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Conserved domains on  [gi|490071752|ref|WP_003973927|]
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MULTISPECIES: nucleotide sugar dehydrogenase [Streptomyces]

Protein Classification

nucleotide sugar dehydrogenase( domain architecture ID 11496319)

nucleotide sugar dehydrogenase such as GDP-mannose 6-dehydrogenase, which catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 15-420 5.82e-160

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: 457.46  E-value: 5.82e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   15 PTVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRDIARGAVDL-LPLHHAQLACASAGDRFRLTPDAT-AVRDADAV 92
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIyEPGLDELLAKALKAGRLRATTDYEeAIRDADVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   93 VICVPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTRDLLVEPLRARGLTVDEDVYVAFAPERIDPGNE 172
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYNPEFLREGNA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  173 RHTPERTPRLVGGAGPRSSRAAADLLAPTASAVRTVPDPETAEMAKLWENTYRAVNIALANELADACHSLGLAPAPVIEA 252
Cdd:TIGR03026 161 VHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  253 AATKPY-GFMPFYPGPGVGGHCIPCDPHYLLWQLGKVRQQAPLVATALAANSRRPARITERALDLLadsaVPAHGARVLL 331
Cdd:TIGR03026 241 AGTDPRiGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLL----GPLKGKTVLI 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  332 IGVAYKEGVADVRESPALEILAGLAEAGAHVAYCDPLVPSLRVGADALHHLPDPHTRPWDLVVLNTVHPV-HDLTWLCAD 410
Cdd:TIGR03026 317 LGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDLEEALKGADALVILTDHSEfKDLDLEKIK 396

                         410
                  ....*....|...
gi 490071752  411 D---APPVLDTRQ 420
Cdd:TIGR03026 397 DlmkGKVVVDTRN 409
 
Name Accession Description Interval E-value
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 15-420 5.82e-160

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: 457.46  E-value: 5.82e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   15 PTVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRDIARGAVDL-LPLHHAQLACASAGDRFRLTPDAT-AVRDADAV 92
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIyEPGLDELLAKALKAGRLRATTDYEeAIRDADVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   93 VICVPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTRDLLVEPLRARGLTVDEDVYVAFAPERIDPGNE 172
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYNPEFLREGNA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  173 RHTPERTPRLVGGAGPRSSRAAADLLAPTASAVRTVPDPETAEMAKLWENTYRAVNIALANELADACHSLGLAPAPVIEA 252
Cdd:TIGR03026 161 VHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  253 AATKPY-GFMPFYPGPGVGGHCIPCDPHYLLWQLGKVRQQAPLVATALAANSRRPARITERALDLLadsaVPAHGARVLL 331
Cdd:TIGR03026 241 AGTDPRiGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLL----GPLKGKTVLI 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  332 IGVAYKEGVADVRESPALEILAGLAEAGAHVAYCDPLVPSLRVGADALHHLPDPHTRPWDLVVLNTVHPV-HDLTWLCAD 410
Cdd:TIGR03026 317 LGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDLEEALKGADALVILTDHSEfKDLDLEKIK 396

                         410
                  ....*....|...
gi 490071752  411 D---APPVLDTRQ 420
Cdd:TIGR03026 397 DlmkGKVVVDTRN 409
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
16-419 2.18e-157

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 451.05  E-value: 2.18e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  16 TVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRDIARGAVDLLPLHHAQLACASAGDRFRLTPDATAVRDADAVVIC 95
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGRLRATTDPEALAEADVVIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  96 VPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTRDLLVEPLRAR-GLTVDEDVYVAFAPERIDPGNERH 174
Cdd:COG0677   81 VPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRsGLKAGEDFFLAYSPERINPGNKLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 175 TPERTPRLVGGAGPRSSRAAADLLAPTASA-VRTVPDPETAEMAKLWENTYRAVNIALANELADACHSLGLAPAPVIEAA 253
Cdd:COG0677  161 ELRNIPKVVGGITPESAERAAALYGSVVTAgVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 254 ATKPyGFMPFYPGPGVGGHCIPCDPHYLLWQLGKVRQQAPLVATALAANSRRPARITERALDLLADSAVPAHGARVLLIG 333
Cdd:COG0677  241 NTKP-GFLIFYPGPGVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLVLG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 334 VAYKEGVADVRESPALEILAGLAEAGAHVAYCDPLVPSLRVGA--DALHHLpDPHTRPWDLVVLNTVHPV---HDLTWLC 408
Cdd:COG0677  320 LAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGeyGELVDL-EEALEGADAVVLAVDHDEfdeLDPEELR 398

                        410
                 ....*....|.
gi 490071752 409 ADDAPPVLDTR 419
Cdd:COG0677  399 LKGAKVVVDTR 409
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 16-357 8.41e-52

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 179.79  E-value: 8.41e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  16 TVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRDIARGAV-----DLLPLHHAqlacASAGDRFRLTpdaTAVRDAD 90
Cdd:PRK11064   5 TISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIhivepDLDMVVKT----AVEGGYLRAT---TTPEPAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  91 AVVICVPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTRDLLVEPLRAR-GLT----VDE--DVYVAFA 163
Cdd:PRK11064  78 AFLIAVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARpDLTfpqqAGEqaDINIAYC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 164 PERIDPGNERHTPERTPRLVGGAGPRSSRAAADLLAPTASAVRTVPDPETAEMAKLWENTYRAVNIALANELADACHSLG 243
Cdd:PRK11064 158 PERVLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 244 LAPAPVIEAAATKPYGFMpFYPGPGVGGHCIPCDPHYLLWQlgkVRQQAPLVATALAANSRRP----ARITERALDLLAD 319
Cdd:PRK11064 238 INVWELIRLANRHPRVNI-LQPGPGVGGHCIAVDPWFIVAQ---NPQQARLIRTAREVNDGKPhwviDQVKAAVADCLAA 313

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 490071752 320 SAVPAHGARVLLIGVAYKEGVADVRESPALEILAGLAE 357
Cdd:PRK11064 314 TDKRASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQ 351
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
 213-302 7.20e-34

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: 122.10  E-value: 7.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  213 TAEMAKLWENTYRAVNIALANELADACHSLGLAPAPVIEAAATKPY-GFMPFYPGPGVGGHCIPCDPHYLLWQLGKVRQQ 291
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRiGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80

                          90
                  ....*....|.
gi 490071752  292 APLVATALAAN 302
Cdd:pfam00984  81 ARLLEAAREVN 91
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 330-419 1.09e-11

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: 60.98  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   330 LLIGVAYKEGVADVRESPALEILAGLAEAGAHVAYCDPLV-PSLRVGADALHHLPDPHTRPWDLVVLNTVHPV-HDLTW- 406
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAmEEAREYGLTYVSDLEEALKGADAVVIATEHDEfRSLDPe 80

                           90
                   ....*....|....*
gi 490071752   407 --LCADDAPPVLDTR 419
Cdd:smart00984  81 elKDLMKKPVVVDGR 95
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 17-134 4.25e-06

atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 48.09  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  17 VAVVGLGYVGLPTALALCDAGATVIGVDSSPERL-RDIARGAVDLlplhhaqlacasAGDrfrlTPDATAVRDADAVVIC 95
Cdd:cd05266    1 VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLaADRPAGVTPL------------AAD----LTQPGLLADVDHLVIS 64

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490071752  96 VPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTS 134
Cdd:cd05266   65 LPPPAGSYRGGYDPGLRALLDALAQLPAVQRVIYLSSTG 103
 
Name Accession Description Interval E-value
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 15-420 5.82e-160

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: 457.46  E-value: 5.82e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   15 PTVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRDIARGAVDL-LPLHHAQLACASAGDRFRLTPDAT-AVRDADAV 92
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIyEPGLDELLAKALKAGRLRATTDYEeAIRDADVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   93 VICVPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTRDLLVEPLRARGLTVDEDVYVAFAPERIDPGNE 172
Cdd:TIGR03026  81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYNPEFLREGNA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  173 RHTPERTPRLVGGAGPRSSRAAADLLAPTASAVRTVPDPETAEMAKLWENTYRAVNIALANELADACHSLGLAPAPVIEA 252
Cdd:TIGR03026 161 VHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  253 AATKPY-GFMPFYPGPGVGGHCIPCDPHYLLWQLGKVRQQAPLVATALAANSRRPARITERALDLLadsaVPAHGARVLL 331
Cdd:TIGR03026 241 AGTDPRiGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLL----GPLKGKTVLI 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  332 IGVAYKEGVADVRESPALEILAGLAEAGAHVAYCDPLVPSLRVGADALHHLPDPHTRPWDLVVLNTVHPV-HDLTWLCAD 410
Cdd:TIGR03026 317 LGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDLEEALKGADALVILTDHSEfKDLDLEKIK 396

                         410
                  ....*....|...
gi 490071752  411 D---APPVLDTRQ 420
Cdd:TIGR03026 397 DlmkGKVVVDTRN 409
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
16-419 2.18e-157

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 451.05  E-value: 2.18e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  16 TVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRDIARGAVDLLPLHHAQLACASAGDRFRLTPDATAVRDADAVVIC 95
Cdd:COG0677    1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGRLRATTDPEALAEADVVIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  96 VPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTRDLLVEPLRAR-GLTVDEDVYVAFAPERIDPGNERH 174
Cdd:COG0677   81 VPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRsGLKAGEDFFLAYSPERINPGNKLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 175 TPERTPRLVGGAGPRSSRAAADLLAPTASA-VRTVPDPETAEMAKLWENTYRAVNIALANELADACHSLGLAPAPVIEAA 253
Cdd:COG0677  161 ELRNIPKVVGGITPESAERAAALYGSVVTAgVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 254 ATKPyGFMPFYPGPGVGGHCIPCDPHYLLWQLGKVRQQAPLVATALAANSRRPARITERALDLLADSAVPAHGARVLLIG 333
Cdd:COG0677  241 NTKP-GFLIFYPGPGVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLVLG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 334 VAYKEGVADVRESPALEILAGLAEAGAHVAYCDPLVPSLRVGA--DALHHLpDPHTRPWDLVVLNTVHPV---HDLTWLC 408
Cdd:COG0677  320 LAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGeyGELVDL-EEALEGADAVVLAVDHDEfdeLDPEELR 398

                        410
                 ....*....|.
gi 490071752 409 ADDAPPVLDTR 419
Cdd:COG0677  399 LKGAKVVVDTR 409
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 16-357 8.41e-52

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 179.79  E-value: 8.41e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  16 TVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRDIARGAV-----DLLPLHHAqlacASAGDRFRLTpdaTAVRDAD 90
Cdd:PRK11064   5 TISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIhivepDLDMVVKT----AVEGGYLRAT---TTPEPAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  91 AVVICVPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTRDLLVEPLRAR-GLT----VDE--DVYVAFA 163
Cdd:PRK11064  78 AFLIAVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARpDLTfpqqAGEqaDINIAYC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 164 PERIDPGNERHTPERTPRLVGGAGPRSSRAAADLLAPTASAVRTVPDPETAEMAKLWENTYRAVNIALANELADACHSLG 243
Cdd:PRK11064 158 PERVLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 244 LAPAPVIEAAATKPYGFMpFYPGPGVGGHCIPCDPHYLLWQlgkVRQQAPLVATALAANSRRP----ARITERALDLLAD 319
Cdd:PRK11064 238 INVWELIRLANRHPRVNI-LQPGPGVGGHCIAVDPWFIVAQ---NPQQARLIRTAREVNDGKPhwviDQVKAAVADCLAA 313

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 490071752 320 SAVPAHGARVLLIGVAYKEGVADVRESPALEILAGLAE 357
Cdd:PRK11064 314 TDKRASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQ 351
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
10-374 1.58e-45

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 163.32  E-value: 1.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  10 FDVSGPTVAVVGLGYVGLPTALALCDAgATVIGVDSSPERLRDIARGAVDLLPLHHAQLACASagdRFRLTPDATAVRDA 89
Cdd:PRK15182   2 FGIDEVKIAIIGLGYVGLPLAVEFGKS-RQVVGFDVNKKRILELKNGVDVNLETTEEELREAR---YLKFTSEIEKIKEC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  90 DAVVICVPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTRDLLVePLRAR--GLTVDEDVYVAFAPERI 167
Cdd:PRK15182  78 NFYIITVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECV-PILARmsGMTFNQDFYVGYSPERI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 168 DPGNERHTPERTPRLVGGAGPRSSRAAADLLAPTASA-VRTVPDPETAEMAKLWENTYRAVNIALANELADACHSLGLAP 246
Cdd:PRK15182 157 NPGDKKHRLTNIKKITSGSTAQIAELIDEVYQQIISAgTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 247 APVIEAAATKpYGFMPFYPGPgVGGHCIPCDPHYLLWQLGKVRQQAPLVATALAANSRRPARITERALDLLADSAVPAHG 326
Cdd:PRK15182 237 EAVLRAAGSK-WNFLPFRPGL-VGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNMGNYVSEQLIKAMIKKGINVEG 314

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 490071752 327 ARVLLIGVAYKEGVADVRESPALEILAGLAEAGAHVAYCDPLVPSLRV 374
Cdd:PRK15182 315 SSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEV 362
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
17-367 1.02e-42

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 155.95  E-value: 1.02e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  17 VAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRDIARGAVdllPLH----HAQLACASAGDRFRLTPD-ATAVRDADA 91
Cdd:COG1004    3 IAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEI---PIYepglEELVARNVAAGRLRFTTDlAEAVAEADV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  92 VVICVPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTrDLLVEPLRARGLTVDEDVYVA---------- 161
Cdd:COG1004   80 VFIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTA-DRVRAIIAEELRGAGVDFDVVsnpeflregs 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 162 -----FAPERIdpgnerhtpertprLVGGAGPRSSRAAADLLAP-TASAVRTVP-DPETAEMAKLWENTYRAVNIALANE 234
Cdd:COG1004  159 avedfLRPDRI--------------VIGVDSERAAEVLRELYAPfVRNGTPIIVtDLRSAELIKYAANAFLATKISFINE 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 235 LADACHSLGlapAPVIEAAatkpYG----------FMpfYPGPGVGGHCIPCDPHYLLWQLGKVRQQAPLVATALAANSR 304
Cdd:COG1004  225 IANLCEKVG---ADVEEVA----RGigldsrigpkFL--YAGIGYGGSCFPKDVRALIATARELGYDLRLLEAVEEVNER 295

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490071752 305 RPARITERALDLLADSavpAHGARVLLIGVAYKEGVADVRESPALEILAGLAEAGAHVAYCDP 367
Cdd:COG1004  296 QKRRLVEKIREHLGGD---LKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDP 355
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
 213-302 7.20e-34

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: 122.10  E-value: 7.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  213 TAEMAKLWENTYRAVNIALANELADACHSLGLAPAPVIEAAATKPY-GFMPFYPGPGVGGHCIPCDPHYLLWQLGKVRQQ 291
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRiGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80

                          90
                  ....*....|.
gi 490071752  292 APLVATALAAN 302
Cdd:pfam00984  81 ARLLEAAREVN 91
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 16-195 9.28e-33

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: 122.36  E-value: 9.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   16 TVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRDIARGAvdlLPLHH---AQLACASAGDRFRLTPDA-TAVRDADA 91
Cdd:pfam03721   2 KISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQ---IPIYEpglDELVKANVSGRLSFTTDYsTAIEEADV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   92 VVICVPTPV-DARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTRDLLVEPLRARGLTVDEDVYVAFAPERIDPG 170
Cdd:pfam03721  79 IFIAVGTPSkKGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFDVASNPEFLREG 158

                         170       180
                  ....*....|....*....|....*
gi 490071752  171 NERHTPERTPRLVGGAGPRSSRAAA 195
Cdd:pfam03721 159 SAVYDLFNPDRVVIGVTEKCAEAAL 183
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
 17-369 5.35e-18

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 85.46  E-value: 5.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  17 VAVVGLGYVGLPTALaLCDAGATVIGVDSSPER---LRDIARGAVDllplHHAQLACASAGDRFRLTPD-ATAVRDADAV 92
Cdd:PRK15057   3 ITISGTGYVGLSNGL-LIAQNHEVVALDILPSRvamLNDRISPIVD----KEIQQFLQSDKIHFNATLDkNEAYRDADYV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  93 VICVPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTSYVGTTrdllvEPLRARGLTVDedvyVAFAPERIDPGNE 172
Cdd:PRK15057  78 IIATPTDYDPKTNYFNTSSVESVIKDVVEINPYAVMVIKSTVPVGFT-----AAMHKKYRTEN----IIFSPEFLREGKA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 173 RHTPERTPRLVggAGPRSSRAA--ADLLAPTASAvRTVP----DPETAEMAKLWENTYRAVNIALANELADACHSLGLAP 246
Cdd:PRK15057 149 LYDNLHPSRIV--IGERSERAErfAALLQEGAIK-QNIPtlftDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNT 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 247 APVIEAAATKP-YGFMPFYPGPGVGGHCIPCDPHYLLWQLGKVRQQapLVATALAANSRRPariteralDLLADSAVPAH 325
Cdd:PRK15057 226 RQIIEGVCLDPrIGNHYNNPSFGYGGYCLPKDTKQLLANYQSVPNN--LISAIVDANRTRK--------DFIADAILSRK 295

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 490071752 326 GARVLLIGVAYKEGVADVRESPALEILAGLAEAGAHVAYCDPLV 369
Cdd:PRK15057 296 PQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVM 339
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
 330-419 3.08e-13

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: 65.67  E-value: 3.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  330 LLIGVAYKEGVADVRESPALEILAGLAEAGAHVAYCDPLVPSLRVGA--DALHHLPDPHT--RPWDLVVLNTVHPV---H 402
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEAlgDGVTLVDDLEEalKGADAIVILTDHDEfksL 80

                          90
                  ....*....|....*...
gi 490071752  403 DLTWLCADDAPP-VLDTR 419
Cdd:pfam03720  81 DWEKLKKLMKPPvVFDGR 98
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 330-419 1.09e-11

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: 60.98  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   330 LLIGVAYKEGVADVRESPALEILAGLAEAGAHVAYCDPLV-PSLRVGADALHHLPDPHTRPWDLVVLNTVHPV-HDLTW- 406
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAmEEAREYGLTYVSDLEEALKGADAVVIATEHDEfRSLDPe 80

                           90
                   ....*....|....*
gi 490071752   407 --LCADDAPPVLDTR 419
Cdd:smart00984  81 elKDLMKKPVVVDGR 95
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 16-152 7.93e-09

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: 54.40  E-value: 7.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   16 TVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRD-IARGAVdllplhhaqlACASAGDrfrltpdatAVRDADAVVI 94
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEElVAAGAI----------AAASPAE---------FVAGLDVVIT 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 490071752   95 CVPTPVDARrrpdlaaLSAACASVVEHAVPGQLIVLTSTSYVGTTRDLLVEpLRARGL 152
Cdd:pfam03446  62 MVPAGAAVD-------AVIFGEGLLPGLKPGDIIIDGSTSSPEDARRRAKE-LKEKGL 111
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 15-152 9.76e-09

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 56.28  E-value: 9.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  15 PTVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRD-IARGAVdllplhhaqlACASAgdrfrltpdATAVRDADAVV 93
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEAlVAAGAR----------VAASP---------AEAAAAADVVI 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490071752  94 ICVPTPVDARRrpdlaaLSAACASVVEHAVPGQLIVLTSTSYVGTTRDlLVEPLRARGL 152
Cdd:COG2084   63 TMLPDDAAVEE------VLLGEDGLLAALRPGAVVVDMSTISPETARE-LAAAAAARGV 114
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
 16-369 5.22e-08

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 55.07  E-value: 5.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  16 TVAVVGLGYVGLPT--ALALCDAGATVIGVDSSPERlrdIARGAVDLLPLHHAQL-----ACASAgDRFRLTPDATAVRD 88
Cdd:PLN02353   3 KICCIGAGYVGGPTmaVIALKCPDIEVVVVDISVPR---IDAWNSDQLPIYEPGLdevvkQCRGK-NLFFSTDVEKHVAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  89 ADAVVICVPTPVDAR-----RRPDLAALSAACASVVEHAVPGQLIVLTSTSYV---------------GTTRDLLVEP-L 147
Cdd:PLN02353  79 ADIVFVSVNTPTKTRglgagKAADLTYWESAARMIADVSKSDKIVVEKSTVPVktaeaiekilthnskGINFQILSNPeF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 148 RARGlTVDEDVyvaFAPERIdpgnerhtpertprLVGGAGPRSSRAAADLLAPTASavRTVPDPE-------TAEMAKLW 220
Cdd:PLN02353 159 LAEG-TAIEDL---FKPDRV--------------LIGGRETPEGQKAVQALKDVYA--HWVPEERiittnlwSAELSKLA 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 221 ENTYRAVNIALANELADACHSLGLAPAPVIEAAATKPY---GFMPfyPGPGVGGHCIP---------CDPHYLlwqlgkv 288
Cdd:PLN02353 219 ANAFLAQRISSVNAMSALCEATGADVSQVSHAVGKDSRigpKFLN--ASVGFGGSCFQkdilnlvyiCECNGL------- 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752 289 rqqaPLVAT----ALAANSRRPARITERALDLLADSavpAHGARVLLIGVAYKEGVADVRESPALEILAGLAEAGAHVAY 364
Cdd:PLN02353 290 ----PEVAEywkqVIKMNDYQKSRFVNRVVSSMFNT---VSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSI 362


                 ....*
gi 490071752 365 CDPLV 369
Cdd:PLN02353 363 YDPQV 367
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 17-134 4.25e-06

atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 48.09  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  17 VAVVGLGYVGLPTALALCDAGATVIGVDSSPERL-RDIARGAVDLlplhhaqlacasAGDrfrlTPDATAVRDADAVVIC 95
Cdd:cd05266    1 VLILGCGYLGQRLARQLLAQGWQVTGTTRSPEKLaADRPAGVTPL------------AAD----LTQPGLLADVDHLVIS 64

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490071752  96 VPTPVDARRRPDLAALSAACASVVEHAVPGQLIVLTSTS 134
Cdd:cd05266   65 LPPPAGSYRGGYDPGLRALLDALAQLPAVQRVIYLSSTG 103
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 16-97 2.54e-05

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: 45.89  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  16 TVAVVGLGYVG--LptALALCDAGA--TVIGVDSSPERLRD-IARGAVDllplhhaqlacasagdrfRLTPD-ATAVRDA 89
Cdd:COG0287    3 RIAIIGLGLIGgsL--ALALKRAGLahEVVGVDRSPETLERaLELGVID------------------RAATDlEEAVADA 62


                 ....*...
gi 490071752  90 DAVVICVP 97
Cdd:COG0287   63 DLVVLAVP 70
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 10-93 2.57e-05

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. 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.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 46.10  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  10 FDVSGPTVAVVGLGYVGLPTALALCDAGA-TVIGVDSSPERLRDIARGAVDLLPLHHAQLAcasagdrfRLTPDATAVRD 88
Cdd:cd08284  164 QVRPGDTVAVIGCGPVGLCAVLSAQVLGAaRVFAVDPVPERLERAAALGAEPINFEDAEPV--------ERVREATEGRG 235


                 ....*
gi 490071752  89 ADAVV 93
Cdd:cd08284  236 ADVVL 240
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 14-84 1.42e-04

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members 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 includes various 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: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 43.72  E-value: 1.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490071752  14 GPTVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLrDIAR--GAVDLLPL----HHAQLACASAGDRFRLTPDAT 84
Cdd:cd08261  160 GDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERL-EFARelGADDTINVgdedVAARLRELTDGEGADVVIDAT 235
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 14-95 1.71e-04

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: 43.03  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  14 GPTVAVVGLGYVGLPTA-LALCDAGATVIGVDSSPERlRDIARGAVDLLPLHHAqlacasagdrfrlTPDATAVRDADAV 92
Cdd:cd08255   98 GERVAVVGLGLVGLLAAqLAKAAGAREVVGVDPDAAR-RELAEALGPADPVAAD-------------TADEIGGRGADVV 163


                 ...
gi 490071752  93 VIC 95
Cdd:cd08255  164 IEA 166
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 16-134 3.47e-04

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 41.37  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752   16 TVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRD----IARGAVDLLPLHHA-QLACASAGDRFRLTPDATAVRDAD 90
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKalerIESSLERLVEKGRItEEEVDAALARISFTTDLAAAVDAD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 490071752   91 AVVICVPTPVDARRRpdlaalsaaCASVVEHAVPGQLIVLTSTS 134
Cdd:pfam02737  81 LVIEAVPENLELKRK---------LFAELDAIAPPDAILATNTS 115
SQD1_like_SDR_e cd05255
UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) ...
 16-78 4.81e-04

UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) SDRs; Arabidopsis thaliana UDP-sulfoquinovose-synthase ( SQD1), an extended SDR, catalyzes the transfer of SO(3)(-) to UDP-glucose in the biosynthesis of plant sulfolipids. Members of this subgroup share the conserved SDR catalytic residues, and a partial match to the characteristic extended-SDR NAD-binding motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187565 [Multi-domain]  Cd Length: 382  Bit Score: 42.37  E-value: 4.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490071752  16 TVAVVGL-GYVGLPTALALCDAGATVIGVDSSPERLRDIARGAVDLLPLhhaqlacASAGDRFR 78
Cdd:cd05255    2 KVLILGGdGYCGWPTALHLSKRGHEVCIVDNLVRRRIDVELGLESLTPI-------ASIHERLR 58
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 14-101 5.69e-04

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 41.64  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  14 GPTVAVVGLGYVGLpTALALCDA-GATVIGVDSSPERLRDIAR-GAvdllplHHAQLacASAGDRFRLtpdATAVRDADA 91
Cdd:COG1064  163 GDRVAVIGAGGLGH-LAVQIAKAlGAEVIAVDRSPEKLELARElGA------DHVVN--SSDEDPVEA---VRELTGADV 230

                         90
                 ....*....|
gi 490071752  92 VVICVPTPVD 101
Cdd:COG1064  231 VIDTVGAPAT 240
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
21-153 9.82e-04

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 41.12  E-value: 9.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  21 GLGYVGLPTALALCDAGATVIGVDSSPERLRDIArgavDLLPLHHAQlacasaGDRFRLTPDATAVRDADAVVICVPTPV 100
Cdd:COG0451    7 GAGFIGSHLARRLLARGHEVVGLDRSPPGAANLA----ALPGVEFVR------GDLRDPEALAAALAGVDAVVHLAAPAG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490071752 101 DARRRPDLAALS--AACASVVEHAV--PGQLIVLTSTSYV-GTTRDLLVEPLRARGLT 153
Cdd:COG0451   77 VGEEDPDETLEVnvEGTLNLLEAARaaGVKRFVYASSSSVyGDGEGPIDEDTPLRPVS 134
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 14-99 1.65e-03

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have 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.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 40.34  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  14 GPTVAVVGLGYVGLPTAL-ALCDAGATVIGVDSSPERLrDIAR--GAVDLLPLHHAQLAcasagDRFRltpDATAVRDAD 90
Cdd:cd05278  168 GSTVAVIGAGPVGLCAVAgARLLGAARIIAVDSNPERL-DLAKeaGATDIINPKNGDIV-----EQIL---ELTGGRGVD 238


                 ....*....
gi 490071752  91 AVVICVPTP 99
Cdd:cd05278  239 CVIEAVGFE 247
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 14-99 2.68e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (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. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 39.61  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  14 GPTVAVVGLGYVGLPTALALCDAGATVIGVDSSPERLrDIAR--GAVDLLplhhaqlacASAGDRFRLTPDATAVRDADA 91
Cdd:cd05188  135 GDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKL-ELAKelGADHVI---------DYKEEDLEEELRLTGGGGADV 204


                 ....*...
gi 490071752  92 VVICVPTP 99
Cdd:cd05188  205 VIDAVGGP 212
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 14-99 2.74e-03

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: 39.74  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  14 GPTVAVVGLGYVGLPTALALCDAGA-TVIGVDSSPERLrDIAR--GAVDLLPLHHAQLAcasagDRFRltpDATAVRDAD 90
Cdd:COG1063  162 GDTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNPERL-ELARelGADAVVNPREEDLV-----EAVR---ELTGGRGAD 232


                 ....*....
gi 490071752  91 AVVICVPTP 99
Cdd:COG1063  233 VVIEAVGAP 241
GdhA COG0334
Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate ...
 11-46 2.77e-03

Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]; Glutamate dehydrogenase/leucine dehydrogenase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440103 [Multi-domain]  Cd Length: 411  Bit Score: 39.66  E-value: 2.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 490071752  11 DVSGPTVAVVGLGYVGLPTALALCDAGATVIGV-DSS 46
Cdd:COG0334  205 SLEGKTVAVQGFGNVGSYAAELLHELGAKVVAVsDSS 241
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 16-97 5.80e-03

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: 38.55  E-value: 5.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  16 TVAVVGLGYVGLPTALALCDAGATVIGVDSSPE-------RLRDIARGAVDLLPLHHAQLAcaSAGDRFRLTPDATAVRD 88
Cdd:COG1250    4 KVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEaleraraRIAKLLDKLVKKGKLTEEEAD--AALARITPTTDLAALAD 81


                 ....*....
gi 490071752  89 ADAVVICVP 97
Cdd:COG1250   82 ADLVIEAVP 90
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 17-97 6.09e-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: 38.51  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  17 VAVVGLGYVGLPTALALCDAGATVIGVDSSPERLRDIARGAVDLLPLHHAQLAC-ASAGdrfrltpdataVRDADAVVIC 95
Cdd:COG0569   98 VIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVlEEAG-----------IEDADAVIAA 166


                 ..
gi 490071752  96 VP 97
Cdd:COG0569  167 TG 168
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 13-61 6.86e-03

class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have 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. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 38.36  E-value: 6.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490071752  13 SGPTVAVVGLGYVGLPTALALCDAGAT-VIGVDSSPERLrDIAR--GAVDLL 61
Cdd:cd08300  186 PGSTVAVFGLGAVGLAVIQGAKAAGASrIIGIDINPDKF-ELAKkfGATDCV 236
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 14-95 8.31e-03

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. 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.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 38.38  E-value: 8.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  14 GPTVAVVGLGYVGL--PTALALCDAGaTVIGVDSSPERLrDIAR--GAVDLLPLHhaqlacasAGDRFRLTPDATAVRDA 89
Cdd:cd08285  167 GDTVAVFGIGPVGLmaVAGARLRGAG-RIIAVGSRPNRV-ELAKeyGATDIVDYK--------NGDVVEQILKLTGGKGV 236


                 ....*.
gi 490071752  90 DAVVIC 95
Cdd:cd08285  237 DAVIIA 242
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 14-100 8.95e-03

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: 37.98  E-value: 8.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490071752  14 GPTVAVVGLGYVGLPTALALCDAGAT-VIGVDSSPERLrDIARGAVdllplhhAQLACASAGDRFRLTPDATAVRDADAV 92
Cdd:cd08236  160 GDTVVVIGAGTIGLLAIQWLKILGAKrVIAVDIDDEKL-AVARELG-------ADDTINPKEEDVEKVRELTEGRGADLV 231


                 ....*...
gi 490071752  93 VICVPTPV 100
Cdd:cd08236  232 IEAAGSPA 239
 
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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