVSEVKSSHyDAI 382
                        410
                 ....*....|....*...
gi 663530329 413 LFVTDHDIFTTLDFSKIK 430
Cdd:PRK15182 383 IVAVGHQQFKQMGSEDIR 400
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
20-212 6.20e-37

UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 397677 [Multi-domain]  Cd Length: 186  Bit Score: 133.91  E-value: 6.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKV-VYEYTdiLEDVVLK--SKKLHVTIEPKEALDNAEII 96
Cdd:pfam03721   2 KISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIpIYEPG--LDELVKAnvSGRLSFTTDYSTAIEEADVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   97 FVCVPTPLNIK-KEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIESLCNLKFGIDLGLAYCPERYNP-T 174
Cdd:pfam03721  80 FIAVGTPSKKGgGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFDVASNPEFLREgS 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 663530329  175 PMKkytkdvdhtisakgESFTVDRIsrvVGGIDEKSTK 212
Cdd:pfam03721 160 AVY--------------DLFNPDRV---VIGVTEKCAE 180
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
234-324 7.42e-36

UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 460015 [Multi-domain]  Cd Length: 92  Bit Score: 127.49  E-value: 7.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  234 TAEATKLLENIFRDVNIALVNELAKIYPKFGLNIYEIINAATSKPF-AFMPHYPGAGVGGECIPVDTWYLISQAEKLGMD 312
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRiGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
                          90
                  ....*....|..
gi 663530329  313 TKILNSARQIND 324
Cdd:pfam00984  81 ARLLEAAREVNE 92
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
18-463 1.87e-27

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 114.39  E-value: 1.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  18 DVRVCVIGVGTIGLPLATFLAKV--GFQVTGLDIDQKRIDEINSAKV-VYEYTdiLEDVV--LKSKKLHVTIEPKEALDN 92
Cdd:PLN02353   1 MVKICCIGAGYVGGPTMAVIALKcpDIEVVVVDISVPRIDAWNSDQLpIYEPG--LDEVVkqCRGKNLFFSTDVEKHVAE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  93 AEIIFVCVPTP-----LNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIESLCN-LKFGIdlgLAy 166
Cdd:PLN02353  79 ADIVFVSVNTPtktrgLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKgINFQI---LS- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 167 cperyNPTPMKKYTkdvdhtisAKGESFTVDRIsrVVGGID----EKSTKITKTIYSQFVKTDVLELSSIETAEATKLLE 242
Cdd:PLN02353 155 -----NPEFLAEGT--------AIEDLFKPDRV--LIGGREtpegQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAA 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 243 NIFRDVNIALVNELAKIYPKFGLNIYEIINAaTSKPFAFMPHYPGAGVG--GECIPVDTWYLISQAEKLGMDtKILNSAR 320
Cdd:PLN02353 220 NAFLAQRISSVNAMSALCEATGADVSQVSHA-VGKDSRIGPKFLNASVGfgGSCFQKDILNLVYICECNGLP-EVAEYWK 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 321 Q---INDSMPTH----MITLLENELhkhgkelSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDP-VYEK 392
Cdd:PLN02353 298 QvikMNDYQKSRfvnrVVSSMFNTV-------SGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPqVTEE 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 393 ------------VDSNVQLTPLSNIF--------------NGSDAILFVTDHDIFTTLDFSKIKDEMKTP-LIIDGRNFF 445
Cdd:PLN02353 371 qiqrdlsmnkfdWDHPRHLQPMSPTAvkqvsvvwdayeatKGAHGICILTEWDEFKTLDYQKIYDNMQKPaFVFDGRNVL 450
                        490
                 ....*....|....*...
gi 663530329 446 NAEKLISLGFYYRAIGKP 463
Cdd:PLN02353 451 DHEKLREIGFIVYSIGKP 468
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
352-446 4.45e-25

UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 214954 [Multi-domain]  Cd Length: 99  Bit Score: 98.73  E-value: 4.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   352 ILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVYEKVDSNVQLTPLSNI---FNGSDAILFVTDHDIFTTLDFSK 428
Cdd:smart00984   2 VLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYGLTYVSDLeeaLKGADAVVIATEHDEFRSLDPEE 81
                           90
                   ....*....|....*...
gi 663530329   429 IKDEMKTPLIIDGRNFFN 446
Cdd:smart00984  82 LKDLMKKPVVVDGRNILD 99
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
352-447 1.57e-22

UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.


Pssm-ID: 427462 [Multi-domain]  Cd Length: 103  Bit Score: 91.87  E-value: 1.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  352 ILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPV---YEKVDSNVQLTPLSNI---FNGSDAILFVTDHDIFTTLD 425
Cdd:pfam03720   2 VLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYvpeEAIEALGDGVTLVDDLeeaLKGADAIVILTDHDEFKSLD 81
                          90       100
                  ....*....|....*....|..
gi 663530329  426 FSKIKDEMKTPLIIDGRNFFNA 447
Cdd:pfam03720  82 WEKLKKLMKPPVVFDGRNVLDP 103
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
19-392 1.86e-15

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 77.76  E-value: 1.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  19 VRVCVIGVGTIGLPLATFLAKvGFQVTGLDIDQKRIDEINSAkvVYEYTDILEDVVLKSKKLH--VTIEPKEALDNAEII 96
Cdd:PRK15057   1 MKITISGTGYVGLSNGLLIAQ-NHEVVALDILPSRVAMLNDR--ISPIVDKEIQQFLQSDKIHfnATLDKNEAYRDADYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  97 FVCVPTPLNIKKEMDNSN-----LLDVANrISPYltkgMILIFESSVAIGSTREISKtieslcnlKFGIDlGLAYCPERY 171
Cdd:PRK15057  78 IIATPTDYDPKTNYFNTSsvesvIKDVVE-INPY----AVMVIKSTVPVGFTAAMHK--------KYRTE-NIIFSPEFL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 172 NPTpmkkytkdvdhtiSAKGESFTVDRIsrVVGGIDEKSTKITKTIYSQFVKTDVLELSSIET-AEATKLLENIFRDVNI 250
Cdd:PRK15057 144 REG-------------KALYDNLHPSRI--VIGERSERAERFAALLQEGAIKQNIPTLFTDSTeAEAIKLFANTYLAMRV 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 251 ALVNELAKIYPKFGLNIYEIINAATSKPfAFMPHY--PGAGVGGECIPVDTWYLISQAEklgmdtkilnsarqindSMPT 328
Cdd:PRK15057 209 AYFNELDSYAESLGLNTRQIIEGVCLDP-RIGNHYnnPSFGYGGYCLPKDTKQLLANYQ-----------------SVPN 270
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663530329 329 HMITLL--ENELHKH--GKELSSAKISILG---LCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVYEK 392
Cdd:PRK15057 271 NLISAIvdANRTRKDfiADAILSRKPQVVGiyrLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKE 341
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
20-133 7.36e-10

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 60.05  E-value: 7.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKvvyEYTDILEDVVLkSKKLHVTIEPKEALDNAEIIFVC 99
Cdd:COG0240    2 KIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETR---ENPRYLPGVKL-PENLRATSDLEEALAGADLVLLA 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 663530329 100 VPTplnikkemdnSNLLDVANRISPYLTKGMILI 133
Cdd:COG0240   78 VPS----------QALREVLEQLAPLLPPGAPVV 101
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
20-148 4.27e-08

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: 52.47  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVVYEYTdiledvvlkskklhvtiePKEALDNAEIIFVC 99
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAAS------------------PAEFVAGLDVVITM 62
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 663530329  100 VPTPLNIKKEMDNSNLLdvanrisPYLTKGMILIFESSVAIGSTREISK 148
Cdd:pfam03446  63 VPAGAAVDAVIFGEGLL-------PGLKPGDIIIDGSTSSPEDARRRAK 104
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
20-151 1.14e-07

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 53.20  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEinsakvvyeytdiledvvLKSKKLHVTIEPKEALDNAEIIFVC 99
Cdd:COG2084    3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEA------------------LVAAGARVAASPAEAAAAADVVITM 64
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663530329 100 VPTPlnikKEMDnsNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIE 151
Cdd:COG2084   65 LPDD----AAVE--EVLLGEDGLLAALRPGAVVVDMSTISPETARELAAAAA 110
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
20-133 1.51e-07

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 53.15  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVVYEYtdiLEDVVLkSKKLHVTIEPKEALDNAEIIFVC 99
Cdd:PRK00094   3 KIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENPRY---LPGIKL-PDNLRATTDLAEALADADLILVA 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 663530329 100 VPTplnikkemdnSNLLDVANRISPYLTKGMILI 133
Cdd:PRK00094  79 VPS----------QALREVLKQLKPLLPPDAPIV 102
NAD_Gly3P_dh_N pfam01210
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ...
21-133 1.98e-07

NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.


Pssm-ID: 395967 [Multi-domain]  Cd Length: 158  Bit Score: 50.65  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   21 VCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVVYEYtdiLEDVVLkSKKLHVTIEPKEALDNAEIIFVCV 100
Cdd:pfam01210   2 IAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINTTHENVRY---LPGIKL-PENLKATTDLAEALKGADIIVIVV 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 663530329  101 PTplnikkemdnSNLLDVANRISPYLTKGMILI 133
Cdd:pfam01210  78 PS----------QALREVLKQLKGLLKPDAILV 100
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
20-133 6.37e-07

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


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 50.90  E-value: 6.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIG--LPLAtfLAKVGF--QVTGLDIDQKRIDEINSAKVVYEYTDiledvvlkskklhvtiEPKEALDNAEI 95
Cdd:COG0287    3 RIAIIGLGLIGgsLALA--LKRAGLahEVVGVDRSPETLERALELGVIDRAAT----------------DLEEAVADADL 64
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 663530329  96 IFVCVPTPLNIkkemdnsnllDVANRISPYLTKGMILI 133
Cdd:COG0287   65 VVLAVPVGATI----------EVLAELAPHLKPGAIVT 92
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
17-153 2.20e-05

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: 45.82  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  17 MDVRVCVIGVGTIGLPLATFLAKVGF---QVTGLDIDQKRIDEINSAKVVyeytdiledvvlkskklHVTIEPKEALDNA 93
Cdd:COG0345    1 MSMKIGFIGAGNMGSAIIKGLLKSGVppeDIIVSDRSPERLEALAERYGV-----------------RVTTDNAEAAAQA 63
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  94 EIIFVCVPtPLNIKkemdnsnllDVANRISPYLTKGMILIfesSVAIGstreisKTIESL 153
Cdd:COG0345   64 DVVVLAVK-PQDLA---------EVLEELAPLLDPDKLVI---SIAAG------VTLATL 104
garR PRK11559
tartronate semialdehyde reductase; Provisional
17-273 1.37e-04

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 43.50  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  17 MDVRVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVVYEYTdiledvvlkskklhvtiePKEALDNAEII 96
Cdd:PRK11559   1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETAST------------------AKAVAEQCDVI 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  97 FVCVPTPLNIKKEMDNSN-LLDVANrispyltKGMILIFESSVAIGSTREISKTIEslcnlKFGIDLglaycperynptp 175
Cdd:PRK11559  63 ITMLPNSPHVKEVALGENgIIEGAK-------PGTVVIDMSSIAPLASREIAAALK-----AKGIEM------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 176 mkkytkdVDHTISAkGESFTVD-RISRVVGG---IDEKSTKITKTIYSQFVKTdvlelSSIETAEATKLLENIFRDVNIA 251
Cdd:PRK11559 118 -------LDAPVSG-GEPKAIDgTLSVMVGGdkaIFDKYYDLMKAMAGSVVHT-----GDIGAGNVTKLANQVIVALNIA 184
                        250       260
                 ....*....|....*....|..
gi 663530329 252 LVNELAKIYPKFGLNIYEIINA 273
Cdd:PRK11559 185 AMSEALVLATKAGVNPDLVYQA 206
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
20-124 1.89e-04

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 43.24  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDeinsaKVVYEYTDILEDVVLKSK-----------KLHVTIEPKE 88
Cdd:PRK09260   3 KLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLE-----SAQQEIASIFEQGVARGKlteaarqaalaRLSYSLDLKA 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 663530329  89 ALDNAEIIFVCVPTPLNIKKEmdnsnLLDVANRISP 124
Cdd:PRK09260  78 AVADADLVIEAVPEKLELKKA-----VFETADAHAP 108
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
10-116 3.48e-04

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: 42.36  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  10 SIRRIQEMDVRVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVVYEYTDILEDVVLKskklhvtiepKEA 89
Cdd:COG0569   87 MERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLE----------EAG 156
                         90       100
                 ....*....|....*....|....*..
gi 663530329  90 LDNAEIIFVCVPTplnikkemDNSNLL 116
Cdd:COG0569  157 IEDADAVIAATGD--------DEANIL 175
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
21-134 6.46e-04

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 39.91  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   21 VCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIdEINSAKvvYEYTDILEDVVLKSKklhVTIEPKEALDNAEIIFVCV 100
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELA-AIKKNG--LRLTSPGGERIVPPP---AVTSASESLGPIDLVIVTV 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 663530329  101 ptplnikKEMDnsnLLDVANRISPYLTKGMILIF 134
Cdd:pfam02558  75 -------KAYQ---TEEALEDIAPLLGPNTVVLL 98
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
19-134 1.20e-03

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 40.60  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329  19 VRVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSakvvyeytdilEDVVLKSKKLHV---TIEPKEALDNAEI 95
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNE-----------NGLRLEDGEITVpvlAADDPAELGPQDL 69
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 663530329  96 IFVCVptplnikKEMDNSnllDVANRISPYLTKGMILIF 134
Cdd:PRK06522  70 VILAV-------KAYQLP---AALPSLAPLLGPDTPVLF 98
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
20-53 8.64e-03

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. 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: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 38.02  E-value: 8.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 663530329  20 RVCVIGVGTIGLPLATFLAKVGFQ-VTGLDIDQKR 53
Cdd:cd08255  100 RVAVVGLGLVGLLAAQLAKAAGAReVVGVDPDAAR 134
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
7-75 8.82e-03

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 36.15  E-value: 8.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329   7 LPNSIRRIQEMDVRVCVIGVGTiGLpLATFLAKVGFQVTGLDIDQKRIDE----INSAKVVYEYTDILE--------DVV 74
Cdd:COG2227   14 LAALLARLLPAGGRVLDVGCGT-GR-LALALARRGADVTGVDISPEALEIarerAAELNVDFVQGDLEDlpledgsfDLV 91

                 .
gi 663530329  75 L 75
Cdd:COG2227   92 I 92
 
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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