|
Name |
Accession |
Description |
Interval |
E-value |
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
53-546 |
0e+00 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 810.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 53 ERIEQKRQAALTGGGQLRIAAQHKRGKLTARERVELLLDADSFVEYDMFVEHRCSDfgmeaDQNKYPGDSVVTGQGRING 132
Cdd:COG4799 7 AELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYD-----DDDRVPGDGVVTGIGTVDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 133 RLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAMLVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVMASGVVPQISLI 212
Cdd:COG4799 82 RPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGGIPQISVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 213 MGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTAVSGVAHRAFENDIDALLNLRDFFN 292
Cdd:COG4799 162 MGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 293 FLPLSNKDSAPVVECHDPrDRLVPGLDTVVPFESTKAYDMLDIVHGIVDEREFFEIMPNYAKNIVVGFARMNGRTVGIVG 372
Cdd:COG4799 242 YLPSNNLEDPPRAEPAPP-ARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 373 NQPKVASGCLDINSSVKGARFVRFCDAFNIPIITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYG 452
Cdd:COG4799 321 NQPMVLAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 453 GAYDVMSSKHLRGDVNYAWPTAEVAVMGAKGAVQIIFRGKQNQAEAEAEYV-------EKFANPFPAAVRGFVDDIIQPS 525
Cdd:COG4799 401 AGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAAEDPEALRaeliaeyEEQANPYYAAARGWIDDVIDPR 480
|
490 500
....*....|....*....|.
gi 47086189 526 TTRRRICRDLEVLASKKQTNP 546
Cdd:COG4799 481 DTRRVLARALEAAANKPEERP 501
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
73-547 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 702.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 73 AQHKRGKLTARERVELLLDADSFVEYDMFVEHRCSDFGMEadqnKYPGDSVVTGQGRINGRLVYVFSQDFTVFGGSLSGA 152
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRK----RIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 153 HAQKICKIMDQAMLVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVMASGVVPQISLIMGPCAGGAVYSPALTDFTFM 232
Cdd:pfam01039 77 KGEKILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGGAYLPALGDFVIM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 233 VKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTAVSGVAHRAFENDIDALLNLRDFFNFLPL---SNKDSAPVVECHD 309
Cdd:pfam01039 157 VEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKpapNNREPVPIVPTKD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 310 PRDRLVPgLDTVVPFESTKAYDMLDIVHGIVDEREFFEIMPNYAKNIVVGFARMNGRTVGIVGNQPKVASGCLDINSSVK 389
Cdd:pfam01039 237 PPDRDAP-LVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 390 GARFVRFCDAFNIPIITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDVMSSKHLRGDVNY 469
Cdd:pfam01039 316 AARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 470 AWPTAEVAVMGAKGAVQIIFRGKQNQAEAE------------AEYVEKFANPFPAAVRGFVDDIIQPSTTRRRICRDLEV 537
Cdd:pfam01039 396 AWPTARIAVMGPEGAVEIKFRKEKAAAEMRgkdlaatrkqkiAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAA 475
|
490
....*....|
gi 47086189 538 LASKKQTNPC 547
Cdd:pfam01039 476 LWTKPRFFPW 485
|
|
| mmdA |
TIGR01117 |
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA ... |
53-546 |
0e+00 |
|
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA decarboxylase aplha subunit in archaea and bacteria. Metylmalonyl-CoA decarboxylase Na+ pump is a representative of a class of Na+ transport decarboxylases that couples the energy derived by decarboxylation of carboxylic acid substrates to drive the extrusion of Na+ ion across the membrane. [Energy metabolism, ATP-proton motive force interconversion, Energy metabolism, Fermentation, Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130187 Cd Length: 512 Bit Score: 688.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 53 ERIEQKRQAALTGGGQLRIAAQHKRGKLTARERVELLLDADSFVEYDMFVEHRCSDFGMeaDQNKYPGDSVVTGQGRING 132
Cdd:TIGR01117 4 EELHEKKEKIKQGGGEKRIEKQHAQGKMTARERLALLFDPGSFVEIDQFVKHRCTNFGM--DKKELPAEGVVTGYGTIDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 133 RLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAMLVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVMASGVVPQISLI 212
Cdd:TIGR01117 82 RLVYAFAQDFTVMGGSLGEMHAAKIVKIMDLAMKMGAPVVGLNDSGGARIQEAVDALKGYGDIFYRNTIASGVVPQISAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 213 MGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTAVSGVAHRAFENDIDALLNLRDFFN 292
Cdd:TIGR01117 162 MGPCAGGAVYSPALTDFIYMVDNTSQMFITGPQVIKTVTGEEVTAEQLGGAMAHNSVSGVAHFIAEDDDDCIMLIRRLLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 293 FLPLSNKDSAPVVECHDPRDRLVPGLDTVVPFESTKAYDMLDIVHGIVDEREFFEIMPNYAKNIVVGFARMNGRTVGIVG 372
Cdd:TIGR01117 242 FLPSNNMEKAPLVKTGDDPTRETPELYDLLPDNPNKPYDMRDVITAIVDNGDYLEVQPYYAPNIITCFARINGQSVGIIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 373 NQPKVASGCLDINSSVKGARFVRFCDAFNIPIITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYG 452
Cdd:TIGR01117 322 NQPKVMAGCLDIDSSDKIARFIRFCDAFNIPIVTFVDVPGFLPGVNQEYGGIIRHGAKVLYAYSEATVPKVTIITRKAYG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 453 GAYDVMSSKHLRGDVNYAWPTAEVAVMGAKGAVQIIFRGKQNQAEAEA--------EYVEKFANPFPAAVRGFVDDIIQP 524
Cdd:TIGR01117 402 GAYLAMCSKHLGADQVYAWPTAEIAVMGPAGAANIIFRKDIKEAKDPAatrkqkiaEYREEFANPYKAAARGYVDDVIEP 481
|
490 500
....*....|....*....|..
gi 47086189 525 STTRRRICRDLEVLASKKQTNP 546
Cdd:TIGR01117 482 KQTRPKIVNALAMLESKREKLP 503
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
16-529 |
2.32e-85 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 275.53 E-value: 2.32e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 16 GLKCPFkCVGQTQYGVFTQSKvlqNARCYSSSHMSVQERIEQKRQAALTGGGQLRIAAQHKRGKLTARERVELLLDADS- 94
Cdd:PLN02820 22 LGKRSF-CLGVLPDGVDRNSD---AFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 95 FVEYDMFvehrcSDFGMEADQnkYPGDSVVTGQGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAMLVGAPVIGL 174
Cdd:PLN02820 98 FLELSQL-----AGHELYGED--LPSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 175 NDSGGARIQEGVESLAG---YADIFL-RNVMASGVVPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSV 250
Cdd:PLN02820 171 VDSGGANLPRQAEVFPDrdhFGRIFYnQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 251 TNEDVTQEELGGAKTHTAVSGVAHRAFENDIDALLNLRDFFNFLPL------SNKDSAPVVECHDPrdrLVP--GLDTVV 322
Cdd:PLN02820 251 TGEEVSAEDLGGADVHCKVSGVSDHFAQDELHALAIGRNIVKNLHLaakqgmENTLGSKNPEYKEP---LYDvkELRGIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 323 PFESTKAYDMLDIVHGIVDEREFFEIMPNYAKNIVVGFARMNGRTVGIVGNqpkvaSGCLDINSSVKGARFVRFCDAFNI 402
Cdd:PLN02820 328 PADHKQSFDVRSVIARIVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIGN-----NGILFTESALKGAHFIELCAQRGI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 403 PIITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDVMSSKHLRGDVNYAWPTAEVAVMGAK 482
Cdd:PLN02820 403 PLLFLQNITGFMVGSRSEASGIAKAGAKMVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGA 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47086189 483 GAVQIIF---------RGKQNQAEAEA-------EYVEKFANPFPAAVRGFVDDIIQPSTTRR 529
Cdd:PLN02820 483 QAAGVLAqierenkkrQGIQWSKEEEEafkaktvEAYEREANPYYSTARLWDDGVIDPADTRR 545
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
53-546 |
0e+00 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 810.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 53 ERIEQKRQAALTGGGQLRIAAQHKRGKLTARERVELLLDADSFVEYDMFVEHRCSDfgmeaDQNKYPGDSVVTGQGRING 132
Cdd:COG4799 7 AELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYD-----DDDRVPGDGVVTGIGTVDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 133 RLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAMLVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVMASGVVPQISLI 212
Cdd:COG4799 82 RPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGGIPQISVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 213 MGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTAVSGVAHRAFENDIDALLNLRDFFN 292
Cdd:COG4799 162 MGPCAAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 293 FLPLSNKDSAPVVECHDPrDRLVPGLDTVVPFESTKAYDMLDIVHGIVDEREFFEIMPNYAKNIVVGFARMNGRTVGIVG 372
Cdd:COG4799 242 YLPSNNLEDPPRAEPAPP-ARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 373 NQPKVASGCLDINSSVKGARFVRFCDAFNIPIITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYG 452
Cdd:COG4799 321 NQPMVLAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 453 GAYDVMSSKHLRGDVNYAWPTAEVAVMGAKGAVQIIFRGKQNQAEAEAEYV-------EKFANPFPAAVRGFVDDIIQPS 525
Cdd:COG4799 401 AGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAAEDPEALRaeliaeyEEQANPYYAAARGWIDDVIDPR 480
|
490 500
....*....|....*....|.
gi 47086189 526 TTRRRICRDLEVLASKKQTNP 546
Cdd:COG4799 481 DTRRVLARALEAAANKPEERP 501
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
73-547 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 702.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 73 AQHKRGKLTARERVELLLDADSFVEYDMFVEHRCSDFGMEadqnKYPGDSVVTGQGRINGRLVYVFSQDFTVFGGSLSGA 152
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRK----RIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 153 HAQKICKIMDQAMLVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVMASGVVPQISLIMGPCAGGAVYSPALTDFTFM 232
Cdd:pfam01039 77 KGEKILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGGAYLPALGDFVIM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 233 VKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTAVSGVAHRAFENDIDALLNLRDFFNFLPL---SNKDSAPVVECHD 309
Cdd:pfam01039 157 VEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKpapNNREPVPIVPTKD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 310 PRDRLVPgLDTVVPFESTKAYDMLDIVHGIVDEREFFEIMPNYAKNIVVGFARMNGRTVGIVGNQPKVASGCLDINSSVK 389
Cdd:pfam01039 237 PPDRDAP-LVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 390 GARFVRFCDAFNIPIITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDVMSSKHLRGDVNY 469
Cdd:pfam01039 316 AARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 470 AWPTAEVAVMGAKGAVQIIFRGKQNQAEAE------------AEYVEKFANPFPAAVRGFVDDIIQPSTTRRRICRDLEV 537
Cdd:pfam01039 396 AWPTARIAVMGPEGAVEIKFRKEKAAAEMRgkdlaatrkqkiAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAA 475
|
490
....*....|
gi 47086189 538 LASKKQTNPC 547
Cdd:pfam01039 476 LWTKPRFFPW 485
|
|
| mmdA |
TIGR01117 |
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA ... |
53-546 |
0e+00 |
|
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA decarboxylase aplha subunit in archaea and bacteria. Metylmalonyl-CoA decarboxylase Na+ pump is a representative of a class of Na+ transport decarboxylases that couples the energy derived by decarboxylation of carboxylic acid substrates to drive the extrusion of Na+ ion across the membrane. [Energy metabolism, ATP-proton motive force interconversion, Energy metabolism, Fermentation, Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130187 Cd Length: 512 Bit Score: 688.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 53 ERIEQKRQAALTGGGQLRIAAQHKRGKLTARERVELLLDADSFVEYDMFVEHRCSDFGMeaDQNKYPGDSVVTGQGRING 132
Cdd:TIGR01117 4 EELHEKKEKIKQGGGEKRIEKQHAQGKMTARERLALLFDPGSFVEIDQFVKHRCTNFGM--DKKELPAEGVVTGYGTIDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 133 RLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAMLVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVMASGVVPQISLI 212
Cdd:TIGR01117 82 RLVYAFAQDFTVMGGSLGEMHAAKIVKIMDLAMKMGAPVVGLNDSGGARIQEAVDALKGYGDIFYRNTIASGVVPQISAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 213 MGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTAVSGVAHRAFENDIDALLNLRDFFN 292
Cdd:TIGR01117 162 MGPCAGGAVYSPALTDFIYMVDNTSQMFITGPQVIKTVTGEEVTAEQLGGAMAHNSVSGVAHFIAEDDDDCIMLIRRLLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 293 FLPLSNKDSAPVVECHDPRDRLVPGLDTVVPFESTKAYDMLDIVHGIVDEREFFEIMPNYAKNIVVGFARMNGRTVGIVG 372
Cdd:TIGR01117 242 FLPSNNMEKAPLVKTGDDPTRETPELYDLLPDNPNKPYDMRDVITAIVDNGDYLEVQPYYAPNIITCFARINGQSVGIIA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 373 NQPKVASGCLDINSSVKGARFVRFCDAFNIPIITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYG 452
Cdd:TIGR01117 322 NQPKVMAGCLDIDSSDKIARFIRFCDAFNIPIVTFVDVPGFLPGVNQEYGGIIRHGAKVLYAYSEATVPKVTIITRKAYG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 453 GAYDVMSSKHLRGDVNYAWPTAEVAVMGAKGAVQIIFRGKQNQAEAEA--------EYVEKFANPFPAAVRGFVDDIIQP 524
Cdd:TIGR01117 402 GAYLAMCSKHLGADQVYAWPTAEIAVMGPAGAANIIFRKDIKEAKDPAatrkqkiaEYREEFANPYKAAARGYVDDVIEP 481
|
490 500
....*....|....*....|..
gi 47086189 525 STTRRRICRDLEVLASKKQTNP 546
Cdd:TIGR01117 482 KQTRPKIVNALAMLESKREKLP 503
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
16-529 |
2.32e-85 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 275.53 E-value: 2.32e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 16 GLKCPFkCVGQTQYGVFTQSKvlqNARCYSSSHMSVQERIEQKRQAALTGGGQLRIAAQHKRGKLTARERVELLLDADS- 94
Cdd:PLN02820 22 LGKRSF-CLGVLPDGVDRNSD---AFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 95 FVEYDMFvehrcSDFGMEADQnkYPGDSVVTGQGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAMLVGAPVIGL 174
Cdd:PLN02820 98 FLELSQL-----AGHELYGED--LPSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 175 NDSGGARIQEGVESLAG---YADIFL-RNVMASGVVPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSV 250
Cdd:PLN02820 171 VDSGGANLPRQAEVFPDrdhFGRIFYnQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 251 TNEDVTQEELGGAKTHTAVSGVAHRAFENDIDALLNLRDFFNFLPL------SNKDSAPVVECHDPrdrLVP--GLDTVV 322
Cdd:PLN02820 251 TGEEVSAEDLGGADVHCKVSGVSDHFAQDELHALAIGRNIVKNLHLaakqgmENTLGSKNPEYKEP---LYDvkELRGIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 323 PFESTKAYDMLDIVHGIVDEREFFEIMPNYAKNIVVGFARMNGRTVGIVGNqpkvaSGCLDINSSVKGARFVRFCDAFNI 402
Cdd:PLN02820 328 PADHKQSFDVRSVIARIVDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIGN-----NGILFTESALKGAHFIELCAQRGI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 403 PIITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDVMSSKHLRGDVNYAWPTAEVAVMGAK 482
Cdd:PLN02820 403 PLLFLQNITGFMVGSRSEASGIAKAGAKMVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGA 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47086189 483 GAVQIIF---------RGKQNQAEAEA-------EYVEKFANPFPAAVRGFVDDIIQPSTTRR 529
Cdd:PLN02820 483 QAAGVLAqierenkkrQGIQWSKEEEEafkaktvEAYEREANPYYSTARLWDDGVIDPADTRR 545
|
|
| AccD |
COG0777 |
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
79-189 |
1.71e-18 |
|
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase beta subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440540 [Multi-domain] Cd Length: 280 Bit Score: 85.88 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 79 KLTARERVELLLDADSFVEYDmfvEHRCS----DFgmeADQNKYP------------GDSVVTGQGRINGRLVYVFSQDF 142
Cdd:COG0777 55 RISARERLELLLDEGSFEELD---ADLVPvdplKF---KDSKKYKdrlkeaqkktglKDAVVTGTGTINGIPVVVAVMDF 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 47086189 143 TVFGGSLSGAHAQKICKIMDQAMLVGAPVIGLNDSGGARIQEGVESL 189
Cdd:COG0777 129 SFMGGSMGSVVGEKITRAIERAIEKKLPLIIFSASGGARMQEGILSL 175
|
|
| PRK07189 |
PRK07189 |
malonate decarboxylase subunit beta; Reviewed |
80-283 |
7.31e-14 |
|
malonate decarboxylase subunit beta; Reviewed
Pssm-ID: 235954 Cd Length: 301 Bit Score: 72.24 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 80 LTARERVELLLDADSFVEY-DMFvEHRCS------DFGMEADqnkypgDSVVTGQGRINGRLVYVFSQDFTVFGGSLSGA 152
Cdd:PRK07189 15 ASARERAAALLDAGSFRELlGPF-ERVMSphlplqGIPPQFD------DGVVVGKGTLDGRPVVVAAQEGRFMGGSVGEV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 153 HAQKICKIMDQAMLVG-----APVIGLNDSGGARIQEGVESLAGYADIFLRNVMASGVVPQISLIMGP--CAGGAVYSPA 225
Cdd:PRK07189 88 HGAKLAGALELAAEDNrngipTAVLLLFETGGVRLQEANAGLAAIAEIMRAIVDLRAAVPVIGLIGGRvgCFGGMGIAAA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 226 LTDfTFMVKDTSYLFITGPDVVKsvTNEDVtqEEL------------GGAktHTAVSGVAHRAFENDIDA 283
Cdd:PRK07189 168 LCS-YLIVSEEGRLGLSGPEVIE--QEAGV--EEFdsrdralvwrttGGK--HRYLSGLADALVDDDVAA 230
|
|
| PRK05724 |
PRK05724 |
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated |
333-454 |
2.99e-09 |
|
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
Pssm-ID: 235580 [Multi-domain] Cd Length: 319 Bit Score: 58.62 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 333 LDIVHGIVDEreFFEIM--PNYA--KNIVVGFARMNGRTVGIVGNQpkvaSGClDINSSV-------------KGARFVR 395
Cdd:PRK05724 73 LDYIELLFTD--FTELHgdRAFAddKAIVGGLARLNGRPVMVIGHQ----KGR-DTKEKIrrnfgmprpegyrKALRLMK 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086189 396 FCDAFNIPIITFVDVPGFLPG-TAQEYG---GIirhgAKLLYAFAEATVPKI-TVITRKAYGGA 454
Cdd:PRK05724 146 MAEKFGLPIITFIDTPGAYPGiGAEERGqseAI----ARNLREMARLKVPIIcTVIGEGGSGGA 205
|
|
| AccA |
COG0825 |
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
333-447 |
8.08e-08 |
|
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase alpha subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440587 [Multi-domain] Cd Length: 315 Bit Score: 54.27 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 333 LDIVHGIVDEreFFEIM--PNYA--KNIVVGFARMNGRTVGIVGNQpKvasGClDINSSV-------------KGARFVR 395
Cdd:COG0825 70 LDYIEAIFTD--FIELHgdRAFGddPAIVGGLARFDGRPVMVIGHQ-K---GR-DTKERIkrnfgmphpegyrKALRLMK 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 47086189 396 FCDAFNIPIITFVDVPGFLPG-TAQEYG---GIirhgAKLLYAFAEATVPKITVIT 447
Cdd:COG0825 143 LAEKFGLPIITFIDTPGAYPGiGAEERGqseAI----ARNLREMARLKVPIISVVI 194
|
|
| accD |
CHL00174 |
acetyl-CoA carboxylase beta subunit; Reviewed |
79-195 |
5.55e-07 |
|
acetyl-CoA carboxylase beta subunit; Reviewed
Pssm-ID: 214384 [Multi-domain] Cd Length: 296 Bit Score: 51.44 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 79 KLTARERVELLLDADSFVEYDmfvEHRCS-D-FGMEADQNKYPG------------DSVVTGQGRINGRLVYVFSQDFTV 144
Cdd:CHL00174 68 KMSSSDRIELLIDPGTWNPMD---EDMVSlDpIEFHSDEEPYKDridsyqkktgltDAVQTGIGQLNGIPVALGVMDFQF 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 47086189 145 FGGSLSGAHAQKICKIMDQAMLVGAPVIGLNDSGGARIQEGVESLAGYADI 195
Cdd:CHL00174 145 MGGSMGSVVGEKITRLIEYATNESLPLIIVCASGGARMQEGSLSLMQMAKI 195
|
|
| PLN03230 |
PLN03230 |
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional |
332-454 |
2.78e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
Pssm-ID: 178769 [Multi-domain] Cd Length: 431 Bit Score: 46.86 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 332 MLDIVHGIVDEreFFEIMPNYA----KNIVVGFARMNGRTVGIVGNQPKVAS--------GCLDINSSVKGARFVRFCDA 399
Cdd:PLN03230 142 FLDHVLNMTDK--WVELHGDRAgfddPAIVCGIGSMEGMSFMFIGHQKGRNTkeniyrnfAMPQPNGYRKALRFMRHAEK 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 400 FNIPIITFVDVPGFLPG-TAQEYGgiirHGAKLLYAFAEA---TVPKI-TVITRKAYGGA 454
Cdd:PLN03230 220 FGFPILTFVDTPGAYAGiKAEELG----QGEAIAFNLREMfglRVPIIaTVIGEGGSGGA 275
|
|
| PRK12319 |
PRK12319 |
acetyl-CoA carboxylase subunit alpha; Provisional |
77-238 |
4.78e-03 |
|
acetyl-CoA carboxylase subunit alpha; Provisional
Pssm-ID: 183435 [Multi-domain] Cd Length: 256 Bit Score: 38.99 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 77 RGKLTARERVELLLDadSFVEydmfvehrcsdfgMEADQNKYPGDSVVTGQGRINGRLVYVFS-------QD--FTVFGG 147
Cdd:PRK12319 14 QGRLTTLDYATLIFD--DFME-------------LHGDRHFRDDGAVVGGIGYLAGQPVTVVGiqkgknlQDnlKRNFGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086189 148 SLSGAHaQKICKIMDQAMLVGAPVIGLNDSGGARIQEGVESlAGYADIFLRNV--MASGVVPQISLIMGPCAGGAVYSPA 225
Cdd:PRK12319 79 PHPEGY-RKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEE-RGQGEAIARNLmeMSDLKVPIIAIIIGEGGSGGALALA 156
|
170
....*....|...
gi 47086189 226 LTDFTFMVKDTSY 238
Cdd:PRK12319 157 VADQVWMLENTMY 169
|
|
|