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Conserved domains on  [gi|1387845397|ref|NP_001350076|]
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methylcrotonoyl-CoA carboxylase beta chain, mitochondrial isoform 2 precursor [Homo sapiens]

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 ...
36-525 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: 799.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397  36 DLGSALYQENYKQMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDnEEVP 115
Cdd:PLN02820   37 DRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHELYG-EDLP 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 116 GGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTF 195
Cdd:PLN02820  116 SGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIF 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 196 YNQAIMSSKNIAQ--------------------------------------VKAATGEEVSAEDLGGADLHCRKSGVSDH 237
Cdd:PLN02820  196 YNQARMSSAGIPQialvlgsctaggayvpamadesvivkgngtiflagpplVKAATGEEVSAEDLGGADVHCKVSGVSDH 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 238 WALDDHHALHLTRKVVRNL------NYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKA 311
Cdd:PLN02820  276 FAQDELHALAIGRNIVKNLhlaakqGMENTLGSKNPEYKEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEFDEFKK 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 312 FYGDTLVTGFARIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAV 391
Cdd:PLN02820  356 NYGTTLVTGFARIYGQPVGIIGNNGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMVMAV 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 392 ACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAANVLATITKDQRAREGKQFSSADEAALKEPI 471
Cdd:PLN02820  436 ACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENKKRQGIQWSKEEEEAFKAKT 515
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1387845397 472 IKKFEEEGNPYYSSARVWDDGIIDPADTRLVLGLSFSAALNAPIEKTDFGIFRM 525
Cdd:PLN02820  516 VEAYEREANPYYSTARLWDDGVIDPADTRRVLGLCLSAALNRSPEDTKFGVFRM 569
 
Name Accession Description Interval E-value
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
36-525 0e+00

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 799.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397  36 DLGSALYQENYKQMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDnEEVP 115
Cdd:PLN02820   37 DRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHELYG-EDLP 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 116 GGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTF 195
Cdd:PLN02820  116 SGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIF 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 196 YNQAIMSSKNIAQ--------------------------------------VKAATGEEVSAEDLGGADLHCRKSGVSDH 237
Cdd:PLN02820  196 YNQARMSSAGIPQialvlgsctaggayvpamadesvivkgngtiflagpplVKAATGEEVSAEDLGGADVHCKVSGVSDH 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 238 WALDDHHALHLTRKVVRNL------NYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKA 311
Cdd:PLN02820  276 FAQDELHALAIGRNIVKNLhlaakqGMENTLGSKNPEYKEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEFDEFKK 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 312 FYGDTLVTGFARIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAV 391
Cdd:PLN02820  356 NYGTTLVTGFARIYGQPVGIIGNNGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMVMAV 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 392 ACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAANVLATITKDQRAREGKQFSSADEAALKEPI 471
Cdd:PLN02820  436 ACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENKKRQGIQWSKEEEEAFKAKT 515
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1387845397 472 IKKFEEEGNPYYSSARVWDDGIIDPADTRLVLGLSFSAALNAPIEKTDFGIFRM 525
Cdd:PLN02820  516 VEAYEREANPYYSTARLWDDGVIDPADTRRVLGLCLSAALNRSPEDTKFGVFRM 569
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
48-523 0e+00

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 671.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397  48 QMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSpFLELSQFAGYQLYD-NEEVPGGGIITGIGRV 126
Cdd:COG4799     1 AMRALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGS-FLELGALAGHRMYDdDDRVPGDGVVTGIGTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 127 SGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFpdrDHFGRTFYNQAiMSSKNI 206
Cdd:COG4799    80 DGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESF---AGYGRIFYRNA-RSSGGI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 207 AQ--------------------------------------VKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHL 248
Cdd:COG4799   156 PQisvimgpcaaggayspalsdfvimvkgtsqmflggppvVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALAL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 249 TRKVVRNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFARIFGYP 328
Cdd:COG4799   236 ARRLLSYLPSNNLEDPPRAEPAPPARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRP 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 329 VGIVGNN-----GVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAVACAQVPKITLII 403
Cdd:COG4799   316 VGIVANQpmvlaGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVIL 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 404 GGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAANVLATITKDQraregkqfsSADEAALKEPIIKKFEEEGNPYY 483
Cdd:COG4799   396 RKAYGAGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAA---------AEDPEALRAELIAEYEEQANPYY 466
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1387845397 484 SSARVWDDGIIDPADTRLVLGLSFSAALNAPIEKTD--FGIF 523
Cdd:COG4799   467 AAARGWIDDVIDPRDTRRVLARALEAAANKPEERPPkkHGVI 508
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
77-516 3.49e-152

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: 444.01  E-value: 3.49e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397  77 SRGKLLPRERIDNLIDPGSpFLELSQFAGYQLYDN--EEVPGGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQL 154
Cdd:pfam01039   4 PRGKLTARERIDLLLDPGS-FGELEDLFFHRATEFgrKRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEKIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 155 RAQEIAMQNRLPCIYLVDSGGAylpRQADVFPDRDHFGRTFYNQAIMSS-----------------------------KN 205
Cdd:pfam01039  83 RAMEIAIKTGLPLIGINDSGGA---RIQEGVENLRGSGKIFGRNSLASGvipqislimgpcagggaylpalgdfvimvEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 206 IAQ--------VKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKK---LDVTIEPSEEPLF 274
Cdd:pfam01039 160 TSPmfltgppvIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAPnnrEPVPIVPTKDPPD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 275 PADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFARIFGYPVGIVGNN-----GVLFSESAKKGTHF 349
Cdd:pfam01039 240 RDAPLVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQprvgaGVLFPDSADKAARF 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 350 VQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPN 429
Cdd:pfam01039 320 IRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAWPT 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 430 ARISVMGGEQAANVLATITKDQRAREGKqfssaDEAALKEPIIKKFEEE-GNPYYSSARVWDDGIIDPADTRLVLGLSFS 508
Cdd:pfam01039 400 ARIAVMGPEGAVEIKFRKEKAAAEMRGK-----DLAATRKQKIAEYEEElSPPYVAAARGFADAVIDPGRTRAKLVIALA 474

                  ....*...
gi 1387845397 509 AALNAPIE 516
Cdd:pfam01039 475 ALWTKPRF 482
 
Name Accession Description Interval E-value
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
36-525 0e+00

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 799.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397  36 DLGSALYQENYKQMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDnEEVP 115
Cdd:PLN02820   37 DRNSDAFSANSKAMEGLLSELRSHVAKVRAGGGPEAVKRHRSRNKLLPRERIDRLLDPGSPFLELSQLAGHELYG-EDLP 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 116 GGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFPDRDHFGRTF 195
Cdd:PLN02820  116 SGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEVFPDRDHFGRIF 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 196 YNQAIMSSKNIAQ--------------------------------------VKAATGEEVSAEDLGGADLHCRKSGVSDH 237
Cdd:PLN02820  196 YNQARMSSAGIPQialvlgsctaggayvpamadesvivkgngtiflagpplVKAATGEEVSAEDLGGADVHCKVSGVSDH 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 238 WALDDHHALHLTRKVVRNL------NYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKA 311
Cdd:PLN02820  276 FAQDELHALAIGRNIVKNLhlaakqGMENTLGSKNPEYKEPLYDVKELRGIVPADHKQSFDVRSVIARIVDGSEFDEFKK 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 312 FYGDTLVTGFARIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAV 391
Cdd:PLN02820  356 NYGTTLVTGFARIYGQPVGIIGNNGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMVMAV 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 392 ACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAANVLATITKDQRAREGKQFSSADEAALKEPI 471
Cdd:PLN02820  436 ACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAQIERENKKRQGIQWSKEEEEAFKAKT 515
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1387845397 472 IKKFEEEGNPYYSSARVWDDGIIDPADTRLVLGLSFSAALNAPIEKTDFGIFRM 525
Cdd:PLN02820  516 VEAYEREANPYYSTARLWDDGVIDPADTRRVLGLCLSAALNRSPEDTKFGVFRM 569
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
48-523 0e+00

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 671.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397  48 QMKALVNQLHERVEHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSpFLELSQFAGYQLYD-NEEVPGGGIITGIGRV 126
Cdd:COG4799     1 AMRALLAELRARREEALLGGGEKAIERQHARGKLTARERIDLLLDPGS-FLELGALAGHRMYDdDDRVPGDGVVTGIGTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 127 SGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPRQADVFpdrDHFGRTFYNQAiMSSKNI 206
Cdd:COG4799    80 DGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESF---AGYGRIFYRNA-RSSGGI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 207 AQ--------------------------------------VKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHL 248
Cdd:COG4799   156 PQisvimgpcaaggayspalsdfvimvkgtsqmflggppvVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALAL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 249 TRKVVRNLNYQKKLDVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFARIFGYP 328
Cdd:COG4799   236 ARRLLSYLPSNNLEDPPRAEPAPPARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRP 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 329 VGIVGNN-----GVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAVACAQVPKITLII 403
Cdd:COG4799   316 VGIVANQpmvlaGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVIL 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 404 GGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAANVLATITKDQraregkqfsSADEAALKEPIIKKFEEEGNPYY 483
Cdd:COG4799   396 RKAYGAGYYAMCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRRELAA---------AEDPEALRAELIAEYEEQANPYY 466
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1387845397 484 SSARVWDDGIIDPADTRLVLGLSFSAALNAPIEKTD--FGIF 523
Cdd:COG4799   467 AAARGWIDDVIDPRDTRRVLARALEAAANKPEERPPkkHGVI 508
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
77-516 3.49e-152

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: 444.01  E-value: 3.49e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397  77 SRGKLLPRERIDNLIDPGSpFLELSQFAGYQLYDN--EEVPGGGIITGIGRVSGVECMIIANDATVKGGAYYPVTVKKQL 154
Cdd:pfam01039   4 PRGKLTARERIDLLLDPGS-FGELEDLFFHRATEFgrKRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEKIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 155 RAQEIAMQNRLPCIYLVDSGGAylpRQADVFPDRDHFGRTFYNQAIMSS-----------------------------KN 205
Cdd:pfam01039  83 RAMEIAIKTGLPLIGINDSGGA---RIQEGVENLRGSGKIFGRNSLASGvipqislimgpcagggaylpalgdfvimvEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 206 IAQ--------VKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKK---LDVTIEPSEEPLF 274
Cdd:pfam01039 160 TSPmfltgppvIKKVTGEEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAPnnrEPVPIVPTKDPPD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 275 PADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFARIFGYPVGIVGNN-----GVLFSESAKKGTHF 349
Cdd:pfam01039 240 RDAPLVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGYAKTVVTGFARLGGIPVGVVANQprvgaGVLFPDSADKAARF 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 350 VQLCCQRNIPLLFLQNITGFMVGREYEAEGIAKDGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPN 429
Cdd:pfam01039 320 IRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAWPT 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387845397 430 ARISVMGGEQAANVLATITKDQRAREGKqfssaDEAALKEPIIKKFEEE-GNPYYSSARVWDDGIIDPADTRLVLGLSFS 508
Cdd:pfam01039 400 ARIAVMGPEGAVEIKFRKEKAAAEMRGK-----DLAATRKQKIAEYEEElSPPYVAAARGFADAVIDPGRTRAKLVIALA 474

                  ....*...
gi 1387845397 509 AALNAPIE 516
Cdd:pfam01039 475 ALWTKPRF 482
 
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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