|
Name |
Accession |
Description |
Interval |
E-value |
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
1-373 |
0e+00 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 874.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 1 MSFATISVIGLGYIGLPTRA-FASRQKQVIGVDINQHAVDTINRGEIHIVEPDLASVVKTAVEGGFLRASTTPVEADRWL 79
Cdd:PRK11064 1 MSFETISVIGLGYIGLPTAAaFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 80 IAVPTPFKGDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMRPDLTFPQQVGEQADVNIAYCPER 159
Cdd:PRK11064 81 IAVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTFPQQAGEQADINIAYCPER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 160 VLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 239
Cdd:PRK11064 161 VLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 240 WELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDHKPFWVIDQVKAAVADCLAATDKRASE 319
Cdd:PRK11064 241 WELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKRASE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 148190 320 LKIACFGLAFKPNIDDLRESPAMEIAELIAQWHSGETLVVEPNIHQLPKKLTGL 373
Cdd:PRK11064 321 VKIACFGLAFKPNIDDLRESPAMEIAELIAQWHSGETLVVEPNIHQLPKKLDGL 374
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
5-367 |
0e+00 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 518.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 5 TISVIGLGYIGLPT-RAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDlASVVKTAVEGGFLRASTTPV---EADRWLI 80
Cdd:COG0677 1 KIAVIGLGYVGLPLaVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTDPEalaEADVVII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 81 AVPTPFKGDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMRPDLTFPQqvgeqaDVNIAYCPERV 160
Cdd:COG0677 80 AVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAGE------DFFLAYSPERI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 161 LPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLE-GECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 239
Cdd:COG0677 154 NPGNKLHELRNIPKVVGGITPESAERAAALYGSVVTaGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 240 WELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQ---QARLIRTAREVNDHKPFWVIDQVKAAvadcLAATDKR 316
Cdd:COG0677 234 WEVIEAANTKPGFLIFYPGPGVGGHCIPVDPYYLTWKARElgyHPRLILAAREINDSMPEYVVERVVKA----LNEAGKS 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 148190 317 ASELKIACFGLAFKPNIDDLRESPAMEIAELIAQWHsGETLVVEPNIHQLP 367
Cdd:COG0677 310 LKGARVLVLGLAYKENVDDLRESPALDIIEELREYG-AEVDVHDPYVDEEE 359
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
5-351 |
8.61e-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: 378.49 E-value: 8.61e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 5 TISVIGLGYIGLPTRA-FASRQKQVIGVDINQHAVDTINRGEIHIVEPDLASVVKTAVEGGFLRASTTPV----EADRWL 79
Cdd:TIGR03026 2 KIAVIGLGYVGLPLAAlLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEeairDADVII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 80 IAVPTPFKGDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMRPdltfpQQVGEqaDVNIAYCPER 159
Cdd:TIGR03026 82 ICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSG-----LKLGE--DFYLAYNPEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 160 VLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 239
Cdd:TIGR03026 155 LREGNAVHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 240 WELIRLANRHPR--VNILQPGPGVGGHCIAVDPWFIVA---QNPQQARLIRTAREVNDHKPFWVIDQVKAAVADCLAATd 314
Cdd:TIGR03026 235 YEVIEAAGTDPRigFNFLNPGPGVGGHCIPKDPLALIAkakELGYNPELIEAAREINDSQPDYVVEKIKDLLGPLKGKT- 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 148190 315 kraselkIACFGLAFKPNIDDLRESPAMEIAELIAQW 351
Cdd:TIGR03026 314 -------VLILGLAFKPNTDDVRESPALDIIELLKEK 343
|
|
| UDPMaNacDH_Arch |
NF040825 |
UDP-N-acetyl-D-mannosamine dehydrogenase; |
4-348 |
1.30e-108 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase;
Pssm-ID: 468765 [Multi-domain] Cd Length: 418 Bit Score: 324.79 E-value: 1.30e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 4 ATISVIGLGYIGLPTR-AFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLASVVKTAVEGGFLRASTTPVE---ADRWL 79
Cdd:NF040825 1 MKIAVIGLGYIGLPTAiMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTDPEDlkgADAFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 80 IAVPTPFKGDhEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMrpdltfpQQVGEQADVNIAYCPER 159
Cdd:NF040825 81 ICVQTPLKED-KPDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLLEEL-------TGLKEGEDFYMAHAPER 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 160 VLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 239
Cdd:NF040825 153 VMPGRIFKELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTFRDVNIALANEFALLAHQYGVNV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 240 WELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDHKPFWvidqVKAAVADCLAATDKRASE 319
Cdd:NF040825 233 FEAIELANTHPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLAREINEDMPLF----AKDLLFEALEEANVPPEE 308
|
330 340
....*....|....*....|....*....
gi 148190 320 LKIACFGLAFKPNIDDLRESPAMEIAELI 348
Cdd:NF040825 309 AVVTVLGLAYKGDTDDTRNSPALKFVELI 337
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
4-190 |
9.02e-78 |
|
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: 237.53 E-value: 9.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 4 ATISVIGLGYIGLPTRA-FASRQKQVIGVDINQHAVDTINRGEIHIVEPDLASVVKTAVEG---GFLRASTTPVEADRWL 79
Cdd:pfam03721 1 MKISVIGLGYVGLPTAAcLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGrlsFTTDYSTAIEEADVIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 80 IAVPTPFK-GDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMRPDLTfpqqvgeQADVNIAYCPE 158
Cdd:pfam03721 81 IAVGTPSKkGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKV-------GVDFDVASNPE 153
|
170 180 190
....*....|....*....|....*....|...
gi 148190 159 RVLPGQVMVELIKNDRVIGGMTPVCS-ARASEL 190
Cdd:pfam03721 154 FLREGSAVYDLFNPDRVVIGVTEKCAeAALEEL 186
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
323-365 |
2.68e-10 |
|
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: 56.75 E-value: 2.68e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 148190 323 ACFGLAFKPNIDDLRESPAMEIAELIAQWHsGETLVVEPNIHQ 365
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAG-AEVVVYDPYAME 42
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
1-373 |
0e+00 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 874.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 1 MSFATISVIGLGYIGLPTRA-FASRQKQVIGVDINQHAVDTINRGEIHIVEPDLASVVKTAVEGGFLRASTTPVEADRWL 79
Cdd:PRK11064 1 MSFETISVIGLGYIGLPTAAaFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 80 IAVPTPFKGDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMRPDLTFPQQVGEQADVNIAYCPER 159
Cdd:PRK11064 81 IAVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLTFPQQAGEQADINIAYCPER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 160 VLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 239
Cdd:PRK11064 161 VLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 240 WELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDHKPFWVIDQVKAAVADCLAATDKRASE 319
Cdd:PRK11064 241 WELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKRASE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 148190 320 LKIACFGLAFKPNIDDLRESPAMEIAELIAQWHSGETLVVEPNIHQLPKKLTGL 373
Cdd:PRK11064 321 VKIACFGLAFKPNIDDLRESPAMEIAELIAQWHSGETLVVEPNIHQLPKKLDGL 374
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
5-367 |
0e+00 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 518.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 5 TISVIGLGYIGLPT-RAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDlASVVKTAVEGGFLRASTTPV---EADRWLI 80
Cdd:COG0677 1 KIAVIGLGYVGLPLaVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTDPEalaEADVVII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 81 AVPTPFKGDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMRPDLTFPQqvgeqaDVNIAYCPERV 160
Cdd:COG0677 80 AVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKAGE------DFFLAYSPERI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 161 LPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLE-GECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 239
Cdd:COG0677 154 NPGNKLHELRNIPKVVGGITPESAERAAALYGSVVTaGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 240 WELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQ---QARLIRTAREVNDHKPFWVIDQVKAAvadcLAATDKR 316
Cdd:COG0677 234 WEVIEAANTKPGFLIFYPGPGVGGHCIPVDPYYLTWKARElgyHPRLILAAREINDSMPEYVVERVVKA----LNEAGKS 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 148190 317 ASELKIACFGLAFKPNIDDLRESPAMEIAELIAQWHsGETLVVEPNIHQLP 367
Cdd:COG0677 310 LKGARVLVLGLAYKENVDDLRESPALDIIEELREYG-AEVDVHDPYVDEEE 359
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
5-351 |
8.61e-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: 378.49 E-value: 8.61e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 5 TISVIGLGYIGLPTRA-FASRQKQVIGVDINQHAVDTINRGEIHIVEPDLASVVKTAVEGGFLRASTTPV----EADRWL 79
Cdd:TIGR03026 2 KIAVIGLGYVGLPLAAlLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEeairDADVII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 80 IAVPTPFKGDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMRPdltfpQQVGEqaDVNIAYCPER 159
Cdd:TIGR03026 82 ICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSG-----LKLGE--DFYLAYNPEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 160 VLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 239
Cdd:TIGR03026 155 LREGNAVHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 240 WELIRLANRHPR--VNILQPGPGVGGHCIAVDPWFIVA---QNPQQARLIRTAREVNDHKPFWVIDQVKAAVADCLAATd 314
Cdd:TIGR03026 235 YEVIEAAGTDPRigFNFLNPGPGVGGHCIPKDPLALIAkakELGYNPELIEAAREINDSQPDYVVEKIKDLLGPLKGKT- 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 148190 315 kraselkIACFGLAFKPNIDDLRESPAMEIAELIAQW 351
Cdd:TIGR03026 314 -------VLILGLAFKPNTDDVRESPALDIIELLKEK 343
|
|
| UDPMaNacDH_Arch |
NF040825 |
UDP-N-acetyl-D-mannosamine dehydrogenase; |
4-348 |
1.30e-108 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase;
Pssm-ID: 468765 [Multi-domain] Cd Length: 418 Bit Score: 324.79 E-value: 1.30e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 4 ATISVIGLGYIGLPTR-AFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLASVVKTAVEGGFLRASTTPVE---ADRWL 79
Cdd:NF040825 1 MKIAVIGLGYIGLPTAiMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTDPEDlkgADAFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 80 IAVPTPFKGDhEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMrpdltfpQQVGEQADVNIAYCPER 159
Cdd:NF040825 81 ICVQTPLKED-KPDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLLEEL-------TGLKEGEDFYMAHAPER 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 160 VLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 239
Cdd:NF040825 153 VMPGRIFKELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTFRDVNIALANEFALLAHQYGVNV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 240 WELIRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDHKPFWvidqVKAAVADCLAATDKRASE 319
Cdd:NF040825 233 FEAIELANTHPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLAREINEDMPLF----AKDLLFEALEEANVPPEE 308
|
330 340
....*....|....*....|....*....
gi 148190 320 LKIACFGLAFKPNIDDLRESPAMEIAELI 348
Cdd:NF040825 309 AVVTVLGLAYKGDTDDTRNSPALKFVELI 337
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
4-190 |
9.02e-78 |
|
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: 237.53 E-value: 9.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 4 ATISVIGLGYIGLPTRA-FASRQKQVIGVDINQHAVDTINRGEIHIVEPDLASVVKTAVEG---GFLRASTTPVEADRWL 79
Cdd:pfam03721 1 MKISVIGLGYVGLPTAAcLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGrlsFTTDYSTAIEEADVIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 80 IAVPTPFK-GDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMRPDLTfpqqvgeQADVNIAYCPE 158
Cdd:pfam03721 81 IAVGTPSKkGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKV-------GVDFDVASNPE 153
|
170 180 190
....*....|....*....|....*....|...
gi 148190 159 RVLPGQVMVELIKNDRVIGGMTPVCS-ARASEL 190
Cdd:pfam03721 154 FLREGSAVYDLFNPDRVVIGVTEKCAeAALEEL 186
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
6-350 |
3.86e-73 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 234.15 E-value: 3.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 6 ISVIGLGYIGLPTRA-FASRQKQVIGVDINQHAVDTINRGEIHIVEPDLASVVKTAVEGGFLRASTTPVEADRW----LI 80
Cdd:COG1004 3 IAVIGTGYVGLVTAAcLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDLAEAVAEadvvFI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 81 AVPTPFKGDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEmrpdltfpQQVGEQADVNIAYCPERV 160
Cdd:COG1004 83 AVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAE--------ELRGAGVDFDVVSNPEFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 161 LPGQVMVELIKNDR-VIGGMTPVCSARASELYKIFLEGEC--VVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGI 237
Cdd:COG1004 155 REGSAVEDFLRPDRiVIGVDSERAAEVLRELYAPFVRNGTpiIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 238 NVWEL---IRLANRhprvnI----LQPGPGVGGHC--------IAvdpwfIVAQNPQQARLIRTAREVNDHKPFWVIDQV 302
Cdd:COG1004 235 DVEEVargIGLDSR-----IgpkfLYAGIGYGGSCfpkdvralIA-----TARELGYDLRLLEAVEEVNERQKRRLVEKI 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 148190 303 KAAVADCLAatDKRaselkIACFGLAFKPNIDDLRESPAMEIAE-LIAQ 350
Cdd:COG1004 305 REHLGGDLK--GKT-----IAVLGLAFKPNTDDMRESPALDIIEaLLEA 346
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
6-351 |
3.54e-38 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 141.75 E-value: 3.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 6 ISVIGLGYIGLPTRAFASRQKQVIGVDINQHAVDTINRGeihiVEPDLASVVKTAVEGGFLRAST---TPVEADRWLIAV 82
Cdd:PRK15182 9 IAIIGLGYVGLPLAVEFGKSRQVVGFDVNKKRILELKNG----VDVNLETTEEELREARYLKFTSeieKIKECNFYIITV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 83 PTPFKGDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMRPDLTFPQqvgeqaDVNIAYCPERVLP 162
Cdd:PRK15182 85 PTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARMSGMTFNQ------DFYVGYSPERINP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 163 GQVMVELIKNDRVIGGMTPVCSARASELY-KIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINVWE 241
Cdd:PRK15182 159 GDKKHRLTNIKKITSGSTAQIAELIDEVYqQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 242 LIRLANRhpRVNILQPGPG-VGGHCIAVDPWFIVAQNP---QQARLIRTAREVNDHKPFWVIDQ-VKAAVADCLAATDKr 316
Cdd:PRK15182 239 VLRAAGS--KWNFLPFRPGlVGGHCIGVDPYYLTHKSQgigYYPEIILAGRRLNDNMGNYVSEQlIKAMIKKGINVEGS- 315
|
330 340 350
....*....|....*....|....*....|....*
gi 148190 317 aselKIACFGLAFKPNIDDLRESPAMEIAELIAQW 351
Cdd:PRK15182 316 ----SVLILGFTFKENCPDIRNTRIIDVVKELGKY 346
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
206-292 |
2.47e-37 |
|
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: 129.81 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 206 TAEMCKLTENSFRDVNIAFANELSLICADQGINVWELIRLANRHPR--VNILQPGPGVGGHCIAVDPWFIVA---QNPQQ 280
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRigPKFLYPGPGVGGSCLPKDPRALIYlarELGVP 80
|
90
....*....|..
gi 148190 281 ARLIRTAREVND 292
Cdd:pfam00984 81 ARLLEAAREVNE 92
|
|
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
5-344 |
8.19e-28 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 114.00 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 5 TISVIGLGYIGLPTRAFASRQ---KQVIGVDINQHAVDTINRGEIHIVEPDLASVVKtAVEGGFLRASTTP----VEADR 77
Cdd:PLN02353 3 KICCIGAGYVGGPTMAVIALKcpdIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVK-QCRGKNLFFSTDVekhvAEADI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 78 WLIAVPTPFK-----GDHEPDMTYVESAARSIAPVLKKGALVILESTSPVGSTEKMAEWLAEMRPDLTFPqqvgeqadvn 152
Cdd:PLN02353 82 VFVSVNTPTKtrglgAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQ---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 153 IAYCPERVLPGQVMVELIKNDRV-IGGM-TPVCSARASELYKIFL----EGECVVTNSRTAEMCKLTENSFRDVNIAFAN 226
Cdd:PLN02353 152 ILSNPEFLAEGTAIEDLFKPDRVlIGGReTPEGQKAVQALKDVYAhwvpEERIITTNLWSAELSKLAANAFLAQRISSVN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 227 ELSLICADQGINVWELIRLANRHPRV--NILQPGPGVGGHCIAVDPW---FIVAQN--PQQARLIRTAREVNDHkpfwvi 299
Cdd:PLN02353 232 AMSALCEATGADVSQVSHAVGKDSRIgpKFLNASVGFGGSCFQKDILnlvYICECNglPEVAEYWKQVIKMNDY------ 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 148190 300 dQVKAAVADCLAATDKRASELKIACFGLAFKPNIDDLRESPAMEI 344
Cdd:PLN02353 306 -QKSRFVNRVVSSMFNTVSGKKIAVLGFAFKKDTGDTRETPAIDV 349
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
6-361 |
4.71e-17 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 81.99 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 6 ISVIGLGYIGLPTRAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLASVVKTavEGGFLRASTTPVEA----DRWLIA 81
Cdd:PRK15057 3 ITISGTGYVGLSNGLLIAQNHEVVALDILPSRVAMLNDRISPIVDKEIQQFLQS--DKIHFNATLDKNEAyrdaDYVIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 82 VPTpfkgDHEPDMTY-----VESAARSIAPVlKKGALVILESTSPVGSTEKMAEwlaemrpdlTFPQQvgeqadvNIAYC 156
Cdd:PRK15057 81 TPT----DYDPKTNYfntssVESVIKDVVEI-NPYAVMVIKSTVPVGFTAAMHK---------KYRTE-------NIIFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 157 PERVLPGQVMVELIKNDRVIGGMTpvcSARASELYKIFLEGE------CVVTNSRTAEMCKLTENSFRDVNIAFANELSL 230
Cdd:PRK15057 140 PEFLREGKALYDNLHPSRIVIGER---SERAERFAALLQEGAikqnipTLFTDSTEAEAIKLFANTYLAMRVAYFNELDS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 231 ICADQGINVWELIRLANRHPRV--NILQPGPGVGGHCIAVDPWFIVAqNPQQA--RLIRTAREVNDHKpfwvidqvKAAV 306
Cdd:PRK15057 217 YAESLGLNTRQIIEGVCLDPRIgnHYNNPSFGYGGYCLPKDTKQLLA-NYQSVpnNLISAIVDANRTR--------KDFI 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 148190 307 ADCLAATDKRAselkIACFGLAFKPNIDDLRESPAMEIAELIaQWHSGETLVVEP 361
Cdd:PRK15057 288 ADAILSRKPQV----VGIYRLIMKSGSDNFRASSIQGIMKRI-KAKGVEVIIYEP 337
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
323-365 |
2.68e-10 |
|
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: 56.75 E-value: 2.68e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 148190 323 ACFGLAFKPNIDDLRESPAMEIAELIAQWHsGETLVVEPNIHQ 365
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAG-AEVVVYDPYAME 42
|
|
| UDPG_MGDP_dh_C |
pfam03720 |
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ... |
323-372 |
4.48e-08 |
|
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: 50.65 E-value: 4.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 148190 323 ACFGLAFKPNIDDLRESPAMEIAELIAQWHsGETLVVEPNIHQLPKKLTG 372
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEG-AEVKVYDPYVPEEAIEALG 49
|
|
| PRK07502 |
PRK07502 |
prephenate/arogenate dehydrogenase family protein; |
1-139 |
1.01e-03 |
|
prephenate/arogenate dehydrogenase family protein;
Pssm-ID: 236034 [Multi-domain] Cd Length: 307 Bit Score: 40.72 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 1 MSFATISVIGLGYIGlPTRAFASRQKQVIGvdinqhavdtinrgEIHIVEPDlASVVKTAVEGGFL-RASTTPVEA---- 75
Cdd:PRK07502 4 PLFDRVALIGIGLIG-SSLARAIRRLGLAG--------------EIVGADRS-AETRARARELGLGdRVTTSAAEAvkga 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148190 76 DRWLIAVPtpfkgdhepdMTYVESAARSIAPVLKKGALVilestSPVGSTEkmAEWLAEMRPDL 139
Cdd:PRK07502 68 DLVILCVP----------VGASGAVAAEIAPHLKPGAIV-----TDVGSVK--ASVIAAMAPHL 114
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
4-134 |
7.65e-03 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 37.79 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148190 4 ATISVIGLGYIGLP-TRAFASRQKQVIGVDINQHAVDtinrgeihivepDLASvvktavEGGflRASTTPVEA----DRW 78
Cdd:COG2084 2 MKVGFIGLGAMGAPmARNLLKAGHEVTVWNRTPAKAE------------ALVA------AGA--RVAASPAEAaaaaDVV 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 148190 79 LIAVPTPfkgDHepdmtyVESAARS---IAPVLKKGALVILESTSPVGSTEKMAEWLAE 134
Cdd:COG2084 62 ITMLPDD---AA------VEEVLLGedgLLAALRPGAVVVDMSTISPETARELAAAAAA 111
|
|
|