|
Name |
Accession |
Description |
Interval |
E-value |
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
11-511 |
0e+00 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 764.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 11 FEERVETIKQGGAPKYHEQNKAKGKLFVRDRLALLFDNGEYVEDALFANCEQTGL----PADGVVTATGKIHGRTACVMA 86
Cdd:COG4799 9 LRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYDDddrvPGDGVVTGIGTVDGRPVVVVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 87 NDSTVKAGSWGSRTVEKILRIQETAEKLRVPLFYLVDSAGARITDQVEMFpgrRGAGRIFYNQVKLSGKVPQVCLLFGPS 166
Cdd:COG4799 89 NDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESF---AGYGRIFYRNARSSGGIPQISVIMGPC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 167 AAGGAYIPAFCDVVMMVEGNASMYLGSPRMAEMVIGEKVTLEEMGGARMHCSVSGCGDVLCKTEEDAITQARQYISYFPN 246
Cdd:COG4799 166 AAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLSYLPS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 247 NYLEKTPLVTPQEPKQFDKTLEQIIPENQNAPFNMKDLINRVIDEGSFYEVKKLFAQELITGLARIDGKPVGIIANQPRM 326
Cdd:COG4799 246 NNLEDPPRAEPAPPARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVANQPMV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 327 KGGVLFHDSADKAAKFINLCDAYHIPLLFLADVPGFMIGTKVERAGIIRHGAKMISAMSEATVPKISIVVRKAYGAGLYA 406
Cdd:COG4799 326 LAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYGAGYYA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 407 MAGPAFEPDCCLALPTASIAVMGPEAAVNAVYANKIAALPEEERasFIAEKREEYKKDIDIYHLASEMVIDGIVHPNNLR 486
Cdd:COG4799 406 MCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAAEDPEA--LRAELIAEYEEQANPYYAAARGWIDDVIDPRDTR 483
|
490 500
....*....|....*....|....*
gi 446809499 487 EELKGRFEMYMSKYQVFTDRKHPVY 511
Cdd:COG4799 484 RVLARALEAAANKPEERPPKKHGVI 508
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
29-511 |
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: 546.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 29 QNKAKGKLFVRDRLALLFDNGEYVE--DALFANCEQTG---LPADGVVTATGKIHGRTACVMANDSTVKAGSWGSRTVEK 103
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGEleDLFFHRATEFGrkrIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 104 ILRIQETAEKLRVPLFYLVDSAGARITdqvEMFPGRRGAGRIFYNQVKLSGKVPQVCLLFGPSAAGGAYIPAFCDVVMMV 183
Cdd:pfam01039 81 ILRAMEIAIKTGLPLIGINDSGGARIQ---EGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGGAYLPALGDFVIMV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 184 EGNASMYLGSPRMAEMVIGEKVTLEEMGGARMHCSVSGCGDVLCKTEEDAITQARQYISYFP---NNYLEKTPLVTPQEP 260
Cdd:pfam01039 158 EGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPkpaPNNREPVPIVPTKDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 261 KQFDKTLEQIIPENQNAPFNMKDLINRVIDEGSFYEVKKLFAQELITGLARIDGKPVGIIANQPRMKGGVLFHDSADKAA 340
Cdd:pfam01039 238 PDRDAPLVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADKAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 341 KFINLCDAYHIPLLFLADVPGFMIGTKVERAGIIRHGAKMISAMSEATVPKISIVVRKAYGAGLYAMAGPAFEPDCCLAL 420
Cdd:pfam01039 318 RFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 421 PTASIAVMGPEAAVNAVYANKIAALPEE--ERASFIAEKREEYKKD-IDIYHLASEMVIDGIVHPNNLREELKGRFEMYM 497
Cdd:pfam01039 398 PTARIAVMGPEGAVEIKFRKEKAAAEMRgkDLAATRKQKIAEYEEElSPPYVAAARGFADAVIDPGRTRAKLVIALAALW 477
|
490
....*....|....
gi 446809499 498 SKYQVFTDRKHPVY 511
Cdd:pfam01039 478 TKPRFFPWRKHGNI 491
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
13-486 |
2.68e-131 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 393.02 E-value: 2.68e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 13 ERVETIKQGGAPKYHEQNKAKGKLFVRDRLALLFDNGE-YVEDALFANCEQTG--LPADGVVTATGKIHGRTACVMANDS 89
Cdd:PLN02820 59 SHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSpFLELSQLAGHELYGedLPSGGIVTGIGPVHGRLCMFVANDP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 90 TVKAGSWGSRTVEKILRIQETAEKLRVPLFYLVDSAGARITDQVEMFPGRRGAGRIFYNQVKLSGK-VPQVCLLFGPSAA 168
Cdd:PLN02820 139 TVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIFYNQARMSSAgIPQIALVLGSCTA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 169 GGAYIPAFCDVVMMVEGNASMYLGSPRMAEMVIGEKVTLEEMGGARMHCSVSGCGDVLCKTEEDAITQARQYISYFP--- 245
Cdd:PLN02820 219 GGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDHFAQDELHALAIGRNIVKNLHlaa 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 246 -----NNYLEKTPLVtpQEPKQFDKTLEQIIPENQNAPFNMKDLINRVIDEGSFYEVKKLFAQELITGLARIDGKPVGII 320
Cdd:PLN02820 299 kqgmeNTLGSKNPEY--KEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEFDEFKKNYGTTLVTGFARIYGQPVGII 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 321 ANQprmkgGVLFHDSADKAAKFINLCDAYHIPLLFLADVPGFMIGTKVERAGIIRHGAKMISAMSEATVPKISIVVRKAY 400
Cdd:PLN02820 377 GNN-----GILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMVMAVACAKVPKITIIVGGSF 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 401 GAGLYAMAGPAFEPDCCLALPTASIAVMGPEAAVNA---VYANKIAA----LPEEERASFIAEKREEYKKDIDIYHLASE 473
Cdd:PLN02820 452 GAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVlaqIERENKKRqgiqWSKEEEEAFKAKTVEAYEREANPYYSTAR 531
|
490
....*....|...
gi 446809499 474 MVIDGIVHPNNLR 486
Cdd:PLN02820 532 LWDDGVIDPADTR 544
|
|
| malonate_gamma |
TIGR03134 |
biotin-independent malonate decarboxylase, gamma subunit; Members of this protein family are ... |
282-433 |
8.98e-05 |
|
biotin-independent malonate decarboxylase, gamma subunit; Members of this protein family are the gamma subunit of malonate decarboxylase. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. In the malonate decarboxylase complex, the beta subunit appears to act as a malonyl-CoA decarboxylase, while the gamma subunit appears either to mediate subunit interaction or to act as a co-decarboxylase with the beta subunit. The beta and gamma subunits exhibit some local sequence similarity.
Pssm-ID: 274441 Cd Length: 238 Bit Score: 44.16 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 282 KDLINRVIDEGSFYEVkklfAQELITGLARIDGKPVGIIANQPRMKGGVlfhDSADKAAKFInlcdaYHI-------PLL 354
Cdd:TIGR03134 3 RDWLAALFPNGHEVAG----DPGVLVGSAELAGGKVTVIGVVPDAEVGL---DEGLALAQAV-----LDVieadpkrPIV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 355 FLADVPGFMIGTKVERAGIIRHGAKMISAMSEATV---PKISIVVRKAYGAGLYAMAGPAfepDCCLALPTASIAVMGPE 431
Cdd:TIGR03134 71 VLVDTPSQAYGRREELLGINQALAHLAKALALARLaghPVIGLVYGRAISGAFLAHGLQA---DRIIALPGAMVHVMDLE 147
|
..
gi 446809499 432 AA 433
Cdd:TIGR03134 148 SM 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
11-511 |
0e+00 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 764.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 11 FEERVETIKQGGAPKYHEQNKAKGKLFVRDRLALLFDNGEYVEDALFANCEQTGL----PADGVVTATGKIHGRTACVMA 86
Cdd:COG4799 9 LRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGSFLELGALAGHRMYDDddrvPGDGVVTGIGTVDGRPVVVVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 87 NDSTVKAGSWGSRTVEKILRIQETAEKLRVPLFYLVDSAGARITDQVEMFpgrRGAGRIFYNQVKLSGKVPQVCLLFGPS 166
Cdd:COG4799 89 NDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESF---AGYGRIFYRNARSSGGIPQISVIMGPC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 167 AAGGAYIPAFCDVVMMVEGNASMYLGSPRMAEMVIGEKVTLEEMGGARMHCSVSGCGDVLCKTEEDAITQARQYISYFPN 246
Cdd:COG4799 166 AAGGAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLSYLPS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 247 NYLEKTPLVTPQEPKQFDKTLEQIIPENQNAPFNMKDLINRVIDEGSFYEVKKLFAQELITGLARIDGKPVGIIANQPRM 326
Cdd:COG4799 246 NNLEDPPRAEPAPPARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVANQPMV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 327 KGGVLFHDSADKAAKFINLCDAYHIPLLFLADVPGFMIGTKVERAGIIRHGAKMISAMSEATVPKISIVVRKAYGAGLYA 406
Cdd:COG4799 326 LAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYGAGYYA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 407 MAGPAFEPDCCLALPTASIAVMGPEAAVNAVYANKIAALPEEERasFIAEKREEYKKDIDIYHLASEMVIDGIVHPNNLR 486
Cdd:COG4799 406 MCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAAEDPEA--LRAELIAEYEEQANPYYAAARGWIDDVIDPRDTR 483
|
490 500
....*....|....*....|....*
gi 446809499 487 EELKGRFEMYMSKYQVFTDRKHPVY 511
Cdd:COG4799 484 RVLARALEAAANKPEERPPKKHGVI 508
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
29-511 |
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: 546.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 29 QNKAKGKLFVRDRLALLFDNGEYVE--DALFANCEQTG---LPADGVVTATGKIHGRTACVMANDSTVKAGSWGSRTVEK 103
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGEleDLFFHRATEFGrkrIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 104 ILRIQETAEKLRVPLFYLVDSAGARITdqvEMFPGRRGAGRIFYNQVKLSGKVPQVCLLFGPSAAGGAYIPAFCDVVMMV 183
Cdd:pfam01039 81 ILRAMEIAIKTGLPLIGINDSGGARIQ---EGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGGAYLPALGDFVIMV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 184 EGNASMYLGSPRMAEMVIGEKVTLEEMGGARMHCSVSGCGDVLCKTEEDAITQARQYISYFP---NNYLEKTPLVTPQEP 260
Cdd:pfam01039 158 EGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPkpaPNNREPVPIVPTKDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 261 KQFDKTLEQIIPENQNAPFNMKDLINRVIDEGSFYEVKKLFAQELITGLARIDGKPVGIIANQPRMKGGVLFHDSADKAA 340
Cdd:pfam01039 238 PDRDAPLVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADKAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 341 KFINLCDAYHIPLLFLADVPGFMIGTKVERAGIIRHGAKMISAMSEATVPKISIVVRKAYGAGLYAMAGPAFEPDCCLAL 420
Cdd:pfam01039 318 RFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 421 PTASIAVMGPEAAVNAVYANKIAALPEE--ERASFIAEKREEYKKD-IDIYHLASEMVIDGIVHPNNLREELKGRFEMYM 497
Cdd:pfam01039 398 PTARIAVMGPEGAVEIKFRKEKAAAEMRgkDLAATRKQKIAEYEEElSPPYVAAARGFADAVIDPGRTRAKLVIALAALW 477
|
490
....*....|....
gi 446809499 498 SKYQVFTDRKHPVY 511
Cdd:pfam01039 478 TKPRFFPWRKHGNI 491
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
13-486 |
2.68e-131 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 393.02 E-value: 2.68e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 13 ERVETIKQGGAPKYHEQNKAKGKLFVRDRLALLFDNGE-YVEDALFANCEQTG--LPADGVVTATGKIHGRTACVMANDS 89
Cdd:PLN02820 59 SHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSpFLELSQLAGHELYGedLPSGGIVTGIGPVHGRLCMFVANDP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 90 TVKAGSWGSRTVEKILRIQETAEKLRVPLFYLVDSAGARITDQVEMFPGRRGAGRIFYNQVKLSGK-VPQVCLLFGPSAA 168
Cdd:PLN02820 139 TVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIFYNQARMSSAgIPQIALVLGSCTA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 169 GGAYIPAFCDVVMMVEGNASMYLGSPRMAEMVIGEKVTLEEMGGARMHCSVSGCGDVLCKTEEDAITQARQYISYFP--- 245
Cdd:PLN02820 219 GGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSDHFAQDELHALAIGRNIVKNLHlaa 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 246 -----NNYLEKTPLVtpQEPKQFDKTLEQIIPENQNAPFNMKDLINRVIDEGSFYEVKKLFAQELITGLARIDGKPVGII 320
Cdd:PLN02820 299 kqgmeNTLGSKNPEY--KEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEFDEFKKNYGTTLVTGFARIYGQPVGII 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 321 ANQprmkgGVLFHDSADKAAKFINLCDAYHIPLLFLADVPGFMIGTKVERAGIIRHGAKMISAMSEATVPKISIVVRKAY 400
Cdd:PLN02820 377 GNN-----GILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMVMAVACAKVPKITIIVGGSF 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 401 GAGLYAMAGPAFEPDCCLALPTASIAVMGPEAAVNA---VYANKIAA----LPEEERASFIAEKREEYKKDIDIYHLASE 473
Cdd:PLN02820 452 GAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVlaqIERENKKRqgiqWSKEEEEAFKAKTVEAYEREANPYYSTAR 531
|
490
....*....|...
gi 446809499 474 MVIDGIVHPNNLR 486
Cdd:PLN02820 532 LWDDGVIDPADTR 544
|
|
| AccD |
COG0777 |
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
39-129 |
2.54e-10 |
|
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: 61.23 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 39 RDRLALLFDNGEYVE--------DAL-FANC-----------EQTGLPaDGVVTATGKIHGRTACVMANDSTVKAGSWGS 98
Cdd:COG0777 59 RERLELLLDEGSFEEldadlvpvDPLkFKDSkkykdrlkeaqKKTGLK-DAVVTGTGTINGIPVVVAVMDFSFMGGSMGS 137
|
90 100 110
....*....|....*....|....*....|.
gi 446809499 99 RTVEKILRIQETAEKLRVPLFYLVDSAGARI 129
Cdd:COG0777 138 VVGEKITRAIERAIEKKLPLIIFSASGGARM 168
|
|
| PRK05724 |
PRK05724 |
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated |
103-213 |
3.41e-05 |
|
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
Pssm-ID: 235580 [Multi-domain] Cd Length: 319 Bit Score: 45.90 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 103 KILRIQETAEKLRVPLFYLVDSAGAritdqvemFPG----RRGAGR-IFYNQVKLSG-KVPQVCLLFGPSAAGGAYIPAF 176
Cdd:PRK05724 139 KALRLMKMAEKFGLPIITFIDTPGA--------YPGigaeERGQSEaIARNLREMARlKVPIICTVIGEGGSGGALAIGV 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446809499 177 CDVVMMV----------EGNAS---------------MYLGSPRMAEMVIGEKVTLEEMGGA 213
Cdd:PRK05724 211 GDRVLMLeystysvispEGCASilwkdaskapeaaeaMKITAQDLKELGIIDEIIPEPLGGA 272
|
|
| malonate_gamma |
TIGR03134 |
biotin-independent malonate decarboxylase, gamma subunit; Members of this protein family are ... |
282-433 |
8.98e-05 |
|
biotin-independent malonate decarboxylase, gamma subunit; Members of this protein family are the gamma subunit of malonate decarboxylase. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. In the malonate decarboxylase complex, the beta subunit appears to act as a malonyl-CoA decarboxylase, while the gamma subunit appears either to mediate subunit interaction or to act as a co-decarboxylase with the beta subunit. The beta and gamma subunits exhibit some local sequence similarity.
Pssm-ID: 274441 Cd Length: 238 Bit Score: 44.16 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 282 KDLINRVIDEGSFYEVkklfAQELITGLARIDGKPVGIIANQPRMKGGVlfhDSADKAAKFInlcdaYHI-------PLL 354
Cdd:TIGR03134 3 RDWLAALFPNGHEVAG----DPGVLVGSAELAGGKVTVIGVVPDAEVGL---DEGLALAQAV-----LDVieadpkrPIV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 355 FLADVPGFMIGTKVERAGIIRHGAKMISAMSEATV---PKISIVVRKAYGAGLYAMAGPAfepDCCLALPTASIAVMGPE 431
Cdd:TIGR03134 71 VLVDTPSQAYGRREELLGINQALAHLAKALALARLaghPVIGLVYGRAISGAFLAHGLQA---DRIIALPGAMVHVMDLE 147
|
..
gi 446809499 432 AA 433
Cdd:TIGR03134 148 SM 149
|
|
| PRK05724 |
PRK05724 |
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated |
283-396 |
1.79e-04 |
|
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
Pssm-ID: 235580 [Multi-domain] Cd Length: 319 Bit Score: 43.59 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 283 DLINRVIDEgsFYEVK--KLFA--QELITGLARIDGKPVGIIANQprmKGgvlfHDSAD---------------KAAKFI 343
Cdd:PRK05724 74 DYIELLFTD--FTELHgdRAFAddKAIVGGLARLNGRPVMVIGHQ---KG----RDTKEkirrnfgmprpegyrKALRLM 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446809499 344 NLCDAYHIPLLFLADVPGFMIGTKVERAGI---IrhgAKMISAMSEATVPKISIVV 396
Cdd:PRK05724 145 KMAEKFGLPIITFIDTPGAYPGIGAEERGQseaI---ARNLREMARLKVPIICTVI 197
|
|
| AccA |
COG0825 |
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
103-184 |
4.37e-04 |
|
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: 42.33 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 103 KILRIQETAEKLRVPLFYLVDSAGAritdqvemFPGR----RGAGR-IFYNQVKLSG-KVPQVCLLFGPSAAGGAYIPAF 176
Cdd:COG0825 136 KALRLMKLAEKFGLPIITFIDTPGA--------YPGIgaeeRGQSEaIARNLREMARlKVPIISVVIGEGGSGGALAIGV 207
|
....*...
gi 446809499 177 CDVVMMVE 184
Cdd:COG0825 208 GDRVLMLE 215
|
|
| AccA |
COG0825 |
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
283-396 |
6.87e-04 |
|
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: 41.95 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 283 DLINRVIDEgsFYEVK--KLFA--QELITGLARIDGKPVGIIANQprmKGgvlfHDSAD---------------KAAKFI 343
Cdd:COG0825 71 DYIEAIFTD--FIELHgdRAFGddPAIVGGLARFDGRPVMVIGHQ---KG----RDTKErikrnfgmphpegyrKALRLM 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446809499 344 NLCDAYHIPLLFLADVPGFMIGTKVERAGI---IrhgAKMISAMSEATVPKISIVV 396
Cdd:COG0825 142 KLAEKFGLPIITFIDTPGAYPGIGAEERGQseaI---ARNLREMARLKVPIISVVI 194
|
|
| PRK12319 |
PRK12319 |
acetyl-CoA carboxylase subunit alpha; Provisional |
103-190 |
8.32e-04 |
|
acetyl-CoA carboxylase subunit alpha; Provisional
Pssm-ID: 183435 [Multi-domain] Cd Length: 256 Bit Score: 41.30 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 103 KILRIQETAEKLRVPLFYLVDSAGAritdqvemFPG----RRGAGR-IFYNQVKLSG-KVPQVCLLFGPSAAGGAYIPAF 176
Cdd:PRK12319 86 KALRLMKQAEKFGRPVVTFINTAGA--------YPGvgaeERGQGEaIARNLMEMSDlKVPIIAIIIGEGGSGGALALAV 157
|
90
....*....|....
gi 446809499 177 CDVVMMVEGnaSMY 190
Cdd:PRK12319 158 ADQVWMLEN--TMY 169
|
|
| accD |
CHL00174 |
acetyl-CoA carboxylase beta subunit; Reviewed |
61-128 |
9.92e-04 |
|
acetyl-CoA carboxylase beta subunit; Reviewed
Pssm-ID: 214384 [Multi-domain] Cd Length: 296 Bit Score: 41.04 E-value: 9.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446809499 61 EQTGLPaDGVVTATGKIHGRTAC--VManDSTVKAGSWGSRTVEKILRIQETAEKLRVPLFYLVDSAGAR 128
Cdd:CHL00174 115 KKTGLT-DAVQTGIGQLNGIPVAlgVM--DFQFMGGSMGSVVGEKITRLIEYATNESLPLIIVCASGGAR 181
|
|
| |
