|
Name |
Accession |
Description |
Interval |
E-value |
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
1-430 |
0e+00 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 637.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVRLHELINYAYENNALIFTSNKEEAFDDVEFI 80
Cdd:COG1004 1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDLAEAVAEADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAVGTPPLLDGTADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEEKLKG-RHTVHIVSNPEFLREGSGI 159
Cdd:COG1004 81 FIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRGaGVDFDVVSNPEFLREGSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 160 YDFFHGDRIVIGADSEEVARRVESLYSELCLET---YVTDIKSAEMIKYASNAFLATKISFINEISNICEKVGANVLDVA 236
Cdd:COG1004 161 EDFLRPDRIVIGVDSERAAEVLRELYAPFVRNGtpiIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGADVEEVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 237 KGMGMDKRIGASFLNAGIGYGGSCFPKDTKALVQIAGNVAHDFRLLKAVIEVNNKQQLLLIEKAKKVM--NMSKKRIAVL 314
Cdd:COG1004 241 RGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYDLRLLEAVEEVNERQKRRLVEKIREHLggDLKGKTIAVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 315 GASFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKAIQYVKNIFGDAIQYSRCIDESIRDASAVFIVTEWEDIQTYPLE 394
Cdd:COG1004 321 GLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRLLPDDITYADDAYEALEGADALVILTEWPEFRALDFA 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 446627584 395 KYVQLMREPILFDGRNCYTDEDVKKQKIDYYSVGRK 430
Cdd:COG1004 401 RLKALMKGPVIFDGRNLLDPEELRAAGFTYYGIGRP 436
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
1-410 |
2.92e-154 |
|
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: 443.21 E-value: 2.92e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVRLHELINYAYENNALIFTSNKEEAFDDVEFI 80
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEEAIRDADVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAVGTPPLLDGTADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEEK--LKGRHTVHIVSNPEFLREGSG 158
Cdd:TIGR03026 81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERsgLKLGEDFYLAYNPEFLREGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 159 IYDFFHGDRIVIGADsEEVARRVESLYSELCLETY-VTDIKSAEMIKYASNAFLATKISFINEISNICEKVGANVLDVAK 237
Cdd:TIGR03026 161 VHDLLHPDRIVGGET-EEAGEAVAELYSPIIDGPVlVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 238 GMGMDKRIGASFLNAGIGYGGSCFPKDTKALVQIAGNVAHDFRLLKAVIEVNNKQQLLLIEKAKKVM-NMSKKRIAVLGA 316
Cdd:TIGR03026 240 AAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLLgPLKGKTVLILGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 317 SFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKAIQYVKNIFGDAIQysrcIDESIRDASAVFIVTEWEDIQTYPLEKY 396
Cdd:TIGR03026 320 AFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDD----LEEALKGADALVILTDHSEFKDLDLEKI 395
|
410
....*....|....
gi 446627584 397 VQLMREPILFDGRN 410
Cdd:TIGR03026 396 KDLMKGKVVVDTRN 409
|
|
| UDPGDh_AglM |
NF041297 |
UDP-glucose 6-dehydrogenase AglM; |
1-416 |
9.45e-119 |
|
UDP-glucose 6-dehydrogenase AglM;
Pssm-ID: 469194 [Multi-domain] Cd Length: 429 Bit Score: 353.44 E-value: 9.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVRLHELINyAYENNALIFTSNKEeAFDDVEFI 80
Cdd:NF041297 1 MNVSVIGSGYVGTTVAACFADLGHDVVNVDIDEDIVATINDGEAPIHEPGLDELVA-EHAGDRLRATTDYD-AVLETDVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAVGTPPLLDGTADLTYIQSACNDIG--LYATNDI-IVVTKSTV-PVGTNDVMKGWIEEKLKGR--HTVHIVSNPEFLR 154
Cdd:NF041297 79 FLALPTPSNDDGSIDLSIMEAGAESLGeaLAEKDDDhLVVVKSTVvPGTTEEVIAPALEDASGKTagEDFGVAMNPEFLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 155 EGSGIYDFFHGDRIVIGADSEEVARRVESLYSELCLET---YV-TDIKSAEMIKYASNAFLATKISFINEISNICEKVGA 230
Cdd:NF041297 159 EGSAVEDFLNPDKVVLGADDDRALDRLREVYEPLVEAAdapVVeTGIREAEMIKYANNAFLASKVSLINDLGNICKEFGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 231 NVLDVAKGMGMDKRIGASFLNAGIGYGGSCFPKDTKALVQIAGNVAHDFRLLKAVIEVNNKQQLLLIEKAKKVMNMSKKR 310
Cdd:NF041297 239 DAYEVADAIGLDDRIGEQFLRSGVGWGGSCFPKDVAAIIAAAREAGYEPALLEAAVEVNDRQPERLLDLLDEHVDVAGER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 311 IAVLGASFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKAIQYVKNIFGDaIQYSRCIDESIRDASAVFIVTEWEDIQT 390
Cdd:NF041297 319 VAVLGLAFKPGTDDVRNSRAIPVIEGLQERGADVVAYDPVATENMRERFPD-IEYADSAADALDGADGALVVTDWDEFAA 397
|
410 420
....*....|....*....|....*.
gi 446627584 391 ypLEKYVQLMREPILFDGRNCYTDED 416
Cdd:NF041297 398 --LDEEFDAMATPVVVDGRRIVERRD 421
|
|
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
1-429 |
4.22e-81 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 258.07 E-value: 4.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLA-KLGH-SVTCFDIDDEKIERIKQGDLPIYEVRLHELINYAYENNaLIFTSNKEEAFDDVE 78
Cdd:PLN02353 2 VKICCIGAGYVGGPTMAVIAlKCPDiEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKN-LFFSTDVEKHVAEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 79 FIFIAVGTPPLLDG-----TADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEEKLKGRHtVHIVSNPEFL 153
Cdd:PLN02353 81 IVFVSVNTPTKTRGlgagkAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGIN-FQILSNPEFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 154 REGSGIYDFFHGDRIVIGA-DSEEVARRVESL---YSELCLETYV--TDIKSAEMIKYASNAFLATKISFINEISNICEK 227
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGrETPEGQKAVQALkdvYAHWVPEERIitTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 228 VGANVLDVAKGMGMDKRIGASFLNAGIGYGGSCFPKDTKALVQIA-----GNVAHDFrllKAVIEVNNKQQLLLIEKAKK 302
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICecnglPEVAEYW---KQVIKMNDYQKSRFVNRVVS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 303 VM--NMSKKRIAVLGASFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKA---------------------IQYVKNIF 359
Cdd:PLN02353 317 SMfnTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVteeqiqrdlsmnkfdwdhprhLQPMSPTA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446627584 360 GDAIQYSRCIDESIRDASAVFIVTEWEDIQTYPLEKYVQLMREP-ILFDGRNCYTDEDVKKQKIDYYSVGR 429
Cdd:PLN02353 397 VKQVSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPaFVFDGRNVLDHEKLREIGFIVYSIGK 467
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
1-184 |
3.83e-64 |
|
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: 204.40 E-value: 3.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVRLHELINYAYENNaLIFTSNKEEAFDDVEFI 80
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGR-LSFTTDYSTAIEEADVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAVGTPPL-LDGTADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEEKLKGRHTVHI--VSNPEFLREGS 157
Cdd:pfam03721 80 FIAVGTPSKkGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFdvASNPEFLREGS 159
|
170 180
....*....|....*....|....*..
gi 446627584 158 GIYDFFHGDRIVIGADSEEVARRVESL 184
Cdd:pfam03721 160 AVYDLFNPDRVVIGVTEKCAEAALEEL 186
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
312-412 |
2.33e-29 |
|
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: 110.29 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 312 AVLGASFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKAIQYVKNIFgdaIQYSRCIDESIRDASAVFIVTEWEDIQTY 391
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYG---LTYVSDLEEALKGADAVVIATEHDEFRSL 77
|
90 100
....*....|....*....|.
gi 446627584 392 PLEKYVQLMREPILFDGRNCY 412
Cdd:smart00984 78 DPEELKDLMKKPVVVDGRNIL 98
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
5-91 |
6.01e-03 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 38.46 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 5 IVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKqgdlpiyEVRLHELINYAYENNALIFTSNKEEAFDdveFIFIAV 84
Cdd:cd05188 140 VLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAK-------ELGADHVIDYKEEDLEEELRLTGGGGAD---VVIDAV 209
|
....*..
gi 446627584 85 GTPPLLD 91
Cdd:cd05188 210 GGPETLA 216
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
1-430 |
0e+00 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 637.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVRLHELINYAYENNALIFTSNKEEAFDDVEFI 80
Cdd:COG1004 1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDLAEAVAEADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAVGTPPLLDGTADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEEKLKG-RHTVHIVSNPEFLREGSGI 159
Cdd:COG1004 81 FIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRGaGVDFDVVSNPEFLREGSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 160 YDFFHGDRIVIGADSEEVARRVESLYSELCLET---YVTDIKSAEMIKYASNAFLATKISFINEISNICEKVGANVLDVA 236
Cdd:COG1004 161 EDFLRPDRIVIGVDSERAAEVLRELYAPFVRNGtpiIVTDLRSAELIKYAANAFLATKISFINEIANLCEKVGADVEEVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 237 KGMGMDKRIGASFLNAGIGYGGSCFPKDTKALVQIAGNVAHDFRLLKAVIEVNNKQQLLLIEKAKKVM--NMSKKRIAVL 314
Cdd:COG1004 241 RGIGLDSRIGPKFLYAGIGYGGSCFPKDVRALIATARELGYDLRLLEAVEEVNERQKRRLVEKIREHLggDLKGKTIAVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 315 GASFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKAIQYVKNIFGDAIQYSRCIDESIRDASAVFIVTEWEDIQTYPLE 394
Cdd:COG1004 321 GLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVAMENARRLLPDDITYADDAYEALEGADALVILTEWPEFRALDFA 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 446627584 395 KYVQLMREPILFDGRNCYTDEDVKKQKIDYYSVGRK 430
Cdd:COG1004 401 RLKALMKGPVIFDGRNLLDPEELRAAGFTYYGIGRP 436
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
1-410 |
2.92e-154 |
|
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: 443.21 E-value: 2.92e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVRLHELINYAYENNALIFTSNKEEAFDDVEFI 80
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEEAIRDADVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAVGTPPLLDGTADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEEK--LKGRHTVHIVSNPEFLREGSG 158
Cdd:TIGR03026 81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERsgLKLGEDFYLAYNPEFLREGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 159 IYDFFHGDRIVIGADsEEVARRVESLYSELCLETY-VTDIKSAEMIKYASNAFLATKISFINEISNICEKVGANVLDVAK 237
Cdd:TIGR03026 161 VHDLLHPDRIVGGET-EEAGEAVAELYSPIIDGPVlVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 238 GMGMDKRIGASFLNAGIGYGGSCFPKDTKALVQIAGNVAHDFRLLKAVIEVNNKQQLLLIEKAKKVM-NMSKKRIAVLGA 316
Cdd:TIGR03026 240 AAGTDPRIGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLLgPLKGKTVLILGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 317 SFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKAIQYVKNIFGDAIQysrcIDESIRDASAVFIVTEWEDIQTYPLEKY 396
Cdd:TIGR03026 320 AFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPEEEVKGLPSIDD----LEEALKGADALVILTDHSEFKDLDLEKI 395
|
410
....*....|....
gi 446627584 397 VQLMREPILFDGRN 410
Cdd:TIGR03026 396 KDLMKGKVVVDTRN 409
|
|
| UDPGDh_AglM |
NF041297 |
UDP-glucose 6-dehydrogenase AglM; |
1-416 |
9.45e-119 |
|
UDP-glucose 6-dehydrogenase AglM;
Pssm-ID: 469194 [Multi-domain] Cd Length: 429 Bit Score: 353.44 E-value: 9.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVRLHELINyAYENNALIFTSNKEeAFDDVEFI 80
Cdd:NF041297 1 MNVSVIGSGYVGTTVAACFADLGHDVVNVDIDEDIVATINDGEAPIHEPGLDELVA-EHAGDRLRATTDYD-AVLETDVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAVGTPPLLDGTADLTYIQSACNDIG--LYATNDI-IVVTKSTV-PVGTNDVMKGWIEEKLKGR--HTVHIVSNPEFLR 154
Cdd:NF041297 79 FLALPTPSNDDGSIDLSIMEAGAESLGeaLAEKDDDhLVVVKSTVvPGTTEEVIAPALEDASGKTagEDFGVAMNPEFLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 155 EGSGIYDFFHGDRIVIGADSEEVARRVESLYSELCLET---YV-TDIKSAEMIKYASNAFLATKISFINEISNICEKVGA 230
Cdd:NF041297 159 EGSAVEDFLNPDKVVLGADDDRALDRLREVYEPLVEAAdapVVeTGIREAEMIKYANNAFLASKVSLINDLGNICKEFGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 231 NVLDVAKGMGMDKRIGASFLNAGIGYGGSCFPKDTKALVQIAGNVAHDFRLLKAVIEVNNKQQLLLIEKAKKVMNMSKKR 310
Cdd:NF041297 239 DAYEVADAIGLDDRIGEQFLRSGVGWGGSCFPKDVAAIIAAAREAGYEPALLEAAVEVNDRQPERLLDLLDEHVDVAGER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 311 IAVLGASFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKAIQYVKNIFGDaIQYSRCIDESIRDASAVFIVTEWEDIQT 390
Cdd:NF041297 319 VAVLGLAFKPGTDDVRNSRAIPVIEGLQERGADVVAYDPVATENMRERFPD-IEYADSAADALDGADGALVVTDWDEFAA 397
|
410 420
....*....|....*....|....*.
gi 446627584 391 ypLEKYVQLMREPILFDGRNCYTDED 416
Cdd:NF041297 398 --LDEEFDAMATPVVVDGRRIVERRD 421
|
|
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
1-429 |
4.22e-81 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 258.07 E-value: 4.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLA-KLGH-SVTCFDIDDEKIERIKQGDLPIYEVRLHELINYAYENNaLIFTSNKEEAFDDVE 78
Cdd:PLN02353 2 VKICCIGAGYVGGPTMAVIAlKCPDiEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQCRGKN-LFFSTDVEKHVAEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 79 FIFIAVGTPPLLDG-----TADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEEKLKGRHtVHIVSNPEFL 153
Cdd:PLN02353 81 IVFVSVNTPTKTRGlgagkAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGIN-FQILSNPEFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 154 REGSGIYDFFHGDRIVIGA-DSEEVARRVESL---YSELCLETYV--TDIKSAEMIKYASNAFLATKISFINEISNICEK 227
Cdd:PLN02353 160 AEGTAIEDLFKPDRVLIGGrETPEGQKAVQALkdvYAHWVPEERIitTNLWSAELSKLAANAFLAQRISSVNAMSALCEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 228 VGANVLDVAKGMGMDKRIGASFLNAGIGYGGSCFPKDTKALVQIA-----GNVAHDFrllKAVIEVNNKQQLLLIEKAKK 302
Cdd:PLN02353 240 TGADVSQVSHAVGKDSRIGPKFLNASVGFGGSCFQKDILNLVYICecnglPEVAEYW---KQVIKMNDYQKSRFVNRVVS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 303 VM--NMSKKRIAVLGASFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKA---------------------IQYVKNIF 359
Cdd:PLN02353 317 SMfnTVSGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQVteeqiqrdlsmnkfdwdhprhLQPMSPTA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446627584 360 GDAIQYSRCIDESIRDASAVFIVTEWEDIQTYPLEKYVQLMREP-ILFDGRNCYTDEDVKKQKIDYYSVGR 429
Cdd:PLN02353 397 VKQVSVVWDAYEATKGAHGICILTEWDEFKTLDYQKIYDNMQKPaFVFDGRNVLDHEKLREIGFIVYSIGK 467
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
2-412 |
9.51e-74 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 236.88 E-value: 9.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 2 KITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVRlHELINYAYENNALIFTSNkEEAFDDVEFIF 81
Cdd:COG0677 1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTD-PEALAEADVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 82 IAVGTPPLLDGTADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEEK---LKGRHTVHIVSNPEflREGSG 158
Cdd:COG0677 79 IAVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKrsgLKAGEDFFLAYSPE--RINPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 159 --IYDFFHGDRIViGADSEEVARRVESLYSELC-LETY-VTDIKSAEMIKYASNAFLATKISFINEISNICEKVGANVLD 234
Cdd:COG0677 157 nkLHELRNIPKVV-GGITPESAERAAALYGSVVtAGVVpVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 235 VAKGMGMDKRigasFL--NAGIGYGGSCFPKDTKALVQIAGNVAHDFRLLKAVIEVNNKQQLLLIEKAKKVMNMSKK--- 309
Cdd:COG0677 236 VIEAANTKPG----FLifYPGPGVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKALNEAGKslk 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 310 --RIAVLGASFKPNTDDIREASSLIIIEALLNIGAEIVLYDPkaiqYVKNIFGDAIQYSRC-IDESIRDASAVFIVTEWE 386
Cdd:COG0677 312 gaRVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDP----YVDEEEVEGEYGELVdLEEALEGADAVVLAVDHD 387
|
410 420
....*....|....*....|....*.
gi 446627584 387 DIQTYPLEKyVQLMREPILFDGRNCY 412
Cdd:COG0677 388 EFDELDPEE-LRLKGAKVVVDTRGVL 412
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
1-184 |
3.83e-64 |
|
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: 204.40 E-value: 3.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVRLHELINYAYENNaLIFTSNKEEAFDDVEFI 80
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGR-LSFTTDYSTAIEEADVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAVGTPPL-LDGTADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEEKLKGRHTVHI--VSNPEFLREGS 157
Cdd:pfam03721 80 FIAVGTPSKkGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFdvASNPEFLREGS 159
|
170 180
....*....|....*....|....*..
gi 446627584 158 GIYDFFHGDRIVIGADSEEVARRVESL 184
Cdd:pfam03721 160 AVYDLFNPDRVVIGVTEKCAEAALEEL 186
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
1-349 |
5.30e-53 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 182.14 E-value: 5.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKlGHSVTCFDIDDEKIERIKQGDLPIYEVRLHELInyAYENNALIFTSNKEEAFDDVEFI 80
Cdd:PRK15057 1 MKITISGTGYVGLSNGLLIAQ-NHEVVALDILPSRVAMLNDRISPIVDKEIQQFL--QSDKIHFNATLDKNEAYRDADYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAvgTPPLLDGTADL---TYIQSACNDIgLYATNDIIVVTKSTVPVGTNDVMKgwieeklKGRHTVHIVSNPEFLREGS 157
Cdd:PRK15057 78 IIA--TPTDYDPKTNYfntSSVESVIKDV-VEINPYAVMVIKSTVPVGFTAAMH-------KKYRTENIIFSPEFLREGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 158 GIYDFFHGDRIVIGADSEEvARRVESLYSELCLE----TYVTDIKSAEMIKYASNAFLATKISFINEISNICEKVGANVL 233
Cdd:PRK15057 148 ALYDNLHPSRIVIGERSER-AERFAALLQEGAIKqnipTLFTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLNTR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 234 DVAKGMGMDKRIGASFLNAGIGYGGSCFPKDTKALVQIAGNVAHDfrLLKAVIEVNNKQQLLLiekAKKVMNMSKKRIAV 313
Cdd:PRK15057 227 QIIEGVCLDPRIGNHYNNPSFGYGGYCLPKDTKQLLANYQSVPNN--LISAIVDANRTRKDFI---ADAILSRKPQVVGI 301
|
330 340 350
....*....|....*....|....*....|....*.
gi 446627584 314 LGASFKPNTDDIREASSLIIIEALLNIGAEIVLYDP 349
Cdd:PRK15057 302 YRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEP 337
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
199-290 |
5.05e-50 |
|
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: 164.47 E-value: 5.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 199 SAEMIKYASNAFLATKISFINEISNICEKVGANVLDVAKGMGMDKRIGASFLNAGIGYGGSCFPKDTKALVQIAGNVAHD 278
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRIGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
|
90
....*....|..
gi 446627584 279 FRLLKAVIEVNN 290
Cdd:pfam00984 81 ARLLEAAREVNE 92
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
2-337 |
6.80e-37 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 139.73 E-value: 6.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 2 KITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVRLHELINYAYENNALIFTSNKEEAfdDVeFIf 81
Cdd:PRK11064 5 TISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPA--DA-FL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 82 IAVGTPPLLDGTADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEE---KLKGRHT------VHIVSNPEF 152
Cdd:PRK11064 81 IAVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEarpDLTFPQQageqadINIAYCPER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 153 LREGSGIYDFFHGDRiVIGADSEEVARRVESLYsELCL--ETYVTDIKSAEMIKYASNAFLATKISFINEISNICEKVGA 230
Cdd:PRK11064 161 VLPGQVMVELIKNDR-VIGGMTPVCSARASELY-KIFLegECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 231 NVLDVAKGMGMDKRIgaSFLNAGIGYGGSCFPKDTKALVQIAGNVAhdfRLLKAVIEVNNKQQLLLIEKAKKV----MNM 306
Cdd:PRK11064 239 NVWELIRLANRHPRV--NILQPGPGVGGHCIAVDPWFIVAQNPQQA---RLIRTAREVNDGKPHWVIDQVKAAvadcLAA 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 446627584 307 SKKR-----IAVLGASFKPNTDDIREASSLIIIEAL 337
Cdd:PRK11064 314 TDKRasevkIACFGLAFKPNIDDLRESPAMEIAELI 349
|
|
| UDPG_MGDP_dh_C |
pfam03720 |
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ... |
312-412 |
9.95e-32 |
|
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: 116.52 E-value: 9.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 312 AVLGASFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKAIQYVKNIFGDAIQYSRCIDESIRDASAVFIVTEWEDIQTY 391
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGDGVTLVDDLEEALKGADAIVILTDHDEFKSL 80
|
90 100
....*....|....*....|.
gi 446627584 392 PLEKYVQLMREPILFDGRNCY 412
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 ... |
312-412 |
2.33e-29 |
|
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: 110.29 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 312 AVLGASFKPNTDDIREASSLIIIEALLNIGAEIVLYDPKAIQYVKNIFgdaIQYSRCIDESIRDASAVFIVTEWEDIQTY 391
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYG---LTYVSDLEEALKGADAVVIATEHDEFRSL 77
|
90 100
....*....|....*....|.
gi 446627584 392 PLEKYVQLMREPILFDGRNCY 412
Cdd:smart00984 78 DPEELKDLMKKPVVVDGRNIL 98
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
1-349 |
9.58e-16 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 78.96 E-value: 9.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKlGHSVTCFDIDDEKIERIKQGdlpiYEVRLHELINYAYENNALIFTSNKEEaFDDVEFI 80
Cdd:PRK15182 7 VKIAIIGLGYVGLPLAVEFGK-SRQVVGFDVNKKRILELKNG----VDVNLETTEEELREARYLKFTSEIEK-IKECNFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAVGTPPLLDGTADLTYIQSACNDIGLYATNDIIVVTKSTVPVGTNDVMKGWIEEKLKG---RHTVHIVSNPEFLREGS 157
Cdd:PRK15182 81 IITVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARMSGmtfNQDFYVGYSPERINPGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 158 GIYDFFHGDRIVIGAdSEEVARRVESLYSEL-CLETYVTD-IKSAEMIKYASNAFLATKISFINEISNICEKVGANVLDV 235
Cdd:PRK15182 161 KKHRLTNIKKITSGS-TAQIAELIDEVYQQIiSAGTYKAEsIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 236 AKGMGMDkrigASFLNAGIGY-GGSCFPKDTKALVQIAGNVAHDFRLLKAVIEVNNK-----QQLLLIEKAKKVMNMSKK 309
Cdd:PRK15182 240 LRAAGSK----WNFLPFRPGLvGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNmgnyvSEQLIKAMIKKGINVEGS 315
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446627584 310 RIAVLGASFKPNTDDIREASSLIIIEALLNIGAEIVLYDP 349
Cdd:PRK15182 316 SVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDP 355
|
|
| PanE |
COG1893 |
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
1-209 |
9.40e-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: 44.08 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDiDDEKIERIKQGDLPIyevrlhELINYAYENNALIFTSNKEEAfDDVEFI 80
Cdd:COG1893 1 MKIAILGAGAIGGLLGARLARAGHDVTLVA-RGAHAEALRENGLRL------ESPDGDRTTVPVPAVTDPEEL-GPADLV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 81 FIAV---GTPPLLDGTADL----TYIQSACNDIGLYATndiivvtkstvpvgtndvmkgwIEEKLKGRHTVHIVSNPEFL 153
Cdd:COG1893 73 LVAVkayDLEAAAEALAPLlgpdTVVLSLQNGLGHEER----------------------LAEALGAERVLGGVVTIGAT 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 154 REGSGIYDFFHGDRIVIGADSEEVARRVESLYSELC---LETYVT-DIKSAEMIKYASNA 209
Cdd:COG1893 131 REEPGVVRHTGGGRLVLGELDGGPSERLEALAELLEaagIPVEVSdDIRGALWEKLLLNA 190
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
2-155 |
4.27e-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: 40.64 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 2 KITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQgdlpiyevrlhELINYAYENN-----ALIFTSNKEEAFDD 76
Cdd:pfam01210 1 KIAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINT-----------THENVRYLPGiklpeNLKATTDLAEALKG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 77 VEFIFIAVGTpplldgtadlTYIQSACNDI-GLYATNDIIV-VTKStVPVGTNDVMKGWIEEKLKGRHTVHIVSNPEFLR 154
Cdd:pfam01210 70 ADIIVIVVPS----------QALREVLKQLkGLLKPDAILVsLSKG-IEPGTLKLLSEVIEEELGIQPPIAVLSGPSHAE 138
|
.
gi 446627584 155 E 155
Cdd:pfam01210 139 E 139
|
|
| PRK06522 |
PRK06522 |
2-dehydropantoate 2-reductase; Reviewed |
1-84 |
8.40e-04 |
|
2-dehydropantoate 2-reductase; Reviewed
Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 40.99 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPIYEVrlhelinyayENNALIFTSNKEEAFDDVEFI 80
Cdd:PRK06522 1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNENGLRLEDG----------EITVPVLAADDPAELGPQDLV 70
|
....
gi 446627584 81 FIAV 84
Cdd:PRK06522 71 ILAV 74
|
|
| gpsA |
PRK00094 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; |
1-84 |
4.61e-03 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
Pssm-ID: 234629 [Multi-domain] Cd Length: 325 Bit Score: 38.90 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQ-GDLPIY--EVRLHElinyayennALIFTSNKEEAFDDV 77
Cdd:PRK00094 2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINAdRENPRYlpGIKLPD---------NLRATTDLAEALADA 72
|
....*..
gi 446627584 78 EFIFIAV 84
Cdd:PRK00094 73 DLILVAV 79
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
1-46 |
5.16e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 38.51 E-value: 5.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKQGDLPI 46
Cdd:COG0569 96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLV 141
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
5-91 |
6.01e-03 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 38.46 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446627584 5 IVGTGYVGLITGVGLAKLGHSVTCFDIDDEKIERIKqgdlpiyEVRLHELINYAYENNALIFTSNKEEAFDdveFIFIAV 84
Cdd:cd05188 140 VLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAK-------ELGADHVIDYKEEDLEEELRLTGGGGAD---VVIDAV 209
|
....*..
gi 446627584 85 GTPPLLD 91
Cdd:cd05188 210 GGPETLA 216
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1-30 |
9.44e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 38.00 E-value: 9.44e-03
10 20 30
....*....|....*....|....*....|
gi 446627584 1 MKITIVGTGYVGLITGVGLAKLGHSVTCFD 30
Cdd:COG0654 4 TDVLIVGGGPAGLALALALARAGIRVTVVE 33
|
|
| |
