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Conserved domains on  [gi|494033510|ref|WP_006975643|]
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nucleotide sugar dehydrogenase [Plesiocystis pacifica]

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];
19-387 4.40e-86

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


:

Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 267.31  E-value: 4.40e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  19 RVVVMGLGYVGAPMA-ELARtAGFEVHGLEVDAERAAALTTEDCPT-------------------SLDPSVLDRAALILV 78
Cdd:COG0677    1 KIAVIGLGYVGLPLAvAFAK-AGFRVIGFDINPERVEELNAGEDPIlepgdellaeavaagrlraTTDPEALAEADVVII 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  79 CVPTPLDDAGQPDRGPVLEAAATIrahaGPRVR----VCLESTVDP----ELAARGFAAAAGLPLDQ---VAHAPERLDP 147
Cdd:COG0677   80 AVPTPLDEDKEPDLSYLESASETI----APHLKpgdlVVLESTVYPgtteEVCVPILEKRSGLKAGEdffLAYSPERINP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 148 GPASRPARDIPRVVGGCTPAATAWAADFYRA-LGLQVHE-TTAEVAALAKLNENAQRLVNVALVGELARLCRARGVDVDA 225
Cdd:COG0677  156 GNKLHELRNIPKVVGGITPESAERAAALYGSvVTAGVVPvSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 226 VIDACATKPfGYTPYRARAGAGGHCVPVDPVWLLDAARSEGAEFgvlraalaanraraaDIVDA----------FV---- 291
Cdd:COG0677  236 VIEAANTKP-GFLIFYPGPGVGGHCIPVDPYYLTWKARELGYHP---------------RLILAareindsmpeYVverv 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 292 -------HTAPEARRVLVLGAAYKPGVGDTRESPAQPIALALAARGLEVRVHDPLTGGLS----PYPATTLEDALPWAEA 360
Cdd:COG0677  300 vkalneaGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEvegeYGELVDLEEALEGADA 379

                        410       420       430
                 ....*....|....*....|....*....|.
gi 494033510 361 ILALTVH---DAMPVEALSRFPGP-IVDACG 387
Cdd:COG0677  380 VVLAVDHdefDELDPEELRLKGAKvVVDTRG 410
 
Name Accession Description Interval E-value
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
19-387 4.40e-86

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 267.31  E-value: 4.40e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  19 RVVVMGLGYVGAPMA-ELARtAGFEVHGLEVDAERAAALTTEDCPT-------------------SLDPSVLDRAALILV 78
Cdd:COG0677    1 KIAVIGLGYVGLPLAvAFAK-AGFRVIGFDINPERVEELNAGEDPIlepgdellaeavaagrlraTTDPEALAEADVVII 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  79 CVPTPLDDAGQPDRGPVLEAAATIrahaGPRVR----VCLESTVDP----ELAARGFAAAAGLPLDQ---VAHAPERLDP 147
Cdd:COG0677   80 AVPTPLDEDKEPDLSYLESASETI----APHLKpgdlVVLESTVYPgtteEVCVPILEKRSGLKAGEdffLAYSPERINP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 148 GPASRPARDIPRVVGGCTPAATAWAADFYRA-LGLQVHE-TTAEVAALAKLNENAQRLVNVALVGELARLCRARGVDVDA 225
Cdd:COG0677  156 GNKLHELRNIPKVVGGITPESAERAAALYGSvVTAGVVPvSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 226 VIDACATKPfGYTPYRARAGAGGHCVPVDPVWLLDAARSEGAEFgvlraalaanraraaDIVDA----------FV---- 291
Cdd:COG0677  236 VIEAANTKP-GFLIFYPGPGVGGHCIPVDPYYLTWKARELGYHP---------------RLILAareindsmpeYVverv 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 292 -------HTAPEARRVLVLGAAYKPGVGDTRESPAQPIALALAARGLEVRVHDPLTGGLS----PYPATTLEDALPWAEA 360
Cdd:COG0677  300 vkalneaGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEvegeYGELVDLEEALEGADA 379

                        410       420       430
                 ....*....|....*....|....*....|.
gi 494033510 361 ILALTVH---DAMPVEALSRFPGP-IVDACG 387
Cdd:COG0677  380 VVLAVDHdefDELDPEELRLKGAKvVVDTRG 410
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 19-380 1.93e-70

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: 227.11  E-value: 1.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510   19 RVVVMGLGYVGAPMAELARTAGFEVHGLEVDAERAAALTTEDCP---------------------TSLDPSVLDRAALIL 77
Cdd:TIGR03026   2 KIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPiyepgldellakalkagrlraTTDYEEAIRDADVII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510   78 VCVPTPLDDAGQPDRGPVLEAAATIRAHAGPRVRVCLESTVDP---ELAARGFAAAAGLPLDQ---VAHAPERLDPGPAS 151
Cdd:TIGR03026  82 ICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPgttEEVVKPILERSGLKLGEdfyLAYNPEFLREGNAV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  152 RPARDIPRVVGGCTPAATAWAADFYRAL-GLQVHETTAEVAALAKLNENAQRLVNVALVGELARLCRARGVDVDAVIDAC 230
Cdd:TIGR03026 162 HDLLHPDRIVGGETEEAGEAVAELYSPIiDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEAA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  231 ATKPF-GYTPYRARAGAGGHCVPVDPVWLLDAARSEGAEF----GVLRAALAANRARAADIVDAFVHTAPeaRRVLVLGA 305
Cdd:TIGR03026 242 GTDPRiGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPelieAAREINDSQPDYVVEKIKDLLGPLKG--KTVLILGL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  306 AYKPGVGDTRESPAQPIALALAARGLEVRVHDPLT-----GGLSPYPatTLEDALPWAEAILALTVHDAMPVEALSRFPG 380
Cdd:TIGR03026 320 AFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVpeeevKGLPSID--DLEEALKGADALVILTDHSEFKDLDLEKIKD 397
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
17-338 9.42e-23

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 99.38  E-value: 9.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  17 DARVVVMGLGYVGAPMA-ELARTAgfEVHGLEVDAERAAAL---------TTED-------CPTSLDPSVLDRAALILVC 79
Cdd:PRK15182   6 EVKIAIIGLGYVGLPLAvEFGKSR--QVVGFDVNKKRILELkngvdvnleTTEEelrearyLKFTSEIEKIKECNFYIIT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  80 VPTPLDDAGQPDRGPVLEAAATIRAHAGPRVRVCLESTVDP----ELAARGFAAAAGLPLDQ---VAHAPERLDPGPASR 152
Cdd:PRK15182  84 VPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPgcteEECVPILARMSGMTFNQdfyVGYSPERINPGDKKH 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 153 PARDIPRVVGGCTPAATAWAADFYRAL---GLQVHETTaEVAALAKLNENAQRLVNVALVGELARLCRARGVDVDAVIDA 229
Cdd:PRK15182 164 RLTNIKKITSGSTAQIAELIDEVYQQIisaGTYKAESI-KVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEAVLRA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 230 CATKpFGYTPYRArAGAGGHCVPVDPVWLLDAARSEGAEFGVLRAALAANRARAADIVDAFVHTA------PEARRVLVL 303
Cdd:PRK15182 243 AGSK-WNFLPFRP-GLVGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNMGNYVSEQLIKAMikkginVEGSSVLIL 320

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 494033510 304 GAAYKPGVGDTRESPAQPIALALAARGLEVRVHDP 338
Cdd:PRK15182 321 GFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDP 355
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
 187-269 5.56e-20

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: 83.97  E-value: 5.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  187 TAEvaaLAKLNENAQRLVNVALVGELARLCRARGVDVDAVIDACATKPF-GYTPYRARAGAGGHCVPVDPVWLLDAARSE 265
Cdd:pfam00984   1 SAE---LIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRiGPKFLYPGPGVGGSCLPKDPRALIYLAREL 77


                  ....
gi 494033510  266 GAEF 269
Cdd:pfam00984  78 GVPA 81
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 301-387 1.33e-15

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: 71.77  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510   301 LVLGAAYKPGVGDTRESPAQPIALALAARGLEVRVHDPL----TGGLSPYPATTLEDALPWAEAILALTVHD---AMPVE 373
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYameeAREYGLTYVSDLEEALKGADAVVIATEHDefrSLDPE 80

                           90
                   ....*....|....*.
gi 494033510   374 ALSRF--PGPIVDACG 387
Cdd:smart00984  81 ELKDLmkKPVVVDGRN 96
 
Name Accession Description Interval E-value
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
19-387 4.40e-86

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 267.31  E-value: 4.40e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  19 RVVVMGLGYVGAPMA-ELARtAGFEVHGLEVDAERAAALTTEDCPT-------------------SLDPSVLDRAALILV 78
Cdd:COG0677    1 KIAVIGLGYVGLPLAvAFAK-AGFRVIGFDINPERVEELNAGEDPIlepgdellaeavaagrlraTTDPEALAEADVVII 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  79 CVPTPLDDAGQPDRGPVLEAAATIrahaGPRVR----VCLESTVDP----ELAARGFAAAAGLPLDQ---VAHAPERLDP 147
Cdd:COG0677   80 AVPTPLDEDKEPDLSYLESASETI----APHLKpgdlVVLESTVYPgtteEVCVPILEKRSGLKAGEdffLAYSPERINP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 148 GPASRPARDIPRVVGGCTPAATAWAADFYRA-LGLQVHE-TTAEVAALAKLNENAQRLVNVALVGELARLCRARGVDVDA 225
Cdd:COG0677  156 GNKLHELRNIPKVVGGITPESAERAAALYGSvVTAGVVPvSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 226 VIDACATKPfGYTPYRARAGAGGHCVPVDPVWLLDAARSEGAEFgvlraalaanraraaDIVDA----------FV---- 291
Cdd:COG0677  236 VIEAANTKP-GFLIFYPGPGVGGHCIPVDPYYLTWKARELGYHP---------------RLILAareindsmpeYVverv 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 292 -------HTAPEARRVLVLGAAYKPGVGDTRESPAQPIALALAARGLEVRVHDPLTGGLS----PYPATTLEDALPWAEA 360
Cdd:COG0677  300 vkalneaGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEvegeYGELVDLEEALEGADA 379

                        410       420       430
                 ....*....|....*....|....*....|.
gi 494033510 361 ILALTVH---DAMPVEALSRFPGP-IVDACG 387
Cdd:COG0677  380 VVLAVDHdefDELDPEELRLKGAKvVVDTRG 410
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 19-380 1.93e-70

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: 227.11  E-value: 1.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510   19 RVVVMGLGYVGAPMAELARTAGFEVHGLEVDAERAAALTTEDCP---------------------TSLDPSVLDRAALIL 77
Cdd:TIGR03026   2 KIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPiyepgldellakalkagrlraTTDYEEAIRDADVII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510   78 VCVPTPLDDAGQPDRGPVLEAAATIRAHAGPRVRVCLESTVDP---ELAARGFAAAAGLPLDQ---VAHAPERLDPGPAS 151
Cdd:TIGR03026  82 ICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPgttEEVVKPILERSGLKLGEdfyLAYNPEFLREGNAV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  152 RPARDIPRVVGGCTPAATAWAADFYRAL-GLQVHETTAEVAALAKLNENAQRLVNVALVGELARLCRARGVDVDAVIDAC 230
Cdd:TIGR03026 162 HDLLHPDRIVGGETEEAGEAVAELYSPIiDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEAA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  231 ATKPF-GYTPYRARAGAGGHCVPVDPVWLLDAARSEGAEF----GVLRAALAANRARAADIVDAFVHTAPeaRRVLVLGA 305
Cdd:TIGR03026 242 GTDPRiGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPelieAAREINDSQPDYVVEKIKDLLGPLKG--KTVLILGL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  306 AYKPGVGDTRESPAQPIALALAARGLEVRVHDPLT-----GGLSPYPatTLEDALPWAEAILALTVHDAMPVEALSRFPG 380
Cdd:TIGR03026 320 AFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVpeeevKGLPSID--DLEEALKGADALVILTDHSEFKDLDLEKIKD 397
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
17-338 9.42e-23

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 99.38  E-value: 9.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  17 DARVVVMGLGYVGAPMA-ELARTAgfEVHGLEVDAERAAAL---------TTED-------CPTSLDPSVLDRAALILVC 79
Cdd:PRK15182   6 EVKIAIIGLGYVGLPLAvEFGKSR--QVVGFDVNKKRILELkngvdvnleTTEEelrearyLKFTSEIEKIKECNFYIIT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  80 VPTPLDDAGQPDRGPVLEAAATIRAHAGPRVRVCLESTVDP----ELAARGFAAAAGLPLDQ---VAHAPERLDPGPASR 152
Cdd:PRK15182  84 VPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPgcteEECVPILARMSGMTFNQdfyVGYSPERINPGDKKH 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 153 PARDIPRVVGGCTPAATAWAADFYRAL---GLQVHETTaEVAALAKLNENAQRLVNVALVGELARLCRARGVDVDAVIDA 229
Cdd:PRK15182 164 RLTNIKKITSGSTAQIAELIDEVYQQIisaGTYKAESI-KVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEAVLRA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 230 CATKpFGYTPYRArAGAGGHCVPVDPVWLLDAARSEGAEFGVLRAALAANRARAADIVDAFVHTA------PEARRVLVL 303
Cdd:PRK15182 243 AGSK-WNFLPFRP-GLVGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNMGNYVSEQLIKAMikkginVEGSSVLIL 320

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 494033510 304 GAAYKPGVGDTRESPAQPIALALAARGLEVRVHDP 338
Cdd:PRK15182 321 GFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDP 355
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
19-365 1.30e-22

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 98.94  E-value: 1.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  19 RVVVMGLGYVGAP----MAELartaGFEVHGLEVDAERAAALTTEDCP----------------------TSLDPSVLDr 72
Cdd:COG1004    2 KIAVIGTGYVGLVtaacLAEL----GHEVTCVDIDEEKIEALNAGEIPiyepgleelvarnvaagrlrftTDLAEAVAE- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  73 AALILVCVPTPLDDAGQPDRGPVLEAAATIRAHAGPRVRVCLESTVDP----ELAARGFAAAAGLPLD-QVAHAPERLDP 147
Cdd:COG1004   77 ADVVFIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVgtadRVRAIIAEELRGAGVDfDVVSNPEFLRE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 148 GPA----SRPARdIprVVGGCTPAATAWAADFYRALGLQ---VHETTAEVAALAKLNEN---AQRlvnVALVGELARLCR 217
Cdd:COG1004  157 GSAvedfLRPDR-I--VIGVDSERAAEVLRELYAPFVRNgtpIIVTDLRSAELIKYAANaflATK---ISFINEIANLCE 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 218 ARGVDVDAVIDACATKP-FGYTPYRARAGAGGHCVPVDPVWLLDAARSEGAEFgvlraalaanraraaDIVDA------- 289
Cdd:COG1004  231 KVGADVEEVARGIGLDSrIGPKFLYAGIGYGGSCFPKDVRALIATARELGYDL---------------RLLEAveevner 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 290 ----FVHTAPEA-------RRVLVLGAAYKPGVGDTRESPAQPIALALAARGLEVRVHDP---------LTGGLSpYpAT 349
Cdd:COG1004  296 qkrrLVEKIREHlggdlkgKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPvamenarrlLPDDIT-Y-AD 373

                        410
                 ....*....|....*.
gi 494033510 350 TLEDALPWAEAILALT 365
Cdd:COG1004  374 DAYEALEGADALVILT 389
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
 187-269 5.56e-20

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: 83.97  E-value: 5.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  187 TAEvaaLAKLNENAQRLVNVALVGELARLCRARGVDVDAVIDACATKPF-GYTPYRARAGAGGHCVPVDPVWLLDAARSE 265
Cdd:pfam00984   1 SAE---LIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRiGPKFLYPGPGVGGSCLPKDPRALIYLAREL 77


                  ....
gi 494033510  266 GAEF 269
Cdd:pfam00984  78 GVPA 81
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 19-367 2.27e-19

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 89.27  E-value: 2.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  19 RVVVMGLGYVGAPMAELARTAGFEVHGLEVDAE------RAAALTTEdcpTSLDPSVLD-------RAALI-------LV 78
Cdd:PRK11064   5 TISVIGLGYIGLPTAAAFASRQKQVIGVDINQHavdtinRGEIHIVE---PDLDMVVKTaveggylRATTTpepadafLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  79 CVPTPLDDAGQPDRGPVLEAAATIRAHAGPRVRVCLESTvDP-----ELAARGFAAAAGLPLDQ---------VAHAPER 144
Cdd:PRK11064  82 AVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILEST-SPvgateQMAEWLAEARPDLTFPQqageqadinIAYCPER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 145 LDPGPASRPARDIPRVVGGCTPAATAWAADFYRAL--GLQVhETTAEVAALAKLNENAQRLVNVALVGELARLCRARGVD 222
Cdd:PRK11064 161 VLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFleGECV-VTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGIN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 223 VDAVIDACATKPfgytpyRAR-----AGAGGHCVPVDPvW-----------LLDAAR--SEGAEFGVLRAALAAnraraa 284
Cdd:PRK11064 240 VWELIRLANRHP------RVNilqpgPGVGGHCIAVDP-WfivaqnpqqarLIRTARevNDGKPHWVIDQVKAA------ 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 285 dIVDAFVHTAPEARRVLV--LGAAYKPGVGDTRESPAQPIALALAARGL-EVRVHDP--------LTGGLspyPATTLED 353
Cdd:PRK11064 307 -VADCLAATDKRASEVKIacFGLAFKPNIDDLRESPAMEIAELIAQWHSgETLVVEPnihqlpkkLDGLV---TLVSLDE 382

                        410
                 ....*....|....
gi 494033510 354 ALPWAEAILALTVH 367
Cdd:PRK11064 383 ALATADVLVMLVDH 396
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 18-173 7.55e-16

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: 74.98  E-value: 7.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510   18 ARVVVMGLGYVGAP-MAELARtAGFEVHGLEVDAERAAALTTEDCPT-------------------SLD-PSVLDRAALI 76
Cdd:pfam03721   1 MKISVIGLGYVGLPtAACLAE-IGHDVIGVDIDEEKVDKLNSGQIPIyepgldelvkanvsgrlsfTTDySTAIEEADVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510   77 LVCVPTPLDDAG-QPDRGPVLEAAATIRAHAGPRVRVCLESTV-----DPELAARGFAAAAGLPLD-QVAHAPERLDPGP 149
Cdd:pfam03721  80 FIAVGTPSKKGGgAADLKYVESAARSIAPHLKKGKVVVVKSTVpvgttENLVKPIIEEGGKKVGVDfDVASNPEFLREGS 159

                         170       180
                  ....*....|....*....|....
gi 494033510  150 ASRPARDIPRVVGGCTPAATAWAA 173
Cdd:pfam03721 160 AVYDLFNPDRVVIGVTEKCAEAAL 183
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 301-387 1.33e-15

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: 71.77  E-value: 1.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510   301 LVLGAAYKPGVGDTRESPAQPIALALAARGLEVRVHDPL----TGGLSPYPATTLEDALPWAEAILALTVHD---AMPVE 373
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYameeAREYGLTYVSDLEEALKGADAVVIATEHDefrSLDPE 80

                           90
                   ....*....|....*.
gi 494033510   374 ALSRF--PGPIVDACG 387
Cdd:smart00984  81 ELKDLmkKPVVVDGRN 96
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
 301-368 4.87e-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: 64.90  E-value: 4.87e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494033510  301 LVLGAAYKPGVGDTRESPAQPIALALAARGLEVRVHDPLT-------GGLSPYPATTLEDALPWAEAILALTVHD 368
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVpeeaieaLGDGVTLVDDLEEALKGADAIVILTDHD 75
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
 191-338 7.83e-04

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 41.59  E-value: 7.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510 191 AALAKLNENA---QRlvnVALVGELARLCRARGVDVDAVIDACATKP-FGYTPYRARAGAGGHCVPVDPVWLLDAARSEG 266
Cdd:PLN02353 212 AELSKLAANAflaQR---ISSVNAMSALCEATGADVSQVSHAVGKDSrIGPKFLNASVGFGGSCFQKDILNLVYICECNG 288

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494033510 267 ----AEF--GVLRAALAANRARAADIVDAFVHTApEARRVLVLGAAYKPGVGDTRESPAQPIALALAARGLEVRVHDP 338
Cdd:PLN02353 289 lpevAEYwkQVIKMNDYQKSRFVNRVVSSMFNTV-SGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDP 365
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 2-73 1.63e-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: 40.05  E-value: 1.63e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494033510   2 RSFAPAKSPRRPRQADARVVVMGLGYVGAPMAELARTAGFEVHGLEVDAERAAALTTEDCPT----SLDPSVLDRA 73
Cdd:COG0569   80 EALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVivgdATDEEVLEEA 155
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 18-229 4.47e-03

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 38.56  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  18 ARVVVMGLGYVGAPMAELARTAGFEVHGLEVDAERAAALTTEDCPTSLDPS-VLDRAALILVCVPTPlDDAGQpdrgpVL 96
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAeAAAAADVVITMLPDD-AAVEE-----VL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494033510  97 EAAATIRAHAGPRVRVCLESTVDPELAARGFAAAAGLPLDQVaHAPerldpgpasrpardiprVVGGCTPAATA------ 170
Cdd:COG2084   76 LGEDGLLAALRPGAVVVDMSTISPETARELAAAAAARGVRYL-DAP-----------------VSGGPAGAEAGtltimv 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494033510 171 --WAADFYRALGL-------QVHETTAEVAALAKLNENAQRLVNVALVGELARLCRARGVDVDAVIDA 229
Cdd:COG2084  138 ggDEAAFERARPVleamgkrIVHVGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEV 205
 
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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