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Conserved domains on  [gi|2580540099|ref|WP_310893745|]
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MULTISPECIES: nucleotide sugar dehydrogenase [unclassified Haloferax]

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];
29-437 2.66e-180

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


:

Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 510.76  E-value: 2.66e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVaKEPGlPELVAEQAERGALRATTDGVAAAEsAAIHV 108
Cdd:COG0677     2 IAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPI-LEPG-DELLAEAVAAGRLRATTDPEALAE-ADVVI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 109 IIVPTPLTDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKDLVVPYLADRSGLSAGE-FGVAFCPERTSSGRA 187
Cdd:COG0677    79 IAVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAGEdFFLAYSPERINPGNK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 188 LRDItESHPKIVGGVDAESTRVAALVYGEITSNEVIPVRDATTAEAVKLFEGVYRDVNIALANELARLRDDLGIDVTEAI 267
Cdd:COG0677   159 LHEL-RNIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 268 DAANTQPYCDIHAPGPGVGGHCIPWYPYFITSRVEA---ETPLLLTAREVNDSMPAFTADKLRDELAAAGREIRGATVAV 344
Cdd:COG0677   238 EAANTKPGFLIFYPGPGVGGHCIPVDPYYLTWKARElgyHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLV 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 345 LGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSDEVVASFGATPVALaDLPTRAIDAAVVVTPHEEFDGIDWAA 424
Cdd:COG0677   318 LGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYGELVDL-EEALEGADAVVLAVDHDEFDELDPEE 396

                         410
                  ....*....|....*.
gi 2580540099 425 F---DDLVVVDGRGTL 437
Cdd:COG0677   397 LrlkGAKVVVDTRGVL 412
 
Name Accession Description Interval E-value
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
29-437 2.66e-180

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 510.76  E-value: 2.66e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVaKEPGlPELVAEQAERGALRATTDGVAAAEsAAIHV 108
Cdd:COG0677     2 IAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPI-LEPG-DELLAEAVAAGRLRATTDPEALAE-ADVVI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 109 IIVPTPLTDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKDLVVPYLADRSGLSAGE-FGVAFCPERTSSGRA 187
Cdd:COG0677    79 IAVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAGEdFFLAYSPERINPGNK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 188 LRDItESHPKIVGGVDAESTRVAALVYGEITSNEVIPVRDATTAEAVKLFEGVYRDVNIALANELARLRDDLGIDVTEAI 267
Cdd:COG0677   159 LHEL-RNIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 268 DAANTQPYCDIHAPGPGVGGHCIPWYPYFITSRVEA---ETPLLLTAREVNDSMPAFTADKLRDELAAAGREIRGATVAV 344
Cdd:COG0677   238 EAANTKPGFLIFYPGPGVGGHCIPVDPYYLTWKARElgyHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLV 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 345 LGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSDEVVASFGATPVALaDLPTRAIDAAVVVTPHEEFDGIDWAA 424
Cdd:COG0677   318 LGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYGELVDL-EEALEGADAVVLAVDHDEFDELDPEE 396

                         410
                  ....*....|....*.
gi 2580540099 425 F---DDLVVVDGRGTL 437
Cdd:COG0677   397 LrlkGAKVVVDTRGVL 412
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 29-435 6.65e-130

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: 382.34  E-value: 6.65e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVaKEPGLPELVAEQAERGALRATTDGVAAAESAAIHV 108
Cdd:TIGR03026   3 IAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPI-YEPGLDELLAKALKAGRLRATTDYEEAIRDADVII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 109 IIVPTPLTDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKDLVVPYLAdRSGLSAGE-FGVAFCPERTSSGRA 187
Cdd:TIGR03026  82 ICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILE-RSGLKLGEdFYLAYNPEFLREGNA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 188 LRDITEShPKIVGGVDAESTRVAALVYGEITSNeVIPVRDATTAEAVKLFEGVYRDVNIALANELARLRDDLGIDVTEAI 267
Cdd:TIGR03026 161 VHDLLHP-DRIVGGETEEAGEAVAELYSPIIDG-PVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 268 DAANTQPY--CDIHAPGPGVGGHCIPWYPYFITSRVE---AETPLLLTAREVNDSMPAFTADKLRDELAAAGreirGATV 342
Cdd:TIGR03026 239 EAAGTDPRigFNFLNPGPGVGGHCIPKDPLALIAKAKelgYNPELIEAAREINDSQPDYVVEKIKDLLGPLK----GKTV 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 343 AVLGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSDEVVASFGATPVALADLPTraIDAAVVVTPHEEFDGIDW 422
Cdd:TIGR03026 315 LILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDLEEALKG--ADALVILTDHSEFKDLDL 392

                         410
                  ....*....|....*..
gi 2580540099 423 AAFDDL----VVVDGRG 435
Cdd:TIGR03026 393 EKIKDLmkgkVVVDTRN 409
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 29-432 4.10e-82

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 259.92  E-value: 4.10e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVAkEPGLPELVAEQAERGALRATTdgvaAAESAAIHV 108
Cdd:PRK11064    6 ISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIV-EPDLDMVVKTAVEGGYLRATT----TPEPADAFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 109 IIVPTPLTDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKDLVVPYLADRSGLS----AGE---FGVAFCPER 181
Cdd:PRK11064   81 IAVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTfpqqAGEqadINIAYCPER 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 182 TSSGRALRDITESHpKIVGGVDAESTRVAALVYGEITSNEVIpVRDATTAEAVKLFEGVYRDVNIALANELARLRDDLGI 261
Cdd:PRK11064  161 VLPGQVMVELIKND-RVIGGMTPVCSARASELYKIFLEGECV-VTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 262 DVTEAIDAANTQPYCDIHAPGPGVGGHCIPWYPYFITSRVEAETPLLLTAREVNDSMPAFTADKLR----DELAAAGREI 337
Cdd:PRK11064  239 NVWELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKaavaDCLAATDKRA 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 338 RGATVAVLGVTYRPGVAETRATPAAGVIDRLNDL-GATVLAVDPMLSDEVVASFG-ATPVALADLPTRAiDAAVVVTPHE 415
Cdd:PRK11064  319 SEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWhSGETLVVEPNIHQLPKKLDGlVTLVSLDEALATA-DVLVMLVDHS 397

                         410
                  ....*....|....*..
gi 2580540099 416 EFDGIDWAAFDDLVVVD 432
Cdd:PRK11064  398 QFKAINGDNVHQQWVVD 414
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 29-211 4.60e-42

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: 147.78  E-value: 4.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVAkEPGLPELVaEQAERGALRATTDGVAAAESAAIHV 108
Cdd:pfam03721   3 ISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIY-EPGLDELV-KANVSGRLSFTTDYSTAIEEADVIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 109 IIVPTPL-TDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKDLVVPYLADRSGLSAGEFGVAFCPERTSSGRA 187
Cdd:pfam03721  81 IAVGTPSkKGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFDVASNPEFLREGSA 160

                         170       180
                  ....*....|....*....|....
gi 2580540099 188 LRDiTESHPKIVGGVDAESTRVAA 211
Cdd:pfam03721 161 VYD-LFNPDRVVIGVTEKCAEAAL 183
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 343-437 1.23e-17

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: 77.93  E-value: 1.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  343 AVLGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSdEVVASFGATPVALADLPTRAIDAAVVVTPHEEFDGIDW 422
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAM-EEAREYGLTYVSDLEEALKGADAVVIATEHDEFRSLDP 79

                           90
                   ....*....|....*....
gi 2580540099  423 AAFDDL----VVVDGRGTL 437
Cdd:smart00984  80 EELKDLmkkpVVVDGRNIL 98
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 303-404 4.73e-03

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


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 38.84  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 303 AETPLLLTAREVNDSMPAFTADKLRDELAAAGREIRGATVAVLGVtyrpG-----VAETRAtpaagvidrlNDLGATVLA 377
Cdd:cd12177   111 AVALILTVLRKINQASEAVKEGKWTERANFVGHELSGKTVGIIGY----GnigsrVAEILK----------EGFNAKVLA 176

                          90       100
                  ....*....|....*....|....*..
gi 2580540099 378 VDPMLSDEVVASFGATPVALADLPTRA 404
Cdd:cd12177   177 YDPYVSEEVIKKKGAKPVSLEELLAES 203
 
Name Accession Description Interval E-value
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
29-437 2.66e-180

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


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 510.76  E-value: 2.66e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVaKEPGlPELVAEQAERGALRATTDGVAAAEsAAIHV 108
Cdd:COG0677     2 IAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPI-LEPG-DELLAEAVAAGRLRATTDPEALAE-ADVVI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 109 IIVPTPLTDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKDLVVPYLADRSGLSAGE-FGVAFCPERTSSGRA 187
Cdd:COG0677    79 IAVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAGEdFFLAYSPERINPGNK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 188 LRDItESHPKIVGGVDAESTRVAALVYGEITSNEVIPVRDATTAEAVKLFEGVYRDVNIALANELARLRDDLGIDVTEAI 267
Cdd:COG0677   159 LHEL-RNIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 268 DAANTQPYCDIHAPGPGVGGHCIPWYPYFITSRVEA---ETPLLLTAREVNDSMPAFTADKLRDELAAAGREIRGATVAV 344
Cdd:COG0677   238 EAANTKPGFLIFYPGPGVGGHCIPVDPYYLTWKARElgyHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLV 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 345 LGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSDEVVASFGATPVALaDLPTRAIDAAVVVTPHEEFDGIDWAA 424
Cdd:COG0677   318 LGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYGELVDL-EEALEGADAVVLAVDHDEFDELDPEE 396

                         410
                  ....*....|....*.
gi 2580540099 425 F---DDLVVVDGRGTL 437
Cdd:COG0677   397 LrlkGAKVVVDTRGVL 412
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 29-435 6.65e-130

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: 382.34  E-value: 6.65e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVaKEPGLPELVAEQAERGALRATTDGVAAAESAAIHV 108
Cdd:TIGR03026   3 IAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPI-YEPGLDELLAKALKAGRLRATTDYEEAIRDADVII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 109 IIVPTPLTDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKDLVVPYLAdRSGLSAGE-FGVAFCPERTSSGRA 187
Cdd:TIGR03026  82 ICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILE-RSGLKLGEdFYLAYNPEFLREGNA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 188 LRDITEShPKIVGGVDAESTRVAALVYGEITSNeVIPVRDATTAEAVKLFEGVYRDVNIALANELARLRDDLGIDVTEAI 267
Cdd:TIGR03026 161 VHDLLHP-DRIVGGETEEAGEAVAELYSPIIDG-PVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 268 DAANTQPY--CDIHAPGPGVGGHCIPWYPYFITSRVE---AETPLLLTAREVNDSMPAFTADKLRDELAAAGreirGATV 342
Cdd:TIGR03026 239 EAAGTDPRigFNFLNPGPGVGGHCIPKDPLALIAKAKelgYNPELIEAAREINDSQPDYVVEKIKDLLGPLK----GKTV 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 343 AVLGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSDEVVASFGATPVALADLPTraIDAAVVVTPHEEFDGIDW 422
Cdd:TIGR03026 315 LILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDLEEALKG--ADALVILTDHSEFKDLDL 392

                         410
                  ....*....|....*..
gi 2580540099 423 AAFDDL----VVVDGRG 435
Cdd:TIGR03026 393 EKIKDLmkgkVVVDTRN 409
wecC PRK11064
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
 29-432 4.10e-82

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


Pssm-ID: 182940 [Multi-domain]  Cd Length: 415  Bit Score: 259.92  E-value: 4.10e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVAkEPGLPELVAEQAERGALRATTdgvaAAESAAIHV 108
Cdd:PRK11064    6 ISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIV-EPDLDMVVKTAVEGGYLRATT----TPEPADAFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 109 IIVPTPLTDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKDLVVPYLADRSGLS----AGE---FGVAFCPER 181
Cdd:PRK11064   81 IAVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTfpqqAGEqadINIAYCPER 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 182 TSSGRALRDITESHpKIVGGVDAESTRVAALVYGEITSNEVIpVRDATTAEAVKLFEGVYRDVNIALANELARLRDDLGI 261
Cdd:PRK11064  161 VLPGQVMVELIKND-RVIGGMTPVCSARASELYKIFLEGECV-VTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 262 DVTEAIDAANTQPYCDIHAPGPGVGGHCIPWYPYFITSRVEAETPLLLTAREVNDSMPAFTADKLR----DELAAAGREI 337
Cdd:PRK11064  239 NVWELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKaavaDCLAATDKRA 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 338 RGATVAVLGVTYRPGVAETRATPAAGVIDRLNDL-GATVLAVDPMLSDEVVASFG-ATPVALADLPTRAiDAAVVVTPHE 415
Cdd:PRK11064  319 SEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWhSGETLVVEPNIHQLPKKLDGlVTLVSLDEALATA-DVLVMLVDHS 397

                         410
                  ....*....|....*..
gi 2580540099 416 EFDGIDWAAFDDLVVVD 432
Cdd:PRK11064  398 QFKAINGDNVHQQWVVD 414
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
29-434 3.50e-59

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


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 200.63  E-value: 3.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYArATGN-VTGVDISEDVVRGVNDGECHVAkEPGLPELVAEQAERGALRATTDGVAAAESAAIH 107
Cdd:COG1004     3 IAVIGTGYVGLVTAACLA-ELGHeVTCVDIDEEKIEALNAGEIPIY-EPGLEELVARNVAAGRLRFTTDLAEAVAEADVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 108 VIIVPTPLTDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSkDLVVPYLADRSGLSAGEFGVAFCPERTSSGRA 187
Cdd:COG1004    81 FIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTA-DRVRAIIAEELRGAGVDFDVVSNPEFLREGSA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 188 LRDITesHP-KIVGGVDAESTR-VAALVYGEITSNEV-IPVRDATTAE----------AVKlfegvyrdvnIALANELAR 254
Cdd:COG1004   160 VEDFL--RPdRIVIGVDSERAAeVLRELYAPFVRNGTpIIVTDLRSAElikyaanaflATK----------ISFINEIAN 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 255 LRDDLGIDVTEAIDAantqpycdIHA----------PGPGVGGHCipwypyF---------ITSRVEAETPLLLTAREVN 315
Cdd:COG1004   228 LCEKVGADVEEVARG--------IGLdsrigpkflyAGIGYGGSC------FpkdvraliaTARELGYDLRLLEAVEEVN 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 316 DSMPAFTADKLRDELaaaGREIRGATVAVLGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSDEVVASFGATpV 395
Cdd:COG1004   294 ERQKRRLVEKIREHL---GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRLLPDD-I 369

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 2580540099 396 ALADLPTRAI---DAAVVVTPHEEFDGIDWAAFDDL----VVVDGR 434
Cdd:COG1004   370 TYADDAYEALegaDALVILTEWPEFRALDFARLKALmkgpVIFDGR 415
PRK15182 PRK15182
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
26-417 1.62e-48

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


Pssm-ID: 185104 [Multi-domain]  Cd Length: 425  Bit Score: 172.18  E-value: 1.62e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  26 EVPVAVYGLGKMGLPLAAVYARATgNVTGVDISEDVVRGVNDGechvaKEPGLPELVAEQAERGALRATTDgVAAAESAA 105
Cdd:PRK15182    6 EVKIAIIGLGYVGLPLAVEFGKSR-QVVGFDVNKKRILELKNG-----VDVNLETTEEELREARYLKFTSE-IEKIKECN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 106 IHVIIVPTPLTDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKDLVVPYLADRSGLSAGE-FGVAFCPERTSS 184
Cdd:PRK15182   79 FYIITVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARMSGMTFNQdFYVGYSPERINP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 185 GRALRDITESHpKIVGGVDAESTRVAALVYGEITSNEVIPVRDATTAEAVKLFEGVYRDVNIALANELARLRDDLGIDVT 264
Cdd:PRK15182  159 GDKKHRLTNIK-KITSGSTAQIAELIDEVYQQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 265 EAIDAANTQPYCDIHAPGPgVGGHCIPWYPYFITSRVEA---ETPLLLTAREVNDSMPAFTADKLRDELAAAGREIRGAT 341
Cdd:PRK15182  238 AVLRAAGSKWNFLPFRPGL-VGGHCIGVDPYYLTHKSQGigyYPEIILAGRRLNDNMGNYVSEQLIKAMIKKGINVEGSS 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2580540099 342 VAVLGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPML-SDEVVASFGATPValADLPTRAIDAAVVVTPHEEF 417
Cdd:PRK15182  317 VLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVdAEEVRREYGIIPV--SEVKSSHYDAIIVAVGHQQF 391
UDPG_MGDP_dh_N pfam03721
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ...
 29-211 4.60e-42

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: 147.78  E-value: 4.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVAkEPGLPELVaEQAERGALRATTDGVAAAESAAIHV 108
Cdd:pfam03721   3 ISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIY-EPGLDELV-KANVSGRLSFTTDYSTAIEEADVIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 109 IIVPTPL-TDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKDLVVPYLADRSGLSAGEFGVAFCPERTSSGRA 187
Cdd:pfam03721  81 IAVGTPSkKGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFDVASNPEFLREGSA 160

                         170       180
                  ....*....|....*....|....
gi 2580540099 188 LRDiTESHPKIVGGVDAESTRVAA 211
Cdd:pfam03721 161 VYD-LFNPDRVVIGVTEKCAEAAL 183
UDPG_MGDP_dh pfam00984
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ...
 230-316 1.08e-27

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: 105.92  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 230 TAEAVKLFEGVYRDVNIALANELARLRDDLGIDVTEAIDAANTQPY--CDIHAPGPGVGGHCIPWYPYFITSRVE---AE 304
Cdd:pfam00984   1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRigPKFLYPGPGVGGSCLPKDPRALIYLARelgVP 80

                          90
                  ....*....|..
gi 2580540099 305 TPLLLTAREVND 316
Cdd:pfam00984  81 ARLLEAAREVNE 92
PRK15057 PRK15057
UDP-glucose 6-dehydrogenase; Provisional
 29-385 4.02e-19

UDP-glucose 6-dehydrogenase; Provisional


Pssm-ID: 185017 [Multi-domain]  Cd Length: 388  Bit Score: 88.93  E-value: 4.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARaTGNVTGVDISEDVVRGVNDgechvAKEPGLPELVAE--QAERGALRATTDGVAAAESAAI 106
Cdd:PRK15057    3 ITISGTGYVGLSNGLLIAQ-NHEVVALDILPSRVAMLND-----RISPIVDKEIQQflQSDKIHFNATLDKNEAYRDADY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 107 HVIIVPTpltdDREPDLTAF-----EAVLDSIAQgLAPGDLVVVECTVPPGTSKDLVVPYLADrsglsagefGVAFCPER 181
Cdd:PRK15057   77 VIIATPT----DYDPKTNYFntssvESVIKDVVE-INPYAVMVIKSTVPVGFTAAMHKKYRTE---------NIIFSPEF 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 182 TSSGRALRDitESHPK--IVGGVDAESTRVAALVY-GEITSNEVIPVRDATTAEAVKLFEGVYRDVNIALANELARLRDD 258
Cdd:PRK15057  143 LREGKALYD--NLHPSriVIGERSERAERFAALLQeGAIKQNIPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAES 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 259 LGIDVTEAIDAANTQPYCDIHAPGP--GVGGHCIPwypyfitsrvEAETPLLLTAREVNDSMPAFTADKLR---DELAAA 333
Cdd:PRK15057  221 LGLNTRQIIEGVCLDPRIGNHYNNPsfGYGGYCLP----------KDTKQLLANYQSVPNNLISAIVDANRtrkDFIADA 290

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2580540099 334 GREIRGATVAVLGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSDE 385
Cdd:PRK15057  291 ILSRKPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKED 342
UDPG_MGDP_dh_C pfam03720
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ...
 343-437 1.63e-18

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: 80.70  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 343 AVLGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSDEVVASFGATPVALADLPTRA--IDAAVVVTPHEEFDGI 420
Cdd:pfam03720   1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGDGVTLVDDLEEALkgADAIVILTDHDEFKSL 80

                          90       100
                  ....*....|....*....|.
gi 2580540099 421 DWAAFDDL----VVVDGRGTL 437
Cdd:pfam03720  81 DWEKLKKLmkppVVFDGRNVL 101
UDPG_MGDP_dh_C smart00984
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ...
 343-437 1.23e-17

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: 77.93  E-value: 1.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  343 AVLGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSdEVVASFGATPVALADLPTRAIDAAVVVTPHEEFDGIDW 422
Cdd:smart00984   1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAM-EEAREYGLTYVSDLEEALKGADAVVIATEHDEFRSLDP 79

                           90
                   ....*....|....*....
gi 2580540099  423 AAFDDL----VVVDGRGTL 437
Cdd:smart00984  80 EELKDLmkkpVVVDGRNIL 98
PLN02353 PLN02353
probable UDP-glucose 6-dehydrogenase
 27-448 6.18e-12

probable UDP-glucose 6-dehydrogenase


Pssm-ID: 177986 [Multi-domain]  Cd Length: 473  Bit Score: 67.39  E-value: 6.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  27 VPVAVYGLGKMGLPLAAVYARATGN--VTGVDISEDVVRGVNDGECHVAkEPGLPELVaeQAERGA-LRATTDGVAAAES 103
Cdd:PLN02353    2 VKICCIGAGYVGGPTMAVIALKCPDieVVVVDISVPRIDAWNSDQLPIY-EPGLDEVV--KQCRGKnLFFSTDVEKHVAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 104 AAIHVIIVPTP-----LTDDREPDLTAFEAVLDSIAQGLAPGDLVVVECTVPPGTSKdlvvpylADRSGLSAGEFGVAF- 177
Cdd:PLN02353   79 ADIVFVSVNTPtktrgLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAE-------AIEKILTHNSKGINFq 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 178 ---CPERTSSGRALRDITESHPKIVGGVDAESTRVAALVYGEITSNEVIPVRDATT----AEAVKLFEGVYRDVNIALAN 250
Cdd:PLN02353  152 ilsNPEFLAEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPEERIITTnlwsAELSKLAANAFLAQRISSVN 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 251 ELARLRDDLGIDVTEAIDAANTQPYCdihapGP-------GVGGHCipwYPYFITSRVE-AETPLLLTARE-------VN 315
Cdd:PLN02353  232 AMSALCEATGADVSQVSHAVGKDSRI-----GPkflnasvGFGGSC---FQKDILNLVYiCECNGLPEVAEywkqvikMN 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 316 DSMPAFTADKLrdeLAAAGREIRGATVAVLGVTYRPGVAETRATPAAGVIDRLNDLGATVLAVDPMLSDEVVASFGATPV 395
Cdd:PLN02353  304 DYQKSRFVNRV---VSSMFNTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVTEEQIQRDLSMNK 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 396 ALADLPTR-----------------AIDAA------VVVTPHEEFDGIDWAA-FDDLV----VVDGR-----GTLGDIGH 442
Cdd:PLN02353  381 FDWDHPRHlqpmsptavkqvsvvwdAYEATkgahgiCILTEWDEFKTLDYQKiYDNMQkpafVFDGRnvldhEKLREIGF 460


                  ....*.
gi 2580540099 443 RVYEIG 448
Cdd:PLN02353  461 IVYSIG 466
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 28-157 1.54e-04

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 43.57  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  28 PVAVYGLGKMGLPLAAVYARATGNVTGVDISedvvrgvndgechvakepglPELVAEQAERGALRATTdGVAAAESAAIH 107
Cdd:COG2084     3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRT--------------------PAKAEALVAAGARVAAS-PAEAAAAADVV 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2580540099 108 VIIVPTPltddrePDLtafEAVL---DSIAQGLAPGDLVVVECTVPPGTSKDL 157
Cdd:COG2084    62 ITMLPDD------AAV---EEVLlgeDGLLAALRPGAVVVDMSTISPETAREL 105
NAD_Gly3P_dh_N pfam01210
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ...
 28-155 2.28e-04

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


Pssm-ID: 395967 [Multi-domain]  Cd Length: 158  Bit Score: 41.41  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  28 PVAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVAKEPG--LPElvaeqaergALRATTDGVAAAESAA 105
Cdd:pfam01210   1 KIAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINTTHENVRYLPGikLPE---------NLKATTDLAEALKGAD 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2580540099 106 IHVIIVPTpltddrepdlTAFEAVLDSIAQGLAPgDLVVVECT--VPPGTSK 155
Cdd:pfam01210  72 IIVIVVPS----------QALREVLKQLKGLLKP-DAILVSLSkgIEPGTLK 112
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
29-145 1.04e-03

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


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 41.21  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVAKEPG--LPElvaeqaergALRATTDGVAAAESAAI 106
Cdd:PRK00094    4 IAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENPRYLPGikLPD---------NLRATTDLAEALADADL 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2580540099 107 HVIIVPTPltddrepdltAFEAVLDSIAQGLAPGDLVVV 145
Cdd:PRK00094   75 ILVAVPSQ----------ALREVLKQLKPLLPPDAPIVW 103
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 29-144 1.10e-03

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


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 41.18  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRGVNDGECHVAKEPG--LPElvaeqaergALRATTDGVAAAESAAI 106
Cdd:COG0240     3 IAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETRENPRYLPGvkLPE---------NLRATSDLEEALAGADL 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2580540099 107 HVIIVPTPltddrepdltAFEAVLDSIAQGLAPGDLVV 144
Cdd:COG0240    74 VLLAVPSQ----------ALREVLEQLAPLLPPGAPVV 101
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 303-404 4.73e-03

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


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 38.84  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099 303 AETPLLLTAREVNDSMPAFTADKLRDELAAAGREIRGATVAVLGVtyrpG-----VAETRAtpaagvidrlNDLGATVLA 377
Cdd:cd12177   111 AVALILTVLRKINQASEAVKEGKWTERANFVGHELSGKTVGIIGY----GnigsrVAEILK----------EGFNAKVLA 176

                          90       100
                  ....*....|....*....|....*..
gi 2580540099 378 VDPMLSDEVVASFGATPVALADLPTRA 404
Cdd:cd12177   177 YDPYVSEEVIKKKGAKPVSLEELLAES 203
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 29-157 7.52e-03

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: 37.06  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580540099  29 VAVYGLGKMGLPLAAVYARATGNVTGVDISEDVVRgvndgechvakepglpELVAEqaerGALRATTDGVAAAESAAIHV 108
Cdd:pfam03446   2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVE----------------ELVAA----GAIAAASPAEFVAGLDVVIT 61

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2580540099 109 IIvptpltddrePDLTAFEAVLDS--IAQGLAPGDLVVVECTVPPGTSKDL 157
Cdd:pfam03446  62 MV----------PAGAAVDAVIFGegLLPGLKPGDIIIDGSTSSPEDARRR 102
 
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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