|
Name |
Accession |
Description |
Interval |
E-value |
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
2-381 |
0e+00 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 576.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 2 KKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEVVRTGNLRAVSKPEQADAFFVVV 81
Cdd:PRK11064 4 ETISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFLIAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 82 PTPFKQNHRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIYKERPEL--------KDKIYIAYCPERVLP 153
Cdd:PRK11064 84 PTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLtfpqqageQADINIAYCPERVLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 154 GNTLYELVHNDRVIGGVNPESTAKAIEFYSAFVQGKLHPTNARTAEMCKLTENSSRDSQIAFANELSMICDKAGINVWEL 233
Cdd:PRK11064 164 GQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINVWEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 234 IELANKHPRVNILQPGCGVGGHCIAVDPWFIVSDYPEQAQIIKRARETNDYKADWCANKVMEACQQFVEKNDR---EPVV 310
Cdd:PRK11064 244 IRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKrasEVKI 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492255706 311 ACMGLAFKPNIDDLRESPAKYIASRIVSESRAEVLIVEPNV-----ASHASFHLTDYREAYQKADIVVWLVRHTPF 381
Cdd:PRK11064 324 ACFGLAFKPNIDDLRESPAMEIAELIAQWHSGETLVVEPNIhqlpkKLDGLVTLVSLDEALATADVLVMLVDHSQF 399
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
3-398 |
0e+00 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 513.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 3 KVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPElDQIVKEVVRTGNLRAVSKPE---QADAFFV 79
Cdd:COG0677 1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTDPEalaEADVVII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 80 VVPTPFKQNHRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIYKERPELK--DKIYIAYCPERVLPGNTL 157
Cdd:COG0677 80 AVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKagEDFFLAYSPERINPGNKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 158 YELVHNDRVIGGVNPESTAKAIEFYSAFVQGKLHP-TNARTAEMCKLTENSSRDSQIAFANELSMICDKAGINVWELIEL 236
Cdd:COG0677 160 HELRNIPKVVGGITPESAERAAALYGSVVTAGVVPvSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 237 ANKHPRVNILQPGCGVGGHCIAVDPWFIVSDYPE---QAQIIKRARETNDYKADWCANKVMEACQQfVEKNDREPVVACM 313
Cdd:COG0677 240 ANTKPGFLIFYPGPGVGGHCIPVDPYYLTWKARElgyHPRLILAAREINDSMPEYVVERVVKALNE-AGKSLKGARVLVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 314 GLAFKPNIDDLRESPAKYIAsRIVSESRAEVLIVEPNV----ASHASFHLTDYREAYQKADIVVWLVRHTPFVELPREES 389
Cdd:COG0677 319 GLAYKENVDDLRESPALDII-EELREYGAEVDVHDPYVdeeeVEGEYGELVDLEEALEGADAVVLAVDHDEFDELDPEEL 397
|
410
....*....|....
gi 492255706 390 KLE-----LDFCGV 398
Cdd:COG0677 398 RLKgakvvVDTRGV 411
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
2-390 |
7.62e-135 |
|
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: 391.97 E-value: 7.62e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 2 KKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEVVRTGNLRAVSKPE----QADAF 77
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEeairDADVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 78 FVVVPTPFKQNHRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIYKERPELKDK-IYIAYCPERVLPGNT 156
Cdd:TIGR03026 81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEdFYLAYNPEFLREGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 157 LYELVHNDRVIGGVNPESTAKAIEFYSAFVQGKLHPTNARTAEMCKLTENSSRDSQIAFANELSMICDKAGINVWELIEL 236
Cdd:TIGR03026 161 VHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 237 ANKHPR--VNILQPGCGVGGHCIAVDPWFIVSDYPE---QAQIIKRARETNDYKADWCANKVMEACQQFVEKNdrepvVA 311
Cdd:TIGR03026 241 AGTDPRigFNFLNPGPGVGGHCIPKDPLALIAKAKElgyNPELIEAAREINDSQPDYVVEKIKDLLGPLKGKT-----VL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 312 CMGLAFKPNIDDLRESPAKYIASRIVSESrAEVLIVEPNVASHASFHLTDYREAYQ---KADIVVWLVRHTPFVELPREE 388
Cdd:TIGR03026 316 ILGLAFKPNTDDVRESPALDIIELLKEKG-AKVKAYDPLVPEEEVKGLPSIDDLEEalkGADALVILTDHSEFKDLDLEK 394
|
..
gi 492255706 389 SK 390
Cdd:TIGR03026 395 IK 396
|
|
| UDPMaNacDH_Arch |
NF040825 |
UDP-N-acetyl-D-mannosamine dehydrogenase; |
3-388 |
9.75e-112 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase;
Pssm-ID: 468765 [Multi-domain] Cd Length: 418 Bit Score: 333.65 E-value: 9.75e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 3 KVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEVVRTGNLRAVSKPEQ---ADAFFV 79
Cdd:NF040825 2 KIAVIGLGYIGLPTAIMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTDPEDlkgADAFII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 80 VVPTPFKQNhRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIyKERPELKDKI--YIAYCPERVLPGNTL 157
Cdd:NF040825 82 CVQTPLKED-KPDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLL-EELTGLKEGEdfYMAHAPERVMPGRIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 158 YELVHNDRVIGGVNPESTAKAIEFYSAFVQGKLHPTNARTAEMCKLTENSSRDSQIAFANELSMICDKAGINVWELIELA 237
Cdd:NF040825 160 KELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTFRDVNIALANEFALLAHQYGVNVFEAIELA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 238 NKHPRVNILQPGCGVGGHCIAVDPWFIVSDYPEQAQIIKRARETNDYKADWCANKVMEACQQfVEKNDREPVVACMGLAF 317
Cdd:NF040825 240 NTHPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLAREINEDMPLFAKDLLFEALEE-ANVPPEEAVVTVLGLAY 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492255706 318 KPNIDDLRESPA-KYIasRIVSESRAEVLIVEPNV-ASHASFhltdyREAYQKADIVVWLVRHTPFVELPREE 388
Cdd:NF040825 319 KGDTDDTRNSPAlKFV--ELIEDDVKEVRTYDPYVgGTHESL-----EDAVKGADAIVIATDHSEFKSLNWEE 384
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
2-180 |
6.65e-67 |
|
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: 210.57 E-value: 6.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 2 KKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEvVRTGNLRAVSK----PEQADAF 77
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKA-NVSGRLSFTTDystaIEEADVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 78 FVVVPTPFK-QNHRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIYKERPELKD-KIYIAYCPERVLPGN 155
Cdd:pfam03721 80 FIAVGTPSKkGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGvDFDVASNPEFLREGS 159
|
170 180
....*....|....*....|....*
gi 492255706 156 TLYELVHNDRVIGGVNPESTAKAIE 180
Cdd:pfam03721 160 AVYDLFNPDRVVIGVTEKCAEAALE 184
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
311-388 |
5.31e-17 |
|
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 214954 [Multi-domain] Cd Length: 99 Bit Score: 75.62 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 311 ACMGLAFKPNIDDLRESPAKYIASRIVSESrAEVLIVEPNVASHASFHLTDY----REAYQKADIVVWLVRHTPFVELPR 386
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAG-AEVVVYDPYAMEEAREYGLTYvsdlEEALKGADAVVIATEHDEFRSLDP 79
|
..
gi 492255706 387 EE 388
Cdd:smart00984 80 EE 81
|
|
| 2-Hacid_dh_6 |
cd12165 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
2-82 |
8.01e-03 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240642 [Multi-domain] Cd Length: 314 Bit Score: 37.99 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 2 KKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNpsvvetinqgkihivePELDQIVKEVVRTGNLRAVSkpEQADAFFVVV 81
Cdd:cd12165 138 KTVGILGYGHIGREIARLLKAFGMRVIGVSRS----------------PKEDEGADFVGTLSDLDEAL--EQADVVVVAL 199
|
.
gi 492255706 82 P 82
Cdd:cd12165 200 P 200
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
2-381 |
0e+00 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 576.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 2 KKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEVVRTGNLRAVSKPEQADAFFVVV 81
Cdd:PRK11064 4 ETISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGGYLRATTTPEPADAFLIAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 82 PTPFKQNHRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIYKERPEL--------KDKIYIAYCPERVLP 153
Cdd:PRK11064 84 PTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLAEARPDLtfpqqageQADINIAYCPERVLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 154 GNTLYELVHNDRVIGGVNPESTAKAIEFYSAFVQGKLHPTNARTAEMCKLTENSSRDSQIAFANELSMICDKAGINVWEL 233
Cdd:PRK11064 164 GQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINVWEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 234 IELANKHPRVNILQPGCGVGGHCIAVDPWFIVSDYPEQAQIIKRARETNDYKADWCANKVMEACQQFVEKNDR---EPVV 310
Cdd:PRK11064 244 IRLANRHPRVNILQPGPGVGGHCIAVDPWFIVAQNPQQARLIRTAREVNDGKPHWVIDQVKAAVADCLAATDKrasEVKI 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492255706 311 ACMGLAFKPNIDDLRESPAKYIASRIVSESRAEVLIVEPNV-----ASHASFHLTDYREAYQKADIVVWLVRHTPF 381
Cdd:PRK11064 324 ACFGLAFKPNIDDLRESPAMEIAELIAQWHSGETLVVEPNIhqlpkKLDGLVTLVSLDEALATADVLVMLVDHSQF 399
|
|
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
3-398 |
0e+00 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 513.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 3 KVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPElDQIVKEVVRTGNLRAVSKPE---QADAFFV 79
Cdd:COG0677 1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPG-DELLAEAVAAGRLRATTDPEalaEADVVII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 80 VVPTPFKQNHRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIYKERPELK--DKIYIAYCPERVLPGNTL 157
Cdd:COG0677 80 AVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRSGLKagEDFFLAYSPERINPGNKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 158 YELVHNDRVIGGVNPESTAKAIEFYSAFVQGKLHP-TNARTAEMCKLTENSSRDSQIAFANELSMICDKAGINVWELIEL 236
Cdd:COG0677 160 HELRNIPKVVGGITPESAERAAALYGSVVTAGVVPvSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 237 ANKHPRVNILQPGCGVGGHCIAVDPWFIVSDYPE---QAQIIKRARETNDYKADWCANKVMEACQQfVEKNDREPVVACM 313
Cdd:COG0677 240 ANTKPGFLIFYPGPGVGGHCIPVDPYYLTWKARElgyHPRLILAAREINDSMPEYVVERVVKALNE-AGKSLKGARVLVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 314 GLAFKPNIDDLRESPAKYIAsRIVSESRAEVLIVEPNV----ASHASFHLTDYREAYQKADIVVWLVRHTPFVELPREES 389
Cdd:COG0677 319 GLAYKENVDDLRESPALDII-EELREYGAEVDVHDPYVdeeeVEGEYGELVDLEEALEGADAVVLAVDHDEFDELDPEEL 397
|
410
....*....|....
gi 492255706 390 KLE-----LDFCGV 398
Cdd:COG0677 398 RLKgakvvVDTRGV 411
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
2-390 |
7.62e-135 |
|
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: 391.97 E-value: 7.62e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 2 KKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEVVRTGNLRAVSKPE----QADAF 77
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKALKAGRLRATTDYEeairDADVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 78 FVVVPTPFKQNHRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIYKERPELKDK-IYIAYCPERVLPGNT 156
Cdd:TIGR03026 81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEdFYLAYNPEFLREGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 157 LYELVHNDRVIGGVNPESTAKAIEFYSAFVQGKLHPTNARTAEMCKLTENSSRDSQIAFANELSMICDKAGINVWELIEL 236
Cdd:TIGR03026 161 VHDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 237 ANKHPR--VNILQPGCGVGGHCIAVDPWFIVSDYPE---QAQIIKRARETNDYKADWCANKVMEACQQFVEKNdrepvVA 311
Cdd:TIGR03026 241 AGTDPRigFNFLNPGPGVGGHCIPKDPLALIAKAKElgyNPELIEAAREINDSQPDYVVEKIKDLLGPLKGKT-----VL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 312 CMGLAFKPNIDDLRESPAKYIASRIVSESrAEVLIVEPNVASHASFHLTDYREAYQ---KADIVVWLVRHTPFVELPREE 388
Cdd:TIGR03026 316 ILGLAFKPNTDDVRESPALDIIELLKEKG-AKVKAYDPLVPEEEVKGLPSIDDLEEalkGADALVILTDHSEFKDLDLEK 394
|
..
gi 492255706 389 SK 390
Cdd:TIGR03026 395 IK 396
|
|
| UDPMaNacDH_Arch |
NF040825 |
UDP-N-acetyl-D-mannosamine dehydrogenase; |
3-388 |
9.75e-112 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase;
Pssm-ID: 468765 [Multi-domain] Cd Length: 418 Bit Score: 333.65 E-value: 9.75e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 3 KVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEVVRTGNLRAVSKPEQ---ADAFFV 79
Cdd:NF040825 2 KIAVIGLGYIGLPTAIMFASSGHNVIGYEIREDVVKKINSGKAHIVEPEIEERLKKVVEEGRLKATTDPEDlkgADAFII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 80 VVPTPFKQNhRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIyKERPELKDKI--YIAYCPERVLPGNTL 157
Cdd:NF040825 82 CVQTPLKED-KPDLSYLENAIRTVAEVMDRGALVIIESTVPPGTTVKMARLL-EELTGLKEGEdfYMAHAPERVMPGRIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 158 YELVHNDRVIGGVNPESTAKAIEFYSAFVQGKLHPTNARTAEMCKLTENSSRDSQIAFANELSMICDKAGINVWELIELA 237
Cdd:NF040825 160 KELVYNSRIIGGVSEKSAELAEKLYRSFVKGEIFLTDATTAEMVKLMENTFRDVNIALANEFALLAHQYGVNVFEAIELA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 238 NKHPRVNILQPGCGVGGHCIAVDPWFIVSDYPEQAQIIKRARETNDYKADWCANKVMEACQQfVEKNDREPVVACMGLAF 317
Cdd:NF040825 240 NTHPRVKIHVPGIGVGGHCLPKDPYLLLSNAKEDFGLIRLAREINEDMPLFAKDLLFEALEE-ANVPPEEAVVTVLGLAY 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492255706 318 KPNIDDLRESPA-KYIasRIVSESRAEVLIVEPNV-ASHASFhltdyREAYQKADIVVWLVRHTPFVELPREE 388
Cdd:NF040825 319 KGDTDDTRNSPAlKFV--ELIEDDVKEVRTYDPYVgGTHESL-----EDAVKGADAIVIATDHSEFKSLNWEE 384
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
2-180 |
6.65e-67 |
|
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: 210.57 E-value: 6.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 2 KKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEvVRTGNLRAVSK----PEQADAF 77
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKA-NVSGRLSFTTDystaIEEADVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 78 FVVVPTPFK-QNHRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIYKERPELKD-KIYIAYCPERVLPGN 155
Cdd:pfam03721 80 FIAVGTPSKkGGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGvDFDVASNPEFLREGS 159
|
170 180
....*....|....*....|....*
gi 492255706 156 TLYELVHNDRVIGGVNPESTAKAIE 180
Cdd:pfam03721 160 AVYDLFNPDRVVIGVTEKCAEAALE 184
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
3-373 |
2.25e-66 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 217.20 E-value: 2.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 3 KVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEVVRTGNLRAVSKPEQA----DAFF 78
Cdd:COG1004 2 KIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPIYEPGLEELVARNVAAGRLRFTTDLAEAvaeaDVVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 79 VVVPTPFKQNHRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIYKERPELKDKIYIAYCPERVLPGNTLY 158
Cdd:COG1004 82 IAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEELRGAGVDFDVVSNPEFLREGSAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 159 ELVHNDR-VIGGVNPESTAKAIEFYSAFVQG--KLHPTNARTAEMCKLTENS---SRdsqIAFANELSMICDKAGINVWE 232
Cdd:COG1004 162 DFLRPDRiVIGVDSERAAEVLRELYAPFVRNgtPIIVTDLRSAELIKYAANAflaTK---ISFINEIANLCEKVGADVEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 233 LIElANKH-PRvnI----LQPGCGVGGHC--------IAvdpwfIVSDYPEQAQIIKRARETNDYKADWCANKVMEACQQ 299
Cdd:COG1004 239 VAR-GIGLdSR--IgpkfLYAGIGYGGSCfpkdvralIA-----TARELGYDLRLLEAVEEVNERQKRRLVEKIREHLGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 300 FVE-KndrepVVACMGLAFKPNIDDLRESPAKYIASRIVSESrAEVLIVEPNVASHASFHL-------TDYREAYQKADI 371
Cdd:COG1004 311 DLKgK-----TIAVLGLAFKPNTDDMRESPALDIIEALLEAG-ARVRAYDPVAMENARRLLpddityaDDAYEALEGADA 384
|
..
gi 492255706 372 VV 373
Cdd:COG1004 385 LV 386
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
3-327 |
4.43e-34 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 131.35 E-value: 4.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 3 KVVFLGLGYIGLPTAaVAAGHGYEVVGVDVNPSVVETINQGkihiVEPELDQIVKEVVRTGNLRAVSKPE---QADAFFV 79
Cdd:PRK15182 8 KIAIIGLGYVGLPLA-VEFGKSRQVVGFDVNKKRILELKNG----VDVNLETTEEELREARYLKFTSEIEkikECNFYII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 80 VVPTPFKQNHRADITYVESATRSVIPYLREGNLFVIESTS-PVFTTERMAEVIYKERP-ELKDKIYIAYCPERVLPGNTL 157
Cdd:PRK15182 83 TVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVyPGCTEEECVPILARMSGmTFNQDFYVGYSPERINPGDKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 158 YELVHNDRVIGGVNPESTAKAIEFYSAFVQ-GKLHPTNARTAEMCKLTENSSRDSQIAFANELSMICDKAGINVWELIEL 236
Cdd:PRK15182 163 HRLTNIKKITSGSTAQIAELIDEVYQQIISaGTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEAVLRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 237 ANKHPRVNILQPGCgVGGHCIAVDPWFI------VSDYPEqaqIIKRARETNDYKADWCANKVMEAcqqFVEK--NDREP 308
Cdd:PRK15182 243 AGSKWNFLPFRPGL-VGGHCIGVDPYYLthksqgIGYYPE---IILAGRRLNDNMGNYVSEQLIKA---MIKKgiNVEGS 315
|
330
....*....|....*....
gi 492255706 309 VVACMGLAFKPNIDDLRES 327
Cdd:PRK15182 316 SVLILGFTFKENCPDIRNT 334
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
197-283 |
9.25e-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: 120.95 E-value: 9.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 197 TAEMCKLTENSSRDSQIAFANELSMICDKAGINVWELIELANKHPR--VNILQPGCGVGGHCIAVDPWFIVS---DYPEQ 271
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRigPKFLYPGPGVGGSCLPKDPRALIYlarELGVP 80
|
90
....*....|..
gi 492255706 272 AQIIKRARETND 283
Cdd:pfam00984 81 ARLLEAAREVNE 92
|
|
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
1-352 |
7.90e-32 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 125.56 E-value: 7.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 1 MKKVVFLGLGYIGLPTAAVAAGH--GYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEVvRTGNL-------RAVSKp 71
Cdd:PLN02353 1 MVKICCIGAGYVGGPTMAVIALKcpDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQC-RGKNLffstdveKHVAE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 72 eqADAFFVVVPTPFKQN-----HRADITYVESATRSVIPYLREGNLFVIESTSPVFTTERMAEVIYKERPELKDKIYIAy 146
Cdd:PLN02353 79 --ADIVFVSVNTPTKTRglgagKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKGINFQILSN- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 147 cPERVLPGNTLYELVHNDRV-IGGVNPESTAKAIE----FYSAFV-QGKLHPTNARTAEMCKLTENSSRDSQIAFANELS 220
Cdd:PLN02353 156 -PEFLAEGTAIEDLFKPDRVlIGGRETPEGQKAVQalkdVYAHWVpEERIITTNLWSAELSKLAANAFLAQRISSVNAMS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 221 MICDKAGINVWELIELANKHPRV--NILQPGCGVGGHCIAVDPWFIVSD-----YPEQAQIIKRARETNDYKADWCANKV 293
Cdd:PLN02353 235 ALCEATGADVSQVSHAVGKDSRIgpKFLNASVGFGGSCFQKDILNLVYIcecngLPEVAEYWKQVIKMNDYQKSRFVNRV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 492255706 294 MEACQQFVekndREPVVACMGLAFKPNIDDLRESPAKYIASRIVSEsRAEVLIVEPNVA 352
Cdd:PLN02353 315 VSSMFNTV----SGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGD-KAKLSIYDPQVT 368
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
3-373 |
2.47e-30 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 120.13 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 3 KVVFLGLGYIGLPTAAVAAGHgYEVVGVDVNPSVVETINQGKIHIVEPELDQIVKEvvrtGNLRAVSKPEQADAF----F 78
Cdd:PRK15057 2 KITISGTGYVGLSNGLLIAQN-HEVVALDILPSRVAMLNDRISPIVDKEIQQFLQS----DKIHFNATLDKNEAYrdadY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 79 VVVPTPFKQNHRAD---ITYVESATRSVIPyLREGNLFVIESTSPVFTTERMAEVIYKERpelkdkiyIAYCPERVLPGN 155
Cdd:PRK15057 77 VIIATPTDYDPKTNyfnTSSVESVIKDVVE-INPYAVMVIKSTVPVGFTAAMHKKYRTEN--------IIFSPEFLREGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 156 TLYELVHNDRVIGGvnpESTAKAIEFYSAFVQGKLHP------TNARTAEMCKLTENSSRDSQIAFANELSMICDKAGIN 229
Cdd:PRK15057 148 ALYDNLHPSRIVIG---ERSERAERFAALLQEGAIKQniptlfTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 230 VWELIELANKHPRV--NILQPGCGVGGHCIAVDPWFIVSDYPE-QAQIIKRARETNDYKADWCANKVMEacqqfvekndR 306
Cdd:PRK15057 225 TRQIIEGVCLDPRIgnHYNNPSFGYGGYCLPKDTKQLLANYQSvPNNLISAIVDANRTRKDFIADAILS----------R 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492255706 307 EP-VVACMGLAFKPNIDDLRESPAKYIASRIVSESrAEVLIVEPnVASHASFHLT----DYREAYQKADIVV 373
Cdd:PRK15057 295 KPqVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKG-VEVIIYEP-VMKEDSFFNSrlerDLATFKQQADVII 364
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
311-388 |
5.31e-17 |
|
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes which possesses the ability to catalyse the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 214954 [Multi-domain] Cd Length: 99 Bit Score: 75.62 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 311 ACMGLAFKPNIDDLRESPAKYIASRIVSESrAEVLIVEPNVASHASFHLTDY----REAYQKADIVVWLVRHTPFVELPR 386
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAG-AEVVVYDPYAMEEAREYGLTYvsdlEEALKGADAVVIATEHDEFRSLDP 79
|
..
gi 492255706 387 EE 388
Cdd:smart00984 80 EE 81
|
|
| UDPG_MGDP_dh_C |
pfam03720 |
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ... |
311-390 |
7.75e-12 |
|
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: 61.44 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 311 ACMGLAFKPNIDDLRESPAKYIASRIVSESrAEVLIVEPNVASHASFHLTDYR-------EAYQKADIVVWLVRHTPFVE 383
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEG-AEVKVYDPYVPEEAIEALGDGVtlvddleEALKGADAIVILTDHDEFKS 79
|
....*..
gi 492255706 384 LPREESK 390
Cdd:pfam03720 80 LDWEKLK 86
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
3-129 |
7.22e-06 |
|
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.
Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 45.54 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 3 KVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVEPeldqiVKEVVrtgnlravskpEQADAFFVVVP 82
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAAS-----PAEFV-----------AGLDVVITMVP 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 492255706 83 TPfkqnhradityveSATRSVI------PYLREGNLFVIESTSPVFTTERMAE 129
Cdd:pfam03446 65 AG-------------AAVDAVIfgegllPGLKPGDIIIDGSTSSPEDARRRAK 104
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
1-129 |
3.85e-05 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 45.11 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 1 MKKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVEtinqgkihivepeldqivkEVVRTGnLRAVSKP----EQADA 76
Cdd:COG2084 1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAE-------------------ALVAAG-ARVAASPaeaaAAADV 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 492255706 77 FFVVVPTPfkqnhrADityVESATRS---VIPYLREGNLFVIESTSPVFTTERMAE 129
Cdd:COG2084 61 VITMLPDD------AA---VEEVLLGedgLLAALRPGAVVVDMSTISPETARELAA 107
|
|
| gpsA |
PRK00094 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; |
1-146 |
7.05e-05 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
Pssm-ID: 234629 [Multi-domain] Cd Length: 325 Bit Score: 44.29 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 1 MKKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHivepelDQIVKEVVRTGNLRAVSKPEQA----DA 76
Cdd:PRK00094 1 MMKIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADREN------PRYLPGIKLPDNLRATTDLAEAladaDL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492255706 77 FFVVVPTpfkqnhradityveSATRSVI----PYLREGNLFV-----IESTspvfTTERMAEVIyKErpELKDKIYIAY 146
Cdd:PRK00094 75 ILVAVPS--------------QALREVLkqlkPLLPPDAPIVwatkgIEPG----TGKLLSEVL-EE--ELPDLAPIAV 132
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
1-110 |
6.28e-04 |
|
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 41.27 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 1 MKKVVFLGLGYIG----LptAAVAAGHGYEVVGVDVNPSVVET-INQGKIHIVEPELDQIVKEvvrtgnlravskpeqAD 75
Cdd:COG0287 1 FMRIAIIGLGLIGgslaL--ALKRAGLAHEVVGVDRSPETLERaLELGVIDRAATDLEEAVAD---------------AD 63
|
90 100 110
....*....|....*....|....*....|....*
gi 492255706 76 afFVVVPTPfkqnhradITYVESATRSVIPYLREG 110
Cdd:COG0287 64 --LVVLAVP--------VGATIEVLAELAPHLKPG 88
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
1-84 |
8.08e-04 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 41.00 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492255706 1 MKKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETInqgkihivepeldqivkevVRTGNLRAVSKPEQA-DAFFV 79
Cdd:PRK15461 1 MAAIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDAL-------------------VDKGATPAASPAQAAaGAEFV 61
|
....*
gi 492255706 80 VVPTP 84
Cdd:PRK15461 62 ITMLP 66
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
2-49 |
2.28e-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: 39.66 E-value: 2.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 492255706 2 KKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNPSVVETINQGKIHIVE 49
Cdd:COG0569 96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIV 143
|
|
| 2-Hacid_dh_6 |
cd12165 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
2-82 |
8.01e-03 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240642 [Multi-domain] Cd Length: 314 Bit Score: 37.99 E-value: 8.01e-03
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gi 492255706 2 KKVVFLGLGYIGLPTAAVAAGHGYEVVGVDVNpsvvetinqgkihivePELDQIVKEVVRTGNLRAVSkpEQADAFFVVV 81
Cdd:cd12165 138 KTVGILGYGHIGREIARLLKAFGMRVIGVSRS----------------PKEDEGADFVGTLSDLDEAL--EQADVVVVAL 199
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gi 492255706 82 P 82
Cdd:cd12165 200 P 200
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