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Conserved domains on  [gi|1549660765|gb|RVJ73308|]
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methylcrotonoyl-CoA carboxylase [Sinorhizobium medicae]

Protein Classification

carboxyltransferase domain-containing protein( domain architecture ID 1001328)

carboxyltransferase domain-containing protein catalyzes the transcarboxylation from biotin to an acyl-CoA acceptor molecule; similar to methylcrotonyl-CoA carboxylase subunit beta

CATH:  3.90.226.10
Gene Ontology:  GO:0016740|GO:0009374
PubMed:  8102604

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Carboxyl_trans super family cl47203
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
3-535 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.


The actual alignment was detected with superfamily member PLN02820:

Pssm-ID: 481543 [Multi-domain]  Cd Length: 569  Bit Score: 851.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765   3 VLRSHISPSSEGFKANRSAMAEAIAAIEDAVRLAASGGGDKARERHVSRGKLLPRDRVAALIDPGTPFLELGATAAHEMY 82
Cdd:PLN02820   31 VLPDGVDRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHELY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765  83 NGDAPAAGLITGIGRISGRECMIVCNDPTVKGGTYYPMTVKKHLRAQEIAAENRLPCVYLVDSGGANLPSQDEVFPDRDH 162
Cdd:PLN02820  111 GEDLPSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDH 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 163 FGRIFYNQANMSAAGIPQIAVVMGSCTAGGAYVPAMSDEAIIVEKQGTIFLAGPPLVRAATGEVVSAEELGGADVHTRLS 242
Cdd:PLN02820  191 FGRIFYNQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVS 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 243 GVADHLARDDAHALALARRAVSAL----NHEKPWPVQRIDPE--PPLYDPEEIAGIVPADLKTPYDIREVIARLVDGSRF 316
Cdd:PLN02820  271 GVSDHFAQDELHALAIGRNIVKNLhlaaKQGMENTLGSKNPEykEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEF 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 317 DEFKARFGTTLVCGFAHVHGIPVGIVANNGVLFSESAVKGAHFVELCAQRRIPLVFLQNITGFMVGRKYETEGIAKHGAK 396
Cdd:PLN02820  351 DEFKKNYGTTLVTGFARIYGQPVGIIGNNGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAK 430
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 397 LVTAVATVKVPKITMLVGGSFGAGNYGMCGRAFSPRFLWTWPNSRISVMGGEQAAGVLSSVRGEALKRSGLPWSEEEEAR 476
Cdd:PLN02820  431 MVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENKKRQGIQWSKEEEEA 510
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1549660765 477 FRQPVLDLFERQSHPLYASARLWDDGVIDPRKSRDVLALSLSAALNAPIEDTHFGLFRM 535
Cdd:PLN02820  511 FKAKTVEAYEREANPYYSTARLWDDGVIDPADTRRVLGLCLSAALNRSPEDTKFGVFRM 569
 
Name Accession Description Interval E-value
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
3-535 0e+00

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 851.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765   3 VLRSHISPSSEGFKANRSAMAEAIAAIEDAVRLAASGGGDKARERHVSRGKLLPRDRVAALIDPGTPFLELGATAAHEMY 82
Cdd:PLN02820   31 VLPDGVDRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHELY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765  83 NGDAPAAGLITGIGRISGRECMIVCNDPTVKGGTYYPMTVKKHLRAQEIAAENRLPCVYLVDSGGANLPSQDEVFPDRDH 162
Cdd:PLN02820  111 GEDLPSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDH 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 163 FGRIFYNQANMSAAGIPQIAVVMGSCTAGGAYVPAMSDEAIIVEKQGTIFLAGPPLVRAATGEVVSAEELGGADVHTRLS 242
Cdd:PLN02820  191 FGRIFYNQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVS 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 243 GVADHLARDDAHALALARRAVSAL----NHEKPWPVQRIDPE--PPLYDPEEIAGIVPADLKTPYDIREVIARLVDGSRF 316
Cdd:PLN02820  271 GVSDHFAQDELHALAIGRNIVKNLhlaaKQGMENTLGSKNPEykEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEF 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 317 DEFKARFGTTLVCGFAHVHGIPVGIVANNGVLFSESAVKGAHFVELCAQRRIPLVFLQNITGFMVGRKYETEGIAKHGAK 396
Cdd:PLN02820  351 DEFKKNYGTTLVTGFARIYGQPVGIIGNNGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAK 430
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 397 LVTAVATVKVPKITMLVGGSFGAGNYGMCGRAFSPRFLWTWPNSRISVMGGEQAAGVLSSVRGEALKRSGLPWSEEEEAR 476
Cdd:PLN02820  431 MVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENKKRQGIQWSKEEEEA 510
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1549660765 477 FRQPVLDLFERQSHPLYASARLWDDGVIDPRKSRDVLALSLSAALNAPIEDTHFGLFRM 535
Cdd:PLN02820  511 FKAKTVEAYEREANPYYSTARLWDDGVIDPADTRRVLGLCLSAALNRSPEDTKFGVFRM 569
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
34-533 0e+00

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 776.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765  34 RLAASGGGDKARERHVSRGKLLPRDRVAALIDPGTpFLELGATAAHEMYNGD--APAAGLITGIGRISGRECMIVCNDPT 111
Cdd:COG4799    14 EEALLGGGEKAIERQHARGKLTARERIDLLLDPGS-FLELGALAGHRMYDDDdrVPGDGVVTGIGTVDGRPVVVVANDFT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 112 VKGGTYYPMTVKKHLRAQEIAAENRLPCVYLVDSGGANLPSQDEVFpdrDHFGRIFYNQAnMSAAGIPQIAVVMGSCTAG 191
Cdd:COG4799    93 VKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESF---AGYGRIFYRNA-RSSGGIPQISVIMGPCAAG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 192 GAYVPAMSDEAIIVEKQGTIFLAGPPLVRAATGEVVSAEELGGADVHTRLSGVADHLARDDAHALALARRAVSALNHEKP 271
Cdd:COG4799   169 GAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLSYLPSNNL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 272 WPVQRIDPEPPLYDPEEIAGIVPADLKTPYDIREVIARLVDGSRFDEFKARFGTTLVCGFAHVHGIPVGIVANN-----G 346
Cdd:COG4799   249 EDPPRAEPAPPARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVANQpmvlaG 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 347 VLFSESAVKGAHFVELCAQRRIPLVFLQNITGFMVGRKYETEGIAKHGAKLVTAVATVKVPKITMLVGGSFGAGNYGMCG 426
Cdd:COG4799   329 VLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYGAGYYAMCG 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 427 RAFSPRFLWTWPNSRISVMGGEQAAGVLSSVRGEALkrsglpwseEEEARFRQPVLDLFERQSHPLYASARLWDDGVIDP 506
Cdd:COG4799   409 KALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAA---------EDPEALRAELIAEYEEQANPYYAAARGWIDDVIDP 479
                         490       500
                  ....*....|....*....|....*....
gi 1549660765 507 RKSRDVLALSLSAALNAPIE--DTHFGLF 533
Cdd:COG4799   480 RDTRRVLARALEAAANKPEErpPKKHGVI 508
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
47-526 4.93e-176

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: 505.26  E-value: 4.93e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765  47 RHVSRGKLLPRDRVAALIDPGTpFLELGATAAHEMYN---GDAPAAGLITGIGRISGRECMIVCNDPTVKGGTYYPMTVK 123
Cdd:pfam01039   1 PEHPRGKLTARERIDLLLDPGS-FGELEDLFFHRATEfgrKRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 124 KHLRAQEIAAENRLPCVYLVDSGGANlpsQDEVFPDRDHFGRIFYNQANMSAaGIPQIAVVMGSCTAGGAYVPAMSDEAI 203
Cdd:pfam01039  80 KILRAMEIAIKTGLPLIGINDSGGAR---IQEGVENLRGSGKIFGRNSLASG-VIPQISLIMGPCAGGGAYLPALGDFVI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 204 IVEKQGTIFLAGPPLVRAATGEVVSAEELGGADVHTRLSGVADHLARDDAHALALARRAVSAL---NHEKPWPVQRIDPE 280
Cdd:pfam01039 156 MVEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLpkpAPNNREPVPIVPTK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 281 PPLYDPEEIAGIVPADLKTPYDIREVIARLVDGSRFDEFKARFGTTLVCGFAHVHGIPVGIVANN-----GVLFSESAVK 355
Cdd:pfam01039 236 DPPDRDAPLVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQprvgaGVLFPDSADK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 356 GAHFVELCAQRRIPLVFLQNITGFMVGRKYETEGIAKHGAKLVTAVATVKVPKITMLVGGSFGAGNYGMCGRAFSPRFLW 435
Cdd:pfam01039 316 AARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINF 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 436 TWPNSRISVMGGEQAAGVLSSVRGEALKRSGlpwseEEEARFRQPVLDLFERQ-SHPLYASARLWDDGVIDPRKSRDVLA 514
Cdd:pfam01039 396 AWPTARIAVMGPEGAVEIKFRKEKAAAEMRG-----KDLAATRKQKIAEYEEElSPPYVAAARGFADAVIDPGRTRAKLV 470
                         490
                  ....*....|..
gi 1549660765 515 LSLSAALNAPIE 526
Cdd:pfam01039 471 IALAALWTKPRF 482
 
Name Accession Description Interval E-value
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
3-535 0e+00

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 851.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765   3 VLRSHISPSSEGFKANRSAMAEAIAAIEDAVRLAASGGGDKARERHVSRGKLLPRDRVAALIDPGTPFLELGATAAHEMY 82
Cdd:PLN02820   31 VLPDGVDRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHELY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765  83 NGDAPAAGLITGIGRISGRECMIVCNDPTVKGGTYYPMTVKKHLRAQEIAAENRLPCVYLVDSGGANLPSQDEVFPDRDH 162
Cdd:PLN02820  111 GEDLPSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDH 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 163 FGRIFYNQANMSAAGIPQIAVVMGSCTAGGAYVPAMSDEAIIVEKQGTIFLAGPPLVRAATGEVVSAEELGGADVHTRLS 242
Cdd:PLN02820  191 FGRIFYNQARMSSAGIPQIALVLGSCTAGGAYVPAMADESVIVKGNGTIFLAGPPLVKAATGEEVSAEDLGGADVHCKVS 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 243 GVADHLARDDAHALALARRAVSAL----NHEKPWPVQRIDPE--PPLYDPEEIAGIVPADLKTPYDIREVIARLVDGSRF 316
Cdd:PLN02820  271 GVSDHFAQDELHALAIGRNIVKNLhlaaKQGMENTLGSKNPEykEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEF 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 317 DEFKARFGTTLVCGFAHVHGIPVGIVANNGVLFSESAVKGAHFVELCAQRRIPLVFLQNITGFMVGRKYETEGIAKHGAK 396
Cdd:PLN02820  351 DEFKKNYGTTLVTGFARIYGQPVGIIGNNGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAK 430
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 397 LVTAVATVKVPKITMLVGGSFGAGNYGMCGRAFSPRFLWTWPNSRISVMGGEQAAGVLSSVRGEALKRSGLPWSEEEEAR 476
Cdd:PLN02820  431 MVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENKKRQGIQWSKEEEEA 510
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1549660765 477 FRQPVLDLFERQSHPLYASARLWDDGVIDPRKSRDVLALSLSAALNAPIEDTHFGLFRM 535
Cdd:PLN02820  511 FKAKTVEAYEREANPYYSTARLWDDGVIDPADTRRVLGLCLSAALNRSPEDTKFGVFRM 569
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
34-533 0e+00

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 776.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765  34 RLAASGGGDKARERHVSRGKLLPRDRVAALIDPGTpFLELGATAAHEMYNGD--APAAGLITGIGRISGRECMIVCNDPT 111
Cdd:COG4799    14 EEALLGGGEKAIERQHARGKLTARERIDLLLDPGS-FLELGALAGHRMYDDDdrVPGDGVVTGIGTVDGRPVVVVANDFT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 112 VKGGTYYPMTVKKHLRAQEIAAENRLPCVYLVDSGGANLPSQDEVFpdrDHFGRIFYNQAnMSAAGIPQIAVVMGSCTAG 191
Cdd:COG4799    93 VKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESF---AGYGRIFYRNA-RSSGGIPQISVIMGPCAAG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 192 GAYVPAMSDEAIIVEKQGTIFLAGPPLVRAATGEVVSAEELGGADVHTRLSGVADHLARDDAHALALARRAVSALNHEKP 271
Cdd:COG4799   169 GAYSPALSDFVIMVKGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLSYLPSNNL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 272 WPVQRIDPEPPLYDPEEIAGIVPADLKTPYDIREVIARLVDGSRFDEFKARFGTTLVCGFAHVHGIPVGIVANN-----G 346
Cdd:COG4799   249 EDPPRAEPAPPARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVANQpmvlaG 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 347 VLFSESAVKGAHFVELCAQRRIPLVFLQNITGFMVGRKYETEGIAKHGAKLVTAVATVKVPKITMLVGGSFGAGNYGMCG 426
Cdd:COG4799   329 VLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYGAGYYAMCG 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 427 RAFSPRFLWTWPNSRISVMGGEQAAGVLSSVRGEALkrsglpwseEEEARFRQPVLDLFERQSHPLYASARLWDDGVIDP 506
Cdd:COG4799   409 KALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAAA---------EDPEALRAELIAEYEEQANPYYAAARGWIDDVIDP 479
                         490       500
                  ....*....|....*....|....*....
gi 1549660765 507 RKSRDVLALSLSAALNAPIE--DTHFGLF 533
Cdd:COG4799   480 RDTRRVLARALEAAANKPEErpPKKHGVI 508
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
47-526 4.93e-176

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: 505.26  E-value: 4.93e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765  47 RHVSRGKLLPRDRVAALIDPGTpFLELGATAAHEMYN---GDAPAAGLITGIGRISGRECMIVCNDPTVKGGTYYPMTVK 123
Cdd:pfam01039   1 PEHPRGKLTARERIDLLLDPGS-FGELEDLFFHRATEfgrKRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 124 KHLRAQEIAAENRLPCVYLVDSGGANlpsQDEVFPDRDHFGRIFYNQANMSAaGIPQIAVVMGSCTAGGAYVPAMSDEAI 203
Cdd:pfam01039  80 KILRAMEIAIKTGLPLIGINDSGGAR---IQEGVENLRGSGKIFGRNSLASG-VIPQISLIMGPCAGGGAYLPALGDFVI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 204 IVEKQGTIFLAGPPLVRAATGEVVSAEELGGADVHTRLSGVADHLARDDAHALALARRAVSAL---NHEKPWPVQRIDPE 280
Cdd:pfam01039 156 MVEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLpkpAPNNREPVPIVPTK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 281 PPLYDPEEIAGIVPADLKTPYDIREVIARLVDGSRFDEFKARFGTTLVCGFAHVHGIPVGIVANN-----GVLFSESAVK 355
Cdd:pfam01039 236 DPPDRDAPLVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQprvgaGVLFPDSADK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 356 GAHFVELCAQRRIPLVFLQNITGFMVGRKYETEGIAKHGAKLVTAVATVKVPKITMLVGGSFGAGNYGMCGRAFSPRFLW 435
Cdd:pfam01039 316 AARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINF 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 436 TWPNSRISVMGGEQAAGVLSSVRGEALKRSGlpwseEEEARFRQPVLDLFERQ-SHPLYASARLWDDGVIDPRKSRDVLA 514
Cdd:pfam01039 396 AWPTARIAVMGPEGAVEIKFRKEKAAAEMRG-----KDLAATRKQKIAEYEEElSPPYVAAARGFADAVIDPGRTRAKLV 470
                         490
                  ....*....|..
gi 1549660765 515 LSLSAALNAPIE 526
Cdd:pfam01039 471 IALAALWTKPRF 482
AccD COG0777
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
53-148 8.71e-04

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: 41.20  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765  53 KLLPRDRVAALIDPGTpFLELGAtaahEMYNGDaP--------------AA--------GLITGIGRISGRECMIVCNDP 110
Cdd:COG0777    55 RISARERLELLLDEGS-FEELDA----DLVPVD-PlkfkdskkykdrlkEAqkktglkdAVVTGTGTINGIPVVVAVMDF 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1549660765 111 TVKGGTyypM-TV--KKHLRAQEIAAENRLPCVYLVDSGGA 148
Cdd:COG0777   129 SFMGGS---MgSVvgEKITRAIERAIEKKLPLIIFSASGGA 166
PRK07189 PRK07189
malonate decarboxylase subunit beta; Reviewed
57-252 2.08e-03

malonate decarboxylase subunit beta; Reviewed


Pssm-ID: 235954  Cd Length: 301  Bit Score: 40.27  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765  57 RDRVAALIDPGTpFLEL-----GATAAHEMYNGDAPAA--GLITGIGRISGRECMIVCNDPTVKGGTYYPMTVKKHLRAQ 129
Cdd:PRK07189   18 RERAAALLDAGS-FRELlgpfeRVMSPHLPLQGIPPQFddGVVVGKGTLDGRPVVVAAQEGRFMGGSVGEVHGAKLAGAL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549660765 130 EIAAENRL-----PCVYLVDSGGANLpsqdevfpdrdhfgrifyNQAN---------MSA-----AGIPQIAVVMGS--C 188
Cdd:PRK07189   97 ELAAEDNRngiptAVLLLFETGGVRL------------------QEANaglaaiaeiMRAivdlrAAVPVIGLIGGRvgC 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1549660765 189 TAGGAYVPAMSDeAIIVEKQGTIFLAGPPLVRAATGevvsAEEL------------GGAdvHTRLSGVADHLARDD 252
Cdd:PRK07189  159 FGGMGIAAALCS-YLIVSEEGRLGLSGPEVIEQEAG----VEEFdsrdralvwrttGGK--HRYLSGLADALVDDD 227
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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