|
Name |
Accession |
Description |
Interval |
E-value |
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
18-427 |
0e+00 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 603.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKARASG-FEATTDFSRVSECDALILCV 96
Cdd:COG0677 2 IAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGrLRATTDPEALAEADVVIIAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 97 PTPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQEG-GLVVGRDIYLVYSPEREDPGNPNFE 175
Cdd:COG0677 82 PTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRsGLKAGEDFFLAYSPERINPGNKLHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 176 TRTIPKVIGGHTPQCLEVGIALYEQAID-RVVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDIFEVVDAAA 254
Cdd:COG0677 162 LRNIPKVVGGITPESAERAAALYGSVVTaGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEAAN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 255 TKPfGFTPYYPGPGLGGHCIPIDPFYLTWKAREYGLHTRFIELSGEVNQAMPEYVLGKLMDGLNEAGRALKGSRVLVLGI 334
Cdd:COG0677 242 TKP-GFLIFYPGPGVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLVLGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 335 AYKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPVFPKMREHHfelSSEPLTaENLARFDAVVLATDHDKFDY----E 410
Cdd:COG0677 321 AYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYG---ELVDLE-EALEGADAVVLAVDHDEFDEldpeE 396
|
410
....*....|....*..
gi 15598355 411 LIKAEAKLVVDSRGKYR 427
Cdd:COG0677 397 LRLKGAKVVVDTRGVLD 413
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
18-424 |
7.11e-165 |
|
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: 469.79 E-value: 7.11e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYI-EHIPQAKIAKARASG-FEATTDFSRVS-ECDALIL 94
Cdd:TIGR03026 3 IAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIyEPGLDELLAKALKAGrLRATTDYEEAIrDADVIII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 95 CVPTPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQEGGLVVGRDIYLVYSPEREDPGNPNF 174
Cdd:TIGR03026 83 CVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYNPEFLREGNAVH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 175 ETRTIPKVIGGHTPQCLEVGIALYEQAIDRVVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDIFEVVDAAA 254
Cdd:TIGR03026 163 DLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEAAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 255 TKPF-GFTPYYPGPGLGGHCIPIDPFYLTWKAREYGLHTRFIELSGEVNQAMPEYVLGKLMDGLneagRALKGSRVLVLG 333
Cdd:TIGR03026 243 TDPRiGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLL----GPLKGKTVLILG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 334 IAYKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPVfpkmrEHHFELSSEPLTAENLARFDAVVLATDHDKF---DYE 410
Cdd:TIGR03026 319 LAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPE-----EEVKGLPSIDDLEEALKGADALVILTDHSEFkdlDLE 393
|
410
....*....|....*.
gi 15598355 411 LIKA--EAKLVVDSRG 424
Cdd:TIGR03026 394 KIKDlmKGKVVVDTRN 409
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
16-193 |
1.52e-71 |
|
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: 223.28 E-value: 1.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 16 ALIGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKARASG-FEATTDFSR-VSECDALI 93
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGrLSFTTDYSTaIEEADVIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 94 LCVPTPLNK-YREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQEGGLVVGRDIYLVYSPEREDPGNP 172
Cdd:pfam03721 81 IAVGTPSKKgGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFDVASNPEFLREGSA 160
|
170 180
....*....|....*....|.
gi 15598355 173 NFETRTIPKVIGGHTPQCLEV 193
Cdd:pfam03721 161 VYDLFNPDRVVIGVTEKCAEA 181
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
18-407 |
7.59e-71 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 229.96 E-value: 7.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLMLRYNAiGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKARASGFeaTTDFSRVSECDALILCVP 97
Cdd:PRK15182 9 IAIIGLGYVGLPLAVEFGK-SRQVVGFDVNKKRILELKNGVDVNLETTEEELREARYLKF--TSEIEKIKECNFYIITVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 98 TPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQE-GGLVVGRDIYLVYSPEREDPGNPNFET 176
Cdd:PRK15182 86 TPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARmSGMTFNQDFYVGYSPERINPGDKKHRL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 177 RTIPKVIGGHTPQCLEVGIALYEQAIDR-VVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDIFEVVDAAAT 255
Cdd:PRK15182 166 TNIKKITSGSTAQIAELIDEVYQQIISAgTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEAVLRAAGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 256 KpFGFTPYYPGPgLGGHCIPIDPFYLTWKAREYGLHTRFIELSGEVNQAMPEYVLGKLMDGLNEAGRALKGSRVLVLGIA 335
Cdd:PRK15182 246 K-WNFLPFRPGL-VGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNMGNYVSEQLIKAMIKKGINVEGSSVLILGFT 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598355 336 YKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPVFPKMREHHFelssEPLTAENLARFDAVVLATDHDKF 407
Cdd:PRK15182 324 FKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEVRREYGI----IPVSEVKSSHYDAIIVAVGHQQF 391
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
330-426 |
4.90e-24 |
|
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: 95.65 E-value: 4.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 330 LVLGIAYKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPvfPKMREHHFELSSEPLTAenLARFDAVVLATDHDKF-- 407
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAM--EEAREYGLTYVSDLEEA--LKGADAVVIATEHDEFrs 76
|
90 100
....*....|....*....|..
gi 15598355 408 -DYELIKAEAK--LVVDSRGKY 426
Cdd:smart00984 77 lDPEELKDLMKkpVVVDGRNIL 98
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
18-427 |
0e+00 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 603.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKARASG-FEATTDFSRVSECDALILCV 96
Cdd:COG0677 2 IAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDPILEPGDELLAEAVAAGrLRATTDPEALAEADVVIIAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 97 PTPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQEG-GLVVGRDIYLVYSPEREDPGNPNFE 175
Cdd:COG0677 82 PTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPILEKRsGLKAGEDFFLAYSPERINPGNKLHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 176 TRTIPKVIGGHTPQCLEVGIALYEQAID-RVVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDIFEVVDAAA 254
Cdd:COG0677 162 LRNIPKVVGGITPESAERAAALYGSVVTaGVVPVSSIKVAEAAKLIENTYRDVNIALANELALICDRLGIDVWEVIEAAN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 255 TKPfGFTPYYPGPGLGGHCIPIDPFYLTWKAREYGLHTRFIELSGEVNQAMPEYVLGKLMDGLNEAGRALKGSRVLVLGI 334
Cdd:COG0677 242 TKP-GFLIFYPGPGVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKALNEAGKSLKGARVLVLGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 335 AYKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPVFPKMREHHfelSSEPLTaENLARFDAVVLATDHDKFDY----E 410
Cdd:COG0677 321 AYKENVDDLRESPALDIIEELREYGAEVDVHDPYVDEEEVEGEYG---ELVDLE-EALEGADAVVLAVDHDEFDEldpeE 396
|
410
....*....|....*..
gi 15598355 411 LIKAEAKLVVDSRGKYR 427
Cdd:COG0677 397 LRLKGAKVVVDTRGVLD 413
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
18-424 |
7.11e-165 |
|
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: 469.79 E-value: 7.11e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYI-EHIPQAKIAKARASG-FEATTDFSRVS-ECDALIL 94
Cdd:TIGR03026 3 IAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIyEPGLDELLAKALKAGrLRATTDYEEAIrDADVIII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 95 CVPTPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQEGGLVVGRDIYLVYSPEREDPGNPNF 174
Cdd:TIGR03026 83 CVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYNPEFLREGNAVH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 175 ETRTIPKVIGGHTPQCLEVGIALYEQAIDRVVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDIFEVVDAAA 254
Cdd:TIGR03026 163 DLLHPDRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGIDVYEVIEAAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 255 TKPF-GFTPYYPGPGLGGHCIPIDPFYLTWKAREYGLHTRFIELSGEVNQAMPEYVLGKLMDGLneagRALKGSRVLVLG 333
Cdd:TIGR03026 243 TDPRiGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIKDLL----GPLKGKTVLILG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 334 IAYKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPVfpkmrEHHFELSSEPLTAENLARFDAVVLATDHDKF---DYE 410
Cdd:TIGR03026 319 LAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLVPE-----EEVKGLPSIDDLEEALKGADALVILTDHSEFkdlDLE 393
|
410
....*....|....*.
gi 15598355 411 LIKA--EAKLVVDSRG 424
Cdd:TIGR03026 394 KIKDlmKGKVVVDTRN 409
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
16-193 |
1.52e-71 |
|
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: 223.28 E-value: 1.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 16 ALIGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKARASG-FEATTDFSR-VSECDALI 93
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIPIYEPGLDELVKANVSGrLSFTTDYSTaIEEADVIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 94 LCVPTPLNK-YREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQEGGLVVGRDIYLVYSPEREDPGNP 172
Cdd:pfam03721 81 IAVGTPSKKgGGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFDVASNPEFLREGSA 160
|
170 180
....*....|....*....|.
gi 15598355 173 NFETRTIPKVIGGHTPQCLEV 193
Cdd:pfam03721 161 VYDLFNPDRVVIGVTEKCAEA 181
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
18-407 |
7.59e-71 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 229.96 E-value: 7.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLMLRYNAiGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKARASGFeaTTDFSRVSECDALILCVP 97
Cdd:PRK15182 9 IAIIGLGYVGLPLAVEFGK-SRQVVGFDVNKKRILELKNGVDVNLETTEEELREARYLKF--TSEIEKIKECNFYIITVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 98 TPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEEELLPRVQE-GGLVVGRDIYLVYSPEREDPGNPNFET 176
Cdd:PRK15182 86 TPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEECVPILARmSGMTFNQDFYVGYSPERINPGDKKHRL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 177 RTIPKVIGGHTPQCLEVGIALYEQAIDR-VVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDIFEVVDAAAT 255
Cdd:PRK15182 166 TNIKKITSGSTAQIAELIDEVYQQIISAgTYKAESIKVAEAAKVIENTQRDLNIALVNELAIIFNRLNIDTEAVLRAAGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 256 KpFGFTPYYPGPgLGGHCIPIDPFYLTWKAREYGLHTRFIELSGEVNQAMPEYVLGKLMDGLNEAGRALKGSRVLVLGIA 335
Cdd:PRK15182 246 K-WNFLPFRPGL-VGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNMGNYVSEQLIKAMIKKGINVEGSSVLILGFT 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598355 336 YKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPVFPKMREHHFelssEPLTAENLARFDAVVLATDHDKF 407
Cdd:PRK15182 324 FKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVDAEEVRREYGI----IPVSEVKSSHYDAIIVAVGHQQF 391
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
18-421 |
3.59e-70 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 227.56 E-value: 3.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKARASG--FEATTdfsRVSECDALILC 95
Cdd:PRK11064 6 ISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEIHIVEPDLDMVVKTAVEGgyLRATT---TPEPADAFLIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 96 VPTPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTEE------ELLPRV---QEGGLVVgrDIYLVYSPER 166
Cdd:PRK11064 83 VPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQmaewlaEARPDLtfpQQAGEQA--DINIAYCPER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 167 EDPGNPNFETRTIPKVIGGHTPQCLEVGIALYEQAIDRVVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDI 246
Cdd:PRK11064 161 VLPGQVMVELIKNDRVIGGMTPVCSARASELYKIFLEGECVVTNSRTAEMCKLTENSFRDVNIAFANELSLICADQGINV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 247 FEVVDAAATKPfGFTPYYPGPGLGGHCIPIDPFYLTWKAREyglHTRFIELSGEVNQAMPEYVLGK----LMDGLNEAGR 322
Cdd:PRK11064 241 WELIRLANRHP-RVNILQPGPGVGGHCIAVDPWFIVAQNPQ---QARLIRTAREVNDGKPHWVIDQvkaaVADCLAATDK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 323 ALKGSRVLVLGIAYKKNVDDMRESPSVEIMELI-EAKGGMVAYSDPHVPVFPKMREHHFELSSeplTAENLARFDAVVLA 401
Cdd:PRK11064 317 RASEVKIACFGLAFKPNIDDLRESPAMEIAELIaQWHSGETLVVEPNIHQLPKKLDGLVTLVS---LDEALATADVLVML 393
|
410 420
....*....|....*....|...
gi 15598355 402 TDHDKF---DYELIKaeAKLVVD 421
Cdd:PRK11064 394 VDHSQFkaiNGDNVH--QQWVVD 414
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
18-423 |
5.30e-56 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 191.00 E-value: 5.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCYIeHIP--QAKIAKARASG-FEATTDFSR-VSECDALI 93
Cdd:COG1004 3 IAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIPI-YEPglEELVARNVAAGrLRFTTDLAEaVAEADVVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 94 LCVPTPLNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTeEELLPRVQEGGLVVGRDIYLVYSPE--REdpG- 170
Cdd:COG1004 82 IAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTA-DRVRAIIAEELRGAGVDFDVVSNPEflRE--Gs 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 171 ------NPNfetRTipkVIGGHTPQCLEVGIALYEQAIDRVVPVSST--KAAEMTKLlenihrAVN------IGLVNEMK 236
Cdd:COG1004 159 avedflRPD---RI---VIGVDSERAAEVLRELYAPFVRNGTPIIVTdlRSAELIKY------AANaflatkISFINEIA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 237 IVADRMGIDIFEVVDAAATKP-----FgftpYYPGPGLGGHCIPIDPFYLTWKAREYGLHTRFIELSGEVNQAMPEYVLG 311
Cdd:COG1004 227 NLCEKVGADVEEVARGIGLDSrigpkF----LYAGIGYGGSCFPKDVRALIATARELGYDLRLLEAVEEVNERQKRRLVE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 312 KLMDglnEAGRALKGSRVLVLGIAYKKNVDDMRESPSVEIMELIEAKGGMV-AYsDPHV-PVFPKMREHHFELSSEPLTA 389
Cdd:COG1004 303 KIRE---HLGGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVrAY-DPVAmENARRLLPDDITYADDAYEA 378
|
410 420 430
....*....|....*....|....*....|....*....
gi 15598355 390 enLARFDAVVLATDHDKF---DYELIKA--EAKLVVDSR 423
Cdd:COG1004 379 --LEGADALVILTEWPEFralDFARLKAlmKGPVIFDGR 415
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
213-303 |
7.50e-40 |
|
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: 137.89 E-value: 7.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 213 AAEMTKLLENIHRAVNIGLVNEMKIVADRMGIDIFEVVDAAATKPF-GFTPYYPGPGLGGHCIPIDPFYLTWKAREYGLH 291
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRiGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
|
90
....*....|..
gi 15598355 292 TRFIELSGEVNQ 303
Cdd:pfam00984 81 ARLLEAAREVNE 92
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
330-426 |
4.90e-24 |
|
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: 95.65 E-value: 4.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 330 LVLGIAYKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPvfPKMREHHFELSSEPLTAenLARFDAVVLATDHDKF-- 407
Cdd:smart00984 1 AVLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAM--EEAREYGLTYVSDLEEA--LKGADAVVIATEHDEFrs 76
|
90 100
....*....|....*....|..
gi 15598355 408 -DYELIKAEAK--LVVDSRGKY 426
Cdd:smart00984 77 lDPEELKDLMKkpVVVDGRNIL 98
|
|
| UDPG_MGDP_dh_C |
pfam03720 |
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ... |
330-424 |
4.92e-24 |
|
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: 95.72 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 330 LVLGIAYKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHVPVFPKMREH-HFELSSEPLTAenLARFDAVVLATDHDKF- 407
Cdd:pfam03720 1 AVLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYVPEEAIEALGdGVTLVDDLEEA--LKGADAIVILTDHDEFk 78
|
90 100
....*....|....*....|.
gi 15598355 408 --DYELIK--AEAKLVVDSRG 424
Cdd:pfam03720 79 slDWEKLKklMKPPVVFDGRN 99
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
18-367 |
2.86e-13 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 70.82 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLP--LMLRYNaigFDVLGIDIDDVKVDKLNAgqcYIEHIPQAKIAKARASG---FEATTD-FSRVSECDA 91
Cdd:PRK15057 3 ITISGTGYVGLSngLLIAQN---HEVVALDILPSRVAMLND---RISPIVDKEIQQFLQSDkihFNATLDkNEAYRDADY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 92 LILCVPT----PLNKYREPDMSFVINTTDALKPYlrvgQVVSLESTTYPGTTEEELLPRVQEGglvvgrdiyLVYSPERE 167
Cdd:PRK15057 77 VIIATPTdydpKTNYFNTSSVESVIKDVVEINPY----AVMVIKSTVPVGFTAAMHKKYRTEN---------IIFSPEFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 168 DPGNPNFETRTIPK-VIGGHTPQCLEVGIALYEQAIDRVVPV--SSTKAAEMTKLLENIHRAVNIGLVNEMKIVADRMGI 244
Cdd:PRK15057 144 REGKALYDNLHPSRiVIGERSERAERFAALLQEGAIKQNIPTlfTDSTEAEAIKLFANTYLAMRVAYFNELDSYAESLGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 245 DIFEVVDAAATKP-FGFTPYYPGPGLGGHCIPIDPFYLTwkAREYGLHTRFIELSGEVNQAMPEYVLgklmdglnEAGRA 323
Cdd:PRK15057 224 NTRQIIEGVCLDPrIGNHYNNPSFGYGGYCLPKDTKQLL--ANYQSVPNNLISAIVDANRTRKDFIA--------DAILS 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15598355 324 LKGSRVLVLGIAYKKNVDDMRESPSVEIMELIEAKGGMVAYSDP 367
Cdd:PRK15057 294 RKPQVVGIYRLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEP 337
|
|
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
18-369 |
9.36e-07 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 50.83 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLM--LRYNAIGFDVLGIDIDDVKVDKLNAGQCYIEHIPQAKIAKA-RASGFEATTDFSR-VSECDALI 93
Cdd:PLN02353 4 ICCIGAGYVGGPTMavIALKCPDIEVVVVDISVPRIDAWNSDQLPIYEPGLDEVVKQcRGKNLFFSTDVEKhVAEADIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 94 LCVPTP-----LNKYREPDMSFVINTTDALKPYLRVGQVVSLESTTYPGTTE--EELLPRVQEGglvVGRDIYlvysper 166
Cdd:PLN02353 84 VSVNTPtktrgLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEaiEKILTHNSKG---INFQIL------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 167 edpGNPNF--ETRTIPK-------VIGG-HTPQCLEVGIAL---YEQAI--DRVVpVSSTKAAEMTKLLENIHRAVNIGL 231
Cdd:PLN02353 154 ---SNPEFlaEGTAIEDlfkpdrvLIGGrETPEGQKAVQALkdvYAHWVpeERII-TTNLWSAELSKLAANAFLAQRISS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 232 VNEMKIVADRMGIDIFEVVDAAATKP-FGFTPYYPGPGLGGHCIPIDPFYLTWKAREYGLH-----------------TR 293
Cdd:PLN02353 230 VNAMSALCEATGADVSQVSHAVGKDSrIGPKFLNASVGFGGSCFQKDILNLVYICECNGLPevaeywkqvikmndyqkSR 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598355 294 FIElsgEVNQAMPEYVLGKlmdglneagralkgsRVLVLGIAYKKNVDDMRESPSVEIMELIEAKGGMVAYSDPHV 369
Cdd:PLN02353 310 FVN---RVVSSMFNTVSGK---------------KIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPQV 367
|
|
| PRK07417 |
PRK07417 |
prephenate/arogenate dehydrogenase; |
18-128 |
8.70e-06 |
|
prephenate/arogenate dehydrogenase;
Pssm-ID: 180970 [Multi-domain] Cd Length: 279 Bit Score: 47.19 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLMLRYNAIGFDVLGIdiddvkvdklnagqcyiEHIPQ-AKIAKARASGFEATTDFSRVSECDALILCV 96
Cdd:PRK07417 3 IGIVGLGLIGGSLGLDLRSLGHTVYGV-----------------SRREStCERAIERGLVDEASTDLSLLKDCDLVILAL 65
|
90 100 110
....*....|....*....|....*....|..
gi 15598355 97 PTPLnkyrepdmsfVINTTDALKPYLRVGQVV 128
Cdd:PRK07417 66 PIGL----------LLPPSEQLIPALPPEAIV 87
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
18-141 |
1.41e-04 |
|
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: 42.07 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLnagqcyiehipqakiAKARASGFEATTDFsrVSECDALILCVP 97
Cdd:pfam03446 2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEEL---------------VAAGAIAAASPAEF--VAGLDVVITMVP 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15598355 98 TPlnkyrePDMSFVInTTDALKPYLRVGQVVSLESTTYPGTTEE 141
Cdd:pfam03446 65 AG------AAVDAVI-FGEGLLPGLKPGDIIIDGSTSSPEDARR 101
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
18-129 |
2.16e-03 |
|
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: 39.72 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598355 18 IGIVGLGYVG--LPLMLRYNAIGFDVLGIDIDdvkvdklnagqcyiehipQAKIAKARASGF--EATTDFSR-VSECDAL 92
Cdd:COG0287 4 IAIIGLGLIGgsLALALKRAGLAHEVVGVDRS------------------PETLERALELGVidRAATDLEEaVADADLV 65
|
90 100 110
....*....|....*....|....*....|....*..
gi 15598355 93 ILCVPtplnkyrepdMSFVINTTDALKPYLRVGQVVS 129
Cdd:COG0287 66 VLAVP----------VGATIEVLAELAPHLKPGAIVT 92
|
|
| |
