|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
1-388 |
0e+00 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 757.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIAQNHEVVALDIVQAKVDMLNKKQSPIVDKEIEEYLATKDLNFRATTDKYDAYKNADYVIIA 80
Cdd:PRK15057 1 MKITISGTGYVGLSNGLLIAQNHEVVALDILPSRVAMLNDRISPIVDKEIQQFLQSDKIHFNATLDKNEAYRDADYVIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 81 TPTDYDPKTNYFNTSSVEAVIRDVTEINPNAVMIIKSTIPVGFTESIKERFGIENVIFSPEFLREGKALYDNLHPSRIVI 160
Cdd:PRK15057 81 TPTDYDPKTNYFNTSSVESVIKDVVEINPYAVMVIKSTVPVGFTAAMHKKYRTENIIFSPEFLREGKALYDNLHPSRIVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 161 GEQSERAERFAALLQEGAIKQDIPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNSRQIIEGVCLDPRIGN 240
Cdd:PRK15057 161 GERSERAERFAALLQEGAIKQNIPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNTRQIIEGVCLDPRIGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 241 HYNNPSFGYGGYCLPKDTKQLLANYQSVPNNLISAIVDANRTRKDFIADSILARKPKVVGVYRLIMKSGSDNFRASSIQG 320
Cdd:PRK15057 241 HYNNPSFGYGGYCLPKDTKQLLANYQSVPNNLISAIVDANRTRKDFIADAILSRKPQVVGIYRLIMKSGSDNFRASSIQG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446627448 321 IMKRIKAKGVPVIVYEPAMKEDDFFRSRVVRDLDAFKQEADVIISNRMSADLADVADKVYTRDLFGND 388
Cdd:PRK15057 321 IMKRIKAKGVEVIIYEPVMKEDSFFNSRLERDLATFKQQADVIISNRMAEELKDVADKVYTRDLFGSD 388
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
1-385 |
3.14e-125 |
|
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: 366.94 E-value: 3.14e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIA-QNHEVVALDIVQAKVDMLNKKQSPIVDKEIEEYL--ATKDLNFRATTDKYDAYKNADYV 77
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLAdLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLakALKAGRLRATTDYEEAIRDADVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 78 IIATPTDYDPkTNYFNTSSVEAVIRDVTE-INPNAVMIIKSTIPVGFTES----IKERFGIE-----NVIFSPEFLREGK 147
Cdd:TIGR03026 81 IICVPTPLKE-DGSPDLSYVESAAETIAKhLRKGATVVLESTVPPGTTEEvvkpILERSGLKlgedfYLAYNPEFLREGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 148 ALYDNLHPSRIVIGEQSERAERFAALLQEGAikqDIPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNSRQ 227
Cdd:TIGR03026 160 AVHDLLHPDRIVGGETEEAGEAVAELYSPII---DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 228 IIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLLANYQS--VPNNLISAIVDANRTRKDFIADSILAR----KPKVVGV 301
Cdd:TIGR03026 237 VIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKElgYNPELIEAAREINDSQPDYVVEKIKDLlgplKGKTVLI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 302 YRLIMKSGSDNFRASSIQGIMKRIKAKGVPVIVYEPAMKEDDFFRSRVVRDLDAFKQEADVIISNRM-----SADLADVA 376
Cdd:TIGR03026 317 LGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDLEEALKGADALVILTDhsefkDLDLEKIK 396
|
....*....
gi 446627448 377 DKVYTRDLF 385
Cdd:TIGR03026 397 DLMKGKVVV 405
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
1-341 |
9.42e-75 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 238.38 E-value: 9.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIAQ-NHEVVALDIVQAKVDMLNKKQSPIVDKEIEEYLA--TKDLNFRATTDKYDAYKNADYV 77
Cdd:COG1004 1 MKIAVIGTGYVGLVTAACLAElGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVArnVAAGRLRFTTDLAEAVAEADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 78 IIA--TPTDYDpktNYFNTSSVEAVIRDVTE-INPNAVMIIKSTIPVGFTESIKERF-------GIE-NVIFSPEFLREG 146
Cdd:COG1004 81 FIAvgTPSDED---GSADLSYVLAAARSIGEaLKGYKVVVTKSTVPVGTADRVRAIIaeelrgaGVDfDVVSNPEFLREG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 147 KALYDNLHPSRIVIGEQSERAERFAALLQEGAIKQDIPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNSR 226
Cdd:COG1004 158 SAVEDFLRPDRIVIGVDSERAAEVLRELYAPFVRNGTPIIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGADVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 227 QIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLLANYQS--VPNNLISAIVDANRTRKDFIADSILAR-----KPKVV 299
Cdd:COG1004 238 EVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARElgYDLRLLEAVEEVNERQKRRLVEKIREHlggdlKGKTI 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446627448 300 GVYRLIMKSGSDNFR-ASSIQgIMKRIKAKGVPVIVYEP-AMKE 341
Cdd:COG1004 318 AVLGLAFKPNTDDMReSPALD-IIEALLEAGARVRAYDPvAMEN 360
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
1-176 |
1.77e-38 |
|
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: 136.22 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIAQ-NHEVVALDIVQAKVDMLNKKQSPIVDKEIEEYL-ATKDLNFRATTDKYDAYKNADYVI 78
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEiGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVkANVSGRLSFTTDYSTAIEEADVIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 79 IATPTDYDPKTNYFNTSSVEAVIRDVTE-INPNAVMIIKSTIPVGFTESIKERFGIE---------NVIFSPEFLREGKA 148
Cdd:pfam03721 81 IAVGTPSKKGGGAADLKYVESAARSIAPhLKKGKVVVVKSTVPVGTTENLVKPIIEEggkkvgvdfDVASNPEFLREGSA 160
|
170 180
....*....|....*....|....*...
gi 446627448 149 LYDNLHPSRIVIGEQSERAErfaALLQE 176
Cdd:pfam03721 161 VYDLFNPDRVVIGVTEKCAE---AALEE 185
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
300-385 |
6.95e-16 |
|
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: 72.54 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 300 GVYRLIMKSGSDNFRASSIQGIMKRIKAKGVPVIVYEP-AMKEDD-FFRSRVVRDLDAFKQEADVIISNRMS-------A 370
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPyAMEEAReYGLTYVSDLEEALKGADAVVIATEHDefrsldpE 80
|
90
....*....|....*...
gi 446627448 371 DLADVADK---VYTRDLF 385
Cdd:smart00984 81 ELKDLMKKpvvVDGRNIL 98
|
|
| LDH_MDH_like |
cd00650 |
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members ... |
4-137 |
7.73e-04 |
|
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members of this family include ubiquitous enzymes like L-lactate dehydrogenases (LDH), L-2-hydroxyisocaproate dehydrogenases, and some malate dehydrogenases (MDH). LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH/MDH-like proteins are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.
Pssm-ID: 133419 [Multi-domain] Cd Length: 263 Bit Score: 40.77 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 4 TISGTGYVG--LSNGILIAQNH---EVVALDIVQAKVDmlnkkqspIVDKEIEEYLA-TKDLNFRATTDKYDAYKNADYV 77
Cdd:cd00650 3 VIGAGGNVGpaLAFGLADGSVLlaiELVLYDIDEEKLK--------GVAMDLQDAVEpLADIKVSITDDPYEAFKDADVV 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446627448 78 IIAT-----PTDYDPKTNYFNTSSVEAVIRDVTEINPNAVMIIKSTiPVGF-TESIKERFGI--ENVI 137
Cdd:cd00650 75 IITAgvgrkPGMGRLDLLKRNVPIVKEIGDNIEKYSPDAWIIVVSN-PVDIiTYLVWRYSGLpkEKVI 141
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
1-388 |
0e+00 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 757.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIAQNHEVVALDIVQAKVDMLNKKQSPIVDKEIEEYLATKDLNFRATTDKYDAYKNADYVIIA 80
Cdd:PRK15057 1 MKITISGTGYVGLSNGLLIAQNHEVVALDILPSRVAMLNDRISPIVDKEIQQFLQSDKIHFNATLDKNEAYRDADYVIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 81 TPTDYDPKTNYFNTSSVEAVIRDVTEINPNAVMIIKSTIPVGFTESIKERFGIENVIFSPEFLREGKALYDNLHPSRIVI 160
Cdd:PRK15057 81 TPTDYDPKTNYFNTSSVESVIKDVVEINPYAVMVIKSTVPVGFTAAMHKKYRTENIIFSPEFLREGKALYDNLHPSRIVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 161 GEQSERAERFAALLQEGAIKQDIPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNSRQIIEGVCLDPRIGN 240
Cdd:PRK15057 161 GERSERAERFAALLQEGAIKQNIPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNTRQIIEGVCLDPRIGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 241 HYNNPSFGYGGYCLPKDTKQLLANYQSVPNNLISAIVDANRTRKDFIADSILARKPKVVGVYRLIMKSGSDNFRASSIQG 320
Cdd:PRK15057 241 HYNNPSFGYGGYCLPKDTKQLLANYQSVPNNLISAIVDANRTRKDFIADAILSRKPQVVGIYRLIMKSGSDNFRASSIQG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446627448 321 IMKRIKAKGVPVIVYEPAMKEDDFFRSRVVRDLDAFKQEADVIISNRMSADLADVADKVYTRDLFGND 388
Cdd:PRK15057 321 IMKRIKAKGVEVIIYEPVMKEDSFFNSRLERDLATFKQQADVIISNRMAEELKDVADKVYTRDLFGSD 388
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
1-385 |
3.14e-125 |
|
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: 366.94 E-value: 3.14e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIA-QNHEVVALDIVQAKVDMLNKKQSPIVDKEIEEYL--ATKDLNFRATTDKYDAYKNADYV 77
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLAdLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLakALKAGRLRATTDYEEAIRDADVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 78 IIATPTDYDPkTNYFNTSSVEAVIRDVTE-INPNAVMIIKSTIPVGFTES----IKERFGIE-----NVIFSPEFLREGK 147
Cdd:TIGR03026 81 IICVPTPLKE-DGSPDLSYVESAAETIAKhLRKGATVVLESTVPPGTTEEvvkpILERSGLKlgedfYLAYNPEFLREGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 148 ALYDNLHPSRIVIGEQSERAERFAALLQEGAikqDIPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNSRQ 227
Cdd:TIGR03026 160 AVHDLLHPDRIVGGETEEAGEAVAELYSPII---DGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 228 IIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLLANYQS--VPNNLISAIVDANRTRKDFIADSILAR----KPKVVGV 301
Cdd:TIGR03026 237 VIEAAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKElgYNPELIEAAREINDSQPDYVVEKIKDLlgplKGKTVLI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 302 YRLIMKSGSDNFRASSIQGIMKRIKAKGVPVIVYEPAMKEDDFFRSRVVRDLDAFKQEADVIISNRM-----SADLADVA 376
Cdd:TIGR03026 317 LGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDDLEEALKGADALVILTDhsefkDLDLEKIK 396
|
....*....
gi 446627448 377 DKVYTRDLF 385
Cdd:TIGR03026 397 DLMKGKVVV 405
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
1-341 |
9.42e-75 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 238.38 E-value: 9.42e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIAQ-NHEVVALDIVQAKVDMLNKKQSPIVDKEIEEYLA--TKDLNFRATTDKYDAYKNADYV 77
Cdd:COG1004 1 MKIAVIGTGYVGLVTAACLAElGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVArnVAAGRLRFTTDLAEAVAEADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 78 IIA--TPTDYDpktNYFNTSSVEAVIRDVTE-INPNAVMIIKSTIPVGFTESIKERF-------GIE-NVIFSPEFLREG 146
Cdd:COG1004 81 FIAvgTPSDED---GSADLSYVLAAARSIGEaLKGYKVVVTKSTVPVGTADRVRAIIaeelrgaGVDfDVVSNPEFLREG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 147 KALYDNLHPSRIVIGEQSERAERFAALLQEGAIKQDIPTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNSR 226
Cdd:COG1004 158 SAVEDFLRPDRIVIGVDSERAAEVLRELYAPFVRNGTPIIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGADVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 227 QIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLLANYQS--VPNNLISAIVDANRTRKDFIADSILAR-----KPKVV 299
Cdd:COG1004 238 EVARGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARElgYDLRLLEAVEEVNERQKRRLVEKIREHlggdlKGKTI 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446627448 300 GVYRLIMKSGSDNFR-ASSIQgIMKRIKAKGVPVIVYEP-AMKE 341
Cdd:COG1004 318 AVLGLAFKPNTDDMReSPALD-IIEALLEAGARVRAYDPvAMEN 360
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
2-364 |
8.82e-41 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 148.67 E-value: 8.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 2 KITISGTGYVGLSNGILIAQN-HEVVALDIVQAKVDMLNKKQSPIV---DKEIEEYLATKdlNFRATTDkYDAYKNADYV 77
Cdd:COG0677 1 KIAVIGLGYVGLPLAVAFAKAgFRVIGFDINPERVEELNAGEDPILepgDELLAEAVAAG--RLRATTD-PEALAEADVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 78 IIATPTDYDpKTNYFNTSSVEAVIRDVTE-INPNAVMIIKSTIPVGFTESI-----KERFGIE-----NVIFSPEflRE- 145
Cdd:COG0677 78 IIAVPTPLD-EDKEPDLSYLESASETIAPhLKPGDLVVLESTVYPGTTEEVcvpilEKRSGLKagedfFLAYSPE--RIn 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 146 -GKALYDNLHPSRIV--IGEQS-ERAERF-AALLQEGAIKQdiptlfTDSTEAEAIKLFANTYLAMRVAYFNELDSYAES 220
Cdd:COG0677 155 pGNKLHELRNIPKVVggITPESaERAAALyGSVVTAGVVPV------SSIKVAEAAKLIENTYRDVNIALANELALICDR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 221 LGLNSRQIIEGVCLDPRIGNHYnnPSFGYGGYCLPKDTKQLLANYQSVPNN--LISAIVDANRTRKDFIAD---SILARK 295
Cdd:COG0677 229 LGIDVWEVIEAANTKPGFLIFY--PGPGVGGHCIPVDPYYLTWKARELGYHprLILAAREINDSMPEYVVErvvKALNEA 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446627448 296 PK-----VVGVYRLIMKSGSDNFRASSIQGIMKRIKAKGVPVIVYEPAMKEDDFFR-SRVVRDLDAFKQEADVII 364
Cdd:COG0677 307 GKslkgaRVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGeYGELVDLEEALEGADAVV 381
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
1-176 |
1.77e-38 |
|
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: 136.22 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIAQ-NHEVVALDIVQAKVDMLNKKQSPIVDKEIEEYL-ATKDLNFRATTDKYDAYKNADYVI 78
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEiGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVkANVSGRLSFTTDYSTAIEEADVIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 79 IATPTDYDPKTNYFNTSSVEAVIRDVTE-INPNAVMIIKSTIPVGFTESIKERFGIE---------NVIFSPEFLREGKA 148
Cdd:pfam03721 81 IAVGTPSKKGGGAADLKYVESAARSIAPhLKKGKVVVVKSTVPVGTTENLVKPIIEEggkkvgvdfDVASNPEFLREGSA 160
|
170 180
....*....|....*....|....*...
gi 446627448 149 LYDNLHPSRIVIGEQSERAErfaALLQE 176
Cdd:pfam03721 161 VYDLFNPDRVVIGVTEKCAE---AALEE 185
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
192-281 |
3.01e-34 |
|
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 460015 [Multi-domain] Cd Length: 92 Bit Score: 122.10 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 192 EAEAIKLFANTYLAMRVAYFNELDSYAESLGLNSRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLLANYQS--VP 269
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARElgVP 80
|
90
....*....|..
gi 446627448 270 NNLISAIVDANR 281
Cdd:pfam00984 81 ARLLEAAREVNE 92
|
|
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
1-257 |
1.52e-23 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 101.68 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIAQNH---EVVALDIVQAKVDMLNKKQSPIVDKEIEEYLAT---KDLNFRATTDKYDAYKNA 74
Cdd:PLN02353 2 VKICCIGAGYVGGPTMAVIALKCpdiEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQcrgKNLFFSTDVEKHVAEADI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 75 DYVIIATPTdydpKT---------NYFNTSSVEAVIRDVTEinPNAVMIIKSTIPVGFTESIkERF------GIENVIFS 139
Cdd:PLN02353 82 VFVSVNTPT----KTrglgagkaaDLTYWESAARMIADVSK--SDKIVVEKSTVPVKTAEAI-EKIlthnskGINFQILS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 140 -PEFLREGKALYDNLHPSRIVIGEQSERAERFAALLQEGAIKQDIP---TLFTDSTEAEAIKLFANTYLAMRVAYFNELD 215
Cdd:PLN02353 155 nPEFLAEGTAIEDLFKPDRVLIGGRETPEGQKAVQALKDVYAHWVPeerIITTNLWSAELSKLAANAFLAQRISSVNAMS 234
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446627448 216 SYAESLGLNSRQIIEGVCLDPRIGNHYNNPSFGYGGYCLPKD 257
Cdd:PLN02353 235 ALCEATGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKD 276
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
300-385 |
6.95e-16 |
|
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: 72.54 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 300 GVYRLIMKSGSDNFRASSIQGIMKRIKAKGVPVIVYEP-AMKEDD-FFRSRVVRDLDAFKQEADVIISNRMS-------A 370
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPyAMEEAReYGLTYVSDLEEALKGADAVVIATEHDefrsldpE 80
|
90
....*....|....*...
gi 446627448 371 DLADVADK---VYTRDLF 385
Cdd:smart00984 81 ELKDLMKKpvvVDGRNIL 98
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
2-257 |
1.03e-11 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 65.77 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 2 KITISGTGYVGLSNGILIAQ-NHEVVALDIVQAKVDMLNKKQSPIVDKEIEEYL--ATKDLNFRATTdkydAYKNADYVI 78
Cdd:PRK11064 5 TISVIGLGYIGLPTAAAFASrQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVktAVEGGYLRATT----TPEPADAFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 79 IATPT----DYDPKTNYfntssVEAVIRDVTEI-NPNAVMIIKSTIPVGFTESIKE---------RF----GIE---NVI 137
Cdd:PRK11064 81 IAVPTpfkgDHEPDLTY-----VEAAAKSIAPVlKKGDLVILESTSPVGATEQMAEwlaearpdlTFpqqaGEQadiNIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 138 FSPEFLREGKALYDNLHPSRiVIG----EQSERAERFAALLQEGAikqdipTLFTDSTEAEAIKLFANTYLAMRVAYFNE 213
Cdd:PRK11064 156 YCPERVLPGQVMVELIKNDR-VIGgmtpVCSARASELYKIFLEGE------CVVTNSRTAEMCKLTENSFRDVNIAFANE 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446627448 214 LDSYAESLGLNSRQIIEGVCLDPRIgnhyN--NPSFGYGGYCLPKD 257
Cdd:PRK11064 229 LSLICADQGINVWELIRLANRHPRV----NilQPGPGVGGHCIAVD 270
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
1-346 |
4.53e-08 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 54.69 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIAQNHEVVALDIVQAKVDMLNKKQSPIVDKEIEEYLATKDLNFratTDKYDAYKNADYVIIA 80
Cdd:PRK15182 7 VKIAIIGLGYVGLPLAVEFGKSRQVVGFDVNKKRILELKNGVDVNLETTEEELREARYLKF---TSEIEKIKECNFYIIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 81 TPTDYDPKTNYFNTSSVEAVIRDVTEINPNAVMIIKSTIPVGFTES-----IKERFGIE-----NVIFSPEFLREGKALY 150
Cdd:PRK15182 84 VPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEecvpiLARMSGMTfnqdfYVGYSPERINPGDKKH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 151 DNLHPSRIVIGEQSERAErfaaLLQEgaIKQDIPTLFTDSTE----AEAIKLFANTYLAMRVAYFNELDSYAESLGLNSR 226
Cdd:PRK15182 164 RLTNIKKITSGSTAQIAE----LIDE--VYQQIISAGTYKAEsikvAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 227 QIIEGVcldpriGNHYNNPSFG---YGGYCLPKDTKQLLANYQSVpnNLISAIVDANRTRKDFIAD--------SILARK 295
Cdd:PRK15182 238 AVLRAA------GSKWNFLPFRpglVGGHCIGVDPYYLTHKSQGI--GYYPEIILAGRRLNDNMGNyvseqlikAMIKKG 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446627448 296 PKVVGVYRLIM----KSGSDNFRASSIQGIMKRIKAKGVPVIVYEPAMKEDDFFR 346
Cdd:PRK15182 310 INVEGSSVLILgftfKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEVRR 364
|
|
| UDPG_MGDP_dh_C |
pfam03720 |
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ... |
300-364 |
1.52e-06 |
|
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: 46.41 E-value: 1.52e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446627448 300 GVYRLIMKSGSDNFRASSIQGIMKRIKAKGVPVIVYEP----AMKEDDFFRSRVVRDLDAFKQEADVII 364
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPyvpeEAIEALGDGVTLVDDLEEALKGADAIV 69
|
|
| PanE |
COG1893 |
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
1-180 |
1.65e-05 |
|
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 441497 [Multi-domain] Cd Length: 305 Bit Score: 46.39 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTG----YVGlsnGILIAQNHEVVALDiVQAKVDMLNKKqsPIVDKEIEEYLATkdLNFRATTDKyDAYKNADY 76
Cdd:COG1893 1 MKIAILGAGaiggLLG---ARLARAGHDVTLVA-RGAHAEALREN--GLRLESPDGDRTT--VPVPAVTDP-EELGPADL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 77 VIIATPTdYDpktnyfntssVEAVIRDVTE-INPNAVMIiksTI--PVGFTESIKERFGIENVIFS---PEFLREGKALY 150
Cdd:COG1893 72 VLVAVKA-YD----------LEAAAEALAPlLGPDTVVL---SLqnGLGHEERLAEALGAERVLGGvvtIGATREEPGVV 137
|
170 180 190
....*....|....*....|....*....|....
gi 446627448 151 DNLHPSRIVIGE----QSERAERFAALLQEGAIK 180
Cdd:COG1893 138 RHTGGGRLVLGEldggPSERLEALAELLEAAGIP 171
|
|
| LDH_MDH_like |
cd00650 |
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members ... |
4-137 |
7.73e-04 |
|
NAD-dependent, lactate dehydrogenase-like, 2-hydroxycarboxylate dehydrogenase family; Members of this family include ubiquitous enzymes like L-lactate dehydrogenases (LDH), L-2-hydroxyisocaproate dehydrogenases, and some malate dehydrogenases (MDH). LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH/MDH-like proteins are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.
Pssm-ID: 133419 [Multi-domain] Cd Length: 263 Bit Score: 40.77 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 4 TISGTGYVG--LSNGILIAQNH---EVVALDIVQAKVDmlnkkqspIVDKEIEEYLA-TKDLNFRATTDKYDAYKNADYV 77
Cdd:cd00650 3 VIGAGGNVGpaLAFGLADGSVLlaiELVLYDIDEEKLK--------GVAMDLQDAVEpLADIKVSITDDPYEAFKDADVV 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446627448 78 IIAT-----PTDYDPKTNYFNTSSVEAVIRDVTEINPNAVMIIKSTiPVGF-TESIKERFGI--ENVI 137
Cdd:cd00650 75 IITAgvgrkPGMGRLDLLKRNVPIVKEIGDNIEKYSPDAWIIVVSN-PVDIiTYLVWRYSGLpkEKVI 141
|
|
| Mdh |
COG0039 |
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ... |
1-80 |
1.44e-03 |
|
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439809 [Multi-domain] Cd Length: 302 Bit Score: 40.00 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIAQN---HEVVALDIVQAKV--DMLnkkqspivdkEIEEYLATKDLNFRATTDKYDAYKNAD 75
Cdd:COG0039 1 MKVAIIGAGNVGSTLAFRLASGglaDELVLIDINEGKAegEAL----------DLADAFPLLGFDVKITAGDYEDLADAD 70
|
....*
gi 446627448 76 YVIIA 80
Cdd:COG0039 71 VVVIT 75
|
|
| gpsA |
PRK00094 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; |
1-83 |
8.18e-03 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
Pssm-ID: 234629 [Multi-domain] Cd Length: 325 Bit Score: 37.74 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627448 1 MKITISGTGYVGLSNGILIAQN-HEVVALDIVQAKVDMLNKkqspivDKEIEEYLatKDLNF----RATTDKYDAYKNAD 75
Cdd:PRK00094 2 MKIAVLGAGSWGTALAIVLARNgHDVTLWARDPEQAAEINA------DRENPRYL--PGIKLpdnlRATTDLAEALADAD 73
|
....*...
gi 446627448 76 YVIIATPT 83
Cdd:PRK00094 74 LILVAVPS 81
|
|
| |
