|
Name |
Accession |
Description |
Interval |
E-value |
| WecC |
COG0677 |
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
20-446 |
1.13e-160 |
|
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 460.30 E-value: 1.13e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKV-VYEYTDILEDVVLKSKKLHVTIEPkEALDNAEIIFV 98
Cdd:COG0677 1 KIAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELNAGEDpILEPGDELLAEAVAAGRLRATTDP-EALAEADVVII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 99 CVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTI-ESLCNLKFGIDLGLAYCPERYNPTpmk 177
Cdd:COG0677 80 AVPTPLDEDKEPDLSYLESASETIAPHLKPGDLVVLESTVYPGTTEEVCVPIlEKRSGLKAGEDFFLAYSPERINPG--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 178 kytkDVDHTISakgesftvdRISRVVGGIDEKSTKITKTIYSQFVKTDVLELSSIETAEATKLLENIFRDVNIALVNELA 257
Cdd:COG0677 157 ----NKLHELR---------NIPKVVGGITPESAERAAALYGSVVTAGVVPVSSIKVAEAAKLIENTYRDVNIALANELA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 258 KIYPKFGLNIYEIINAATSKPFaFMPHYPGAGVGGECIPVDTWYLISQAEKLGMDTKILNSARQINDSMPTHMITLLENE 337
Cdd:COG0677 224 LICDRLGIDVWEVIEAANTKPG-FLIFYPGPGVGGHCIPVDPYYLTWKARELGYHPRLILAAREINDSMPEYVVERVVKA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 338 LHKHGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVY---EKVDSNVQLTPLSNIFNGSDAILF 414
Cdd:COG0677 303 LNEAGKSLKGARVLVLGLAYKENVDDLRESPALDIIEELREYGAEVDVHDPYVdeeEVEGEYGELVDLEEALEGADAVVL 382
|
410 420 430
....*....|....*....|....*....|..
gi 663530329 415 VTDHDIFTTLDFSKIKdEMKTPLIIDGRNFFN 446
Cdd:COG0677 383 AVDHDEFDELDPEELR-LKGAKVVVDTRGVLD 413
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
20-443 |
4.03e-132 |
|
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: 387.35 E-value: 4.03e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINsAKVVYEYTDILEDVV---LKSKKLHVTIEPKEALDNAEII 96
Cdd:TIGR03026 2 KIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLN-KGKSPIYEPGLDELLakaLKAGRLRATTDYEEAIRDADVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 97 FVCVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIESLCNLKFGIDLGLAYCPERYNPTPM 176
Cdd:TIGR03026 81 IICVPTPLKEDGSPDLSYVESAAETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYNPEFLREGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 177 KkytkdvdhtisakgesFTVDRISRVVGGIDEKSTKITKTIYSQFVKTDVLeLSSIETAEATKLLENIFRDVNIALVNEL 256
Cdd:TIGR03026 161 V----------------HDLLHPDRIVGGETEEAGEAVAELYSPIIDGPVL-VTSIETAEMIKLAENTFRAVKIAFANEL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 257 AKIYPKFGLNIYEIINAATSKPF-AFMPHYPGAGVGGECIPVDTWYLISQAEKLGMDTKILNSARQINDSMPTHMITLLE 335
Cdd:TIGR03026 224 ARICEALGIDVYEVIEAAGTDPRiGFNFLNPGPGVGGHCIPKDPLALIAKAKELGYNPELIEAAREINDSQPDYVVEKIK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 336 NELhkhgKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPV--YEKVDSNVQLTPLSNIFNGSDAIL 413
Cdd:TIGR03026 304 DLL----GPLKGKTVLILGLAFKPNTDDVRESPALDIIELLKEKGAKVKAYDPLvpEEEVKGLPSIDDLEEALKGADALV 379
|
410 420 430
....*....|....*....|....*....|
gi 663530329 414 FVTDHDIFTTLDFSKIKDEMKTPLIIDGRN 443
Cdd:TIGR03026 380 ILTDHSEFKDLDLEKIKDLMKGKVVVDTRN 409
|
|
| Ugd |
COG1004 |
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
20-463 |
1.57e-84 |
|
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440628 [Multi-domain] Cd Length: 436 Bit Score: 266.50 E-value: 1.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKV-VYEYTdiLEDVV---LKSKKLHVTIEPKEALDNAEI 95
Cdd:COG1004 2 KIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEALNAGEIpIYEPG--LEELVarnVAAGRLRFTTDLAEAVAEADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 96 IFVCVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIESLcNLKFGIDLGLAYCPE--Rynp 173
Cdd:COG1004 80 VFIAVGTPSDEDGSADLSYVLAAARSIGEALKGYKVVVTKSTVPVGTADRVRAIIAEE-LRGAGVDFDVVSNPEflR--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 174 tpmkkytkdvdhtisakgESFTV------DRIsrVVGGIDEKSTKITKTIYSQFVKTDV-LELSSIETAEATKLLENIFR 246
Cdd:COG1004 156 ------------------EGSAVedflrpDRI--VIGVDSERAAEVLRELYAPFVRNGTpIIVTDLRSAELIKYAANAFL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 247 DVNIALVNELAKIYPKFGLNIYEIINAATSKP---FAFMphYPGAGVGGECIPVDTWYLISQAEKLGMDTKILNSARQIN 323
Cdd:COG1004 216 ATKISFINEIANLCEKVGADVEEVARGIGLDSrigPKFL--YAGIGYGGSCFPKDVRALIATARELGYDLRLLEAVEEVN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 324 DSMPTHMITLLENELhkhGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPV-----YEKVDSNVQ 398
Cdd:COG1004 294 ERQKRRLVEKIREHL---GGDLKGKTIAVLGLAFKPNTDDMRESPALDIIEALLEAGARVRAYDPVamenaRRLLPDDIT 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663530329 399 L--TPLSNIfNGSDAILFVTDHDIFTTLDFSKIKDEMKTPLIIDGRNFFNAEKLISLGFYYRAIGKP 463
Cdd:COG1004 371 YadDAYEAL-EGADALVILTEWPEFRALDFARLKALMKGPVIFDGRNLLDPEELRAAGFTYYGIGRP 436
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
20-440 |
1.27e-63 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 211.38 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVvyeytDILE---DVVLKSK----KLHVTIEPKEAldN 92
Cdd:PRK11064 5 TISVIGLGYIGLPTAAAFASRQKQVIGVDINQHAVDTINRGEI-----HIVEpdlDMVVKTAveggYLRATTTPEPA--D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 93 AEIIfvCVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTI-ESLCNLKF------GIDLGLA 165
Cdd:PRK11064 78 AFLI--AVPTPFKGDHEPDLTYVEAAAKSIAPVLKKGDLVILESTSPVGATEQMAEWLaEARPDLTFpqqageQADINIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 166 YCPERYNPtpmkkytkdvDHTISakgESFTVDrisRVVGGIDEKSTKITKTIYSQFVKTDVLELSSiETAEATKLLENIF 245
Cdd:PRK11064 156 YCPERVLP----------GQVMV---ELIKND---RVIGGMTPVCSARASELYKIFLEGECVVTNS-RTAEMCKLTENSF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 246 RDVNIALVNELAKIYPKFGLNIYEIINAATSKPFAFMPHyPGAGVGGECIPVDTWYLISQAEKLgmdTKILNSARQINDS 325
Cdd:PRK11064 219 RDVNIAFANELSLICADQGINVWELIRLANRHPRVNILQ-PGPGVGGHCIAVDPWFIVAQNPQQ---ARLIRTAREVNDG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 326 MPTHMI----TLLENELHKHGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKV-NFLVCDP----VYEKVDSN 396
Cdd:PRK11064 295 KPHWVIdqvkAAVADCLAATDKRASEVKIACFGLAFKPNIDDLRESPAMEIAELIAQWHSgETLVVEPnihqLPKKLDGL 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 663530329 397 VQLTPLSNIFNGSDAILFVTDHDIFTTLDfskiKDEMKTPLIID 440
Cdd:PRK11064 375 VTLVSLDEALATADVLVMLVDHSQFKAIN----GDNVHQQWVVD 414
|
|
| PRK15182 |
PRK15182 |
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB; |
18-430 |
8.13e-56 |
|
Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB;
Pssm-ID: 185104 [Multi-domain] Cd Length: 425 Bit Score: 191.44 E-value: 8.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 18 DVRVCVIGVGTIGLPLATFLAKvGFQVTGLDIDQKRIDEI-NSAKVVYEYTdilEDVVLKSKKLHVTIEpKEALDNAEII 96
Cdd:PRK15182 6 EVKIAIIGLGYVGLPLAVEFGK-SRQVVGFDVNKKRILELkNGVDVNLETT---EEELREARYLKFTSE-IEKIKECNFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 97 FVCVPTPLNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTRE-ISKTIESLCNLKFGIDLGLAYCPERYNPtp 175
Cdd:PRK15182 81 IITVPTPINTYKQPDLTPLIKASETVGTVLNRGDIVVYESTVYPGCTEEeCVPILARMSGMTFNQDFYVGYSPERINP-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 176 mkkytKDVDHTISakgesftvdRISRVVGGIDEKSTKITKTIYSQFVKTDVLELSSIETAEATKLLENIFRDVNIALVNE 255
Cdd:PRK15182 159 -----GDKKHRLT---------NIKKITSGSTAQIAELIDEVYQQIISAGTYKAESIKVAEAAKVIENTQRDLNIALVNE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 256 LAKIYPKFGLNIYEIINAATSKpFAFMPHYPGAgVGGECIPVDTWYLISQAEKLGMDTKILNSARQINDSMPTHMITLLE 335
Cdd:PRK15182 225 LAIIFNRLNIDTEAVLRAAGSK-WNFLPFRPGL-VGGHCIGVDPYYLTHKSQGIGYYPEIILAGRRLNDNMGNYVSEQLI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 336 NELHKHGKELSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVY--EKVDSNVQLTPLSNIFNGS-DAI 412
Cdd:PRK15182 303 KAMIKKGINVEGSSVLILGFTFKENCPDIRNTRIIDVVKELGKYSCKVDIFDPWVdaEEVRREYGIIPVSEVKSSHyDAI 382
|
410
....*....|....*...
gi 663530329 413 LFVTDHDIFTTLDFSKIK 430
Cdd:PRK15182 383 IVAVGHQQFKQMGSEDIR 400
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
20-212 |
6.20e-37 |
|
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: 133.91 E-value: 6.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKV-VYEYTdiLEDVVLK--SKKLHVTIEPKEALDNAEII 96
Cdd:pfam03721 2 KISVIGLGYVGLPTAACLAEIGHDVIGVDIDEEKVDKLNSGQIpIYEPG--LDELVKAnvSGRLSFTTDYSTAIEEADVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 97 FVCVPTPLNIK-KEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIESLCNLKFGIDLGLAYCPERYNP-T 174
Cdd:pfam03721 80 FIAVGTPSKKGgGAADLKYVESAARSIAPHLKKGKVVVVKSTVPVGTTENLVKPIIEEGGKKVGVDFDVASNPEFLREgS 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 663530329 175 PMKkytkdvdhtisakgESFTVDRIsrvVGGIDEKSTK 212
Cdd:pfam03721 160 AVY--------------DLFNPDRV---VIGVTEKCAE 180
|
|
| UDPG_MGDP_dh |
pfam00984 |
UDP-glucose/GDP-mannose dehydrogenase family, central domain; The UDP-glucose/GDP-mannose ... |
234-324 |
7.42e-36 |
|
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: 127.49 E-value: 7.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 234 TAEATKLLENIFRDVNIALVNELAKIYPKFGLNIYEIINAATSKPF-AFMPHYPGAGVGGECIPVDTWYLISQAEKLGMD 312
Cdd:pfam00984 1 SAELIKLAENAFLAVKISFINELANLCEALGADVWEVIEAAGTDPRiGPKFLYPGPGVGGSCLPKDPRALIYLARELGVP 80
|
90
....*....|..
gi 663530329 313 TKILNSARQIND 324
Cdd:pfam00984 81 ARLLEAAREVNE 92
|
|
| PLN02353 |
PLN02353 |
probable UDP-glucose 6-dehydrogenase |
18-463 |
1.87e-27 |
|
probable UDP-glucose 6-dehydrogenase
Pssm-ID: 177986 [Multi-domain] Cd Length: 473 Bit Score: 114.39 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 18 DVRVCVIGVGTIGLPLATFLAKV--GFQVTGLDIDQKRIDEINSAKV-VYEYTdiLEDVV--LKSKKLHVTIEPKEALDN 92
Cdd:PLN02353 1 MVKICCIGAGYVGGPTMAVIALKcpDIEVVVVDISVPRIDAWNSDQLpIYEPG--LDEVVkqCRGKNLFFSTDVEKHVAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 93 AEIIFVCVPTP-----LNIKKEMDNSNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIESLCN-LKFGIdlgLAy 166
Cdd:PLN02353 79 ADIVFVSVNTPtktrgLGAGKAADLTYWESAARMIADVSKSDKIVVEKSTVPVKTAEAIEKILTHNSKgINFQI---LS- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 167 cperyNPTPMKKYTkdvdhtisAKGESFTVDRIsrVVGGID----EKSTKITKTIYSQFVKTDVLELSSIETAEATKLLE 242
Cdd:PLN02353 155 -----NPEFLAEGT--------AIEDLFKPDRV--LIGGREtpegQKAVQALKDVYAHWVPEERIITTNLWSAELSKLAA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 243 NIFRDVNIALVNELAKIYPKFGLNIYEIINAaTSKPFAFMPHYPGAGVG--GECIPVDTWYLISQAEKLGMDtKILNSAR 320
Cdd:PLN02353 220 NAFLAQRISSVNAMSALCEATGADVSQVSHA-VGKDSRIGPKFLNASVGfgGSCFQKDILNLVYICECNGLP-EVAEYWK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 321 Q---INDSMPTH----MITLLENELhkhgkelSSAKISILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDP-VYEK 392
Cdd:PLN02353 298 QvikMNDYQKSRfvnrVVSSMFNTV-------SGKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKAKLSIYDPqVTEE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 393 ------------VDSNVQLTPLSNIF--------------NGSDAILFVTDHDIFTTLDFSKIKDEMKTP-LIIDGRNFF 445
Cdd:PLN02353 371 qiqrdlsmnkfdWDHPRHLQPMSPTAvkqvsvvwdayeatKGAHGICILTEWDEFKTLDYQKIYDNMQKPaFVFDGRNVL 450
|
490
....*....|....*...
gi 663530329 446 NAEKLISLGFYYRAIGKP 463
Cdd:PLN02353 451 DHEKLREIGFIVYSIGKP 468
|
|
| UDPG_MGDP_dh_C |
smart00984 |
UDP binding domain; The UDP-glucose/GDP-mannose dehydrogenases are a small group of enzymes ... |
352-446 |
4.45e-25 |
|
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: 98.73 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 352 ILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVYEKVDSNVQLTPLSNI---FNGSDAILFVTDHDIFTTLDFSK 428
Cdd:smart00984 2 VLGLAFKPNTDDLRESPALDIIEELLEAGAEVVVYDPYAMEEAREYGLTYVSDLeeaLKGADAVVIATEHDEFRSLDPEE 81
|
90
....*....|....*...
gi 663530329 429 IKDEMKTPLIIDGRNFFN 446
Cdd:smart00984 82 LKDLMKKPVVVDGRNILD 99
|
|
| UDPG_MGDP_dh_C |
pfam03720 |
UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain; The UDP-glucose/GDP-mannose ... |
352-447 |
1.57e-22 |
|
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: 91.87 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 352 ILGLCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPV---YEKVDSNVQLTPLSNI---FNGSDAILFVTDHDIFTTLD 425
Cdd:pfam03720 2 VLGLAFKPNTDDLRESPALDIIELLLEEGAEVKVYDPYvpeEAIEALGDGVTLVDDLeeaLKGADAIVILTDHDEFKSLD 81
|
90 100
....*....|....*....|..
gi 663530329 426 FSKIKDEMKTPLIIDGRNFFNA 447
Cdd:pfam03720 82 WEKLKKLMKPPVVFDGRNVLDP 103
|
|
| PRK15057 |
PRK15057 |
UDP-glucose 6-dehydrogenase; Provisional |
19-392 |
1.86e-15 |
|
UDP-glucose 6-dehydrogenase; Provisional
Pssm-ID: 185017 [Multi-domain] Cd Length: 388 Bit Score: 77.76 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 19 VRVCVIGVGTIGLPLATFLAKvGFQVTGLDIDQKRIDEINSAkvVYEYTDILEDVVLKSKKLH--VTIEPKEALDNAEII 96
Cdd:PRK15057 1 MKITISGTGYVGLSNGLLIAQ-NHEVVALDILPSRVAMLNDR--ISPIVDKEIQQFLQSDKIHfnATLDKNEAYRDADYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 97 FVCVPTPLNIKKEMDNSN-----LLDVANrISPYltkgMILIFESSVAIGSTREISKtieslcnlKFGIDlGLAYCPERY 171
Cdd:PRK15057 78 IIATPTDYDPKTNYFNTSsvesvIKDVVE-INPY----AVMVIKSTVPVGFTAAMHK--------KYRTE-NIIFSPEFL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 172 NPTpmkkytkdvdhtiSAKGESFTVDRIsrVVGGIDEKSTKITKTIYSQFVKTDVLELSSIET-AEATKLLENIFRDVNI 250
Cdd:PRK15057 144 REG-------------KALYDNLHPSRI--VIGERSERAERFAALLQEGAIKQNIPTLFTDSTeAEAIKLFANTYLAMRV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 251 ALVNELAKIYPKFGLNIYEIINAATSKPfAFMPHY--PGAGVGGECIPVDTWYLISQAEklgmdtkilnsarqindSMPT 328
Cdd:PRK15057 209 AYFNELDSYAESLGLNTRQIIEGVCLDP-RIGNHYnnPSFGYGGYCLPKDTKQLLANYQ-----------------SVPN 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663530329 329 HMITLL--ENELHKH--GKELSSAKISILG---LCYKKNVPDIRLSPTLSIIEQLKEKKVNFLVCDPVYEK 392
Cdd:PRK15057 271 NLISAIvdANRTRKDfiADAILSRKPQVVGiyrLIMKSGSDNFRASSIQGIMKRIKAKGVEVIIYEPVMKE 341
|
|
| GpsA |
COG0240 |
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ... |
20-133 |
7.36e-10 |
|
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440010 [Multi-domain] Cd Length: 327 Bit Score: 60.05 E-value: 7.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKvvyEYTDILEDVVLkSKKLHVTIEPKEALDNAEIIFVC 99
Cdd:COG0240 2 KIAVLGAGSWGTALAKVLARNGHEVTLWGRDPEVAEEINETR---ENPRYLPGVKL-PENLRATSDLEEALAGADLVLLA 77
|
90 100 110
....*....|....*....|....*....|....
gi 663530329 100 VPTplnikkemdnSNLLDVANRISPYLTKGMILI 133
Cdd:COG0240 78 VPS----------QALREVLEQLAPLLPPGAPVV 101
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
20-148 |
4.27e-08 |
|
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: 52.47 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVVYEYTdiledvvlkskklhvtiePKEALDNAEIIFVC 99
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAAS------------------PAEFVAGLDVVITM 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 663530329 100 VPTPLNIKKEMDNSNLLdvanrisPYLTKGMILIFESSVAIGSTREISK 148
Cdd:pfam03446 63 VPAGAAVDAVIFGEGLL-------PGLKPGDIIIDGSTSSPEDARRRAK 104
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
20-151 |
1.14e-07 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 53.20 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEinsakvvyeytdiledvvLKSKKLHVTIEPKEALDNAEIIFVC 99
Cdd:COG2084 3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEA------------------LVAAGARVAASPAEAAAAADVVITM 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 663530329 100 VPTPlnikKEMDnsNLLDVANRISPYLTKGMILIFESSVAIGSTREISKTIE 151
Cdd:COG2084 65 LPDD----AAVE--EVLLGEDGLLAALRPGAVVVDMSTISPETARELAAAAA 110
|
|
| gpsA |
PRK00094 |
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; |
20-133 |
1.51e-07 |
|
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
Pssm-ID: 234629 [Multi-domain] Cd Length: 325 Bit Score: 53.15 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVVYEYtdiLEDVVLkSKKLHVTIEPKEALDNAEIIFVC 99
Cdd:PRK00094 3 KIAVLGAGSWGTALAIVLARNGHDVTLWARDPEQAAEINADRENPRY---LPGIKL-PDNLRATTDLAEALADADLILVA 78
|
90 100 110
....*....|....*....|....*....|....
gi 663530329 100 VPTplnikkemdnSNLLDVANRISPYLTKGMILI 133
Cdd:PRK00094 79 VPS----------QALREVLKQLKPLLPPDAPIV 102
|
|
| NAD_Gly3P_dh_N |
pfam01210 |
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ... |
21-133 |
1.98e-07 |
|
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: 50.65 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 21 VCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVVYEYtdiLEDVVLkSKKLHVTIEPKEALDNAEIIFVCV 100
Cdd:pfam01210 2 IAVLGAGSWGTALAKVLADNGHEVRLWGRDEELIEEINTTHENVRY---LPGIKL-PENLKATTDLAEALKGADIIVIVV 77
|
90 100 110
....*....|....*....|....*....|...
gi 663530329 101 PTplnikkemdnSNLLDVANRISPYLTKGMILI 133
Cdd:pfam01210 78 PS----------QALREVLKQLKGLLKPDAILV 100
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
20-133 |
6.37e-07 |
|
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: 50.90 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIG--LPLAtfLAKVGF--QVTGLDIDQKRIDEINSAKVVYEYTDiledvvlkskklhvtiEPKEALDNAEI 95
Cdd:COG0287 3 RIAIIGLGLIGgsLALA--LKRAGLahEVVGVDRSPETLERALELGVIDRAAT----------------DLEEAVADADL 64
|
90 100 110
....*....|....*....|....*....|....*...
gi 663530329 96 IFVCVPTPLNIkkemdnsnllDVANRISPYLTKGMILI 133
Cdd:COG0287 65 VVLAVPVGATI----------EVLAELAPHLKPGAIVT 92
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
17-153 |
2.20e-05 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 45.82 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 17 MDVRVCVIGVGTIGLPLATFLAKVGF---QVTGLDIDQKRIDEINSAKVVyeytdiledvvlkskklHVTIEPKEALDNA 93
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSGVppeDIIVSDRSPERLEALAERYGV-----------------RVTTDNAEAAAQA 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 94 EIIFVCVPtPLNIKkemdnsnllDVANRISPYLTKGMILIfesSVAIGstreisKTIESL 153
Cdd:COG0345 64 DVVVLAVK-PQDLA---------EVLEELAPLLDPDKLVI---SIAAG------VTLATL 104
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
17-273 |
1.37e-04 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 43.50 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 17 MDVRVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVVYEYTdiledvvlkskklhvtiePKEALDNAEII 96
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETAST------------------AKAVAEQCDVI 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 97 FVCVPTPLNIKKEMDNSN-LLDVANrispyltKGMILIFESSVAIGSTREISKTIEslcnlKFGIDLglaycperynptp 175
Cdd:PRK11559 63 ITMLPNSPHVKEVALGENgIIEGAK-------PGTVVIDMSSIAPLASREIAAALK-----AKGIEM------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 176 mkkytkdVDHTISAkGESFTVD-RISRVVGG---IDEKSTKITKTIYSQFVKTdvlelSSIETAEATKLLENIFRDVNIA 251
Cdd:PRK11559 118 -------LDAPVSG-GEPKAIDgTLSVMVGGdkaIFDKYYDLMKAMAGSVVHT-----GDIGAGNVTKLANQVIVALNIA 184
|
250 260
....*....|....*....|..
gi 663530329 252 LVNELAKIYPKFGLNIYEIINA 273
Cdd:PRK11559 185 AMSEALVLATKAGVNPDLVYQA 206
|
|
| PRK09260 |
PRK09260 |
3-hydroxyacyl-CoA dehydrogenase; |
20-124 |
1.89e-04 |
|
3-hydroxyacyl-CoA dehydrogenase;
Pssm-ID: 236434 [Multi-domain] Cd Length: 288 Bit Score: 43.24 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDeinsaKVVYEYTDILEDVVLKSK-----------KLHVTIEPKE 88
Cdd:PRK09260 3 KLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQLE-----SAQQEIASIFEQGVARGKlteaarqaalaRLSYSLDLKA 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 663530329 89 ALDNAEIIFVCVPTPLNIKKEmdnsnLLDVANRISP 124
Cdd:PRK09260 78 AVADADLVIEAVPEKLELKKA-----VFETADAHAP 108
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
10-116 |
3.48e-04 |
|
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: 42.36 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 10 SIRRIQEMDVRVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSAKVVYEYTDILEDVVLKskklhvtiepKEA 89
Cdd:COG0569 87 MERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATDEEVLE----------EAG 156
|
90 100
....*....|....*....|....*..
gi 663530329 90 LDNAEIIFVCVPTplnikkemDNSNLL 116
Cdd:COG0569 157 IEDADAVIAATGD--------DEANIL 175
|
|
| ApbA |
pfam02558 |
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ... |
21-134 |
6.46e-04 |
|
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.
Pssm-ID: 426831 [Multi-domain] Cd Length: 147 Bit Score: 39.91 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 21 VCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIdEINSAKvvYEYTDILEDVVLKSKklhVTIEPKEALDNAEIIFVCV 100
Cdd:pfam02558 1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELA-AIKKNG--LRLTSPGGERIVPPP---AVTSASESLGPIDLVIVTV 74
|
90 100 110
....*....|....*....|....*....|....
gi 663530329 101 ptplnikKEMDnsnLLDVANRISPYLTKGMILIF 134
Cdd:pfam02558 75 -------KAYQ---TEEALEDIAPLLGPNTVVLL 98
|
|
| PRK06522 |
PRK06522 |
2-dehydropantoate 2-reductase; Reviewed |
19-134 |
1.20e-03 |
|
2-dehydropantoate 2-reductase; Reviewed
Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 40.60 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 19 VRVCVIGVGTIGLPLATFLAKVGFQVTGLDIDQKRIDEINSakvvyeytdilEDVVLKSKKLHV---TIEPKEALDNAEI 95
Cdd:PRK06522 1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNE-----------NGLRLEDGEITVpvlAADDPAELGPQDL 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 663530329 96 IFVCVptplnikKEMDNSnllDVANRISPYLTKGMILIF 134
Cdd:PRK06522 70 VILAV-------KAYQLP---AALPSLAPLLGPDTPVLF 98
|
|
| 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ |
cd08255 |
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ... |
20-53 |
8.64e-03 |
|
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (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. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176217 [Multi-domain] Cd Length: 277 Bit Score: 38.02 E-value: 8.64e-03
10 20 30
....*....|....*....|....*....|....*
gi 663530329 20 RVCVIGVGTIGLPLATFLAKVGFQ-VTGLDIDQKR 53
Cdd:cd08255 100 RVAVVGLGLVGLLAAQLAKAAGAReVVGVDPDAAR 134
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
7-75 |
8.82e-03 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 36.15 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663530329 7 LPNSIRRIQEMDVRVCVIGVGTiGLpLATFLAKVGFQVTGLDIDQKRIDE----INSAKVVYEYTDILE--------DVV 74
Cdd:COG2227 14 LAALLARLLPAGGRVLDVGCGT-GR-LALALARRGADVTGVDISPEALEIarerAAELNVDFVQGDLEDlpledgsfDLV 91
|
.
gi 663530329 75 L 75
Cdd:COG2227 92 I 92
|
|
|