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Conserved domains on  [gi|1907199588|ref|XP_036011089|]
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propionyl-CoA carboxylase beta chain, mitochondrial isoform X2 [Mus musculus]

Protein Classification

acyl-CoA carboxylase subunit beta( domain architecture ID 11469175)

acyl-CoA carboxylase subunit beta, such as propionyl-CoA carboxylase subunit beta, which is the catalytic carboxyltransferase subunit of the enzyme that catalyzes the carboxylation of propionyl-CoA to form methylmalonyl-CoA

CATH:  3.90.226.10
Gene Ontology:  GO:0016874|GO:0006633|GO:0009317|GO:0003989
PubMed:  8102604
SCOP:  4000456

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
39-462 0e+00

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


:

Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 632.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  39 ERIDNKRHAALLGGGQRRIDAQHKR-----------------------------------FPGDSVVTGRGRINGRLVYV 83
Cdd:COG4799     7 AELRARREEALLGGGEKAIERQHARgkltareridllldpgsflelgalaghrmyddddrVPGDGVVTGIGTVDGRPVVV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  84 FSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFL-------------------- 143
Cdd:COG4799    87 VANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYrnarssggipqisvimgpca 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 144 -----------------DTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHRAFDNDVDALCNLREFFNFLPLS 206
Cdd:COG4799   167 aggayspalsdfvimvkGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLSYLPSN 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 207 SQDPAPIRECHDPsDRLVPELDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSYAKNIVVGFARMNGRTVGIVGNQPNV 286
Cdd:COG4799   247 NLEDPPRAEPAPP-ARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVANQPMV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 287 ASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDV 366
Cdd:COG4799   326 LAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYGAGYYA 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 367 MSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIFK----GHQDVEAAQAEYVEKF---ANPFPAAVRGFVDDIIQPSSTRAR 439
Cdd:COG4799   406 MCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRrelaAAEDPEALRAELIAEYeeqANPYYAAARGWIDDVIDPRDTRRV 485

                         490       500
                  ....*....|....*....|...
gi 1907199588 440 ICCDLEVLASKKVHRPWRKHANI 462
Cdd:COG4799   486 LARALEAAANKPEERPPKKHGVI 508
 
Name Accession Description Interval E-value
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
39-462 0e+00

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 632.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  39 ERIDNKRHAALLGGGQRRIDAQHKR-----------------------------------FPGDSVVTGRGRINGRLVYV 83
Cdd:COG4799     7 AELRARREEALLGGGEKAIERQHARgkltareridllldpgsflelgalaghrmyddddrVPGDGVVTGIGTVDGRPVVV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  84 FSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFL-------------------- 143
Cdd:COG4799    87 VANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYrnarssggipqisvimgpca 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 144 -----------------DTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHRAFDNDVDALCNLREFFNFLPLS 206
Cdd:COG4799   167 aggayspalsdfvimvkGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLSYLPSN 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 207 SQDPAPIRECHDPsDRLVPELDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSYAKNIVVGFARMNGRTVGIVGNQPNV 286
Cdd:COG4799   247 NLEDPPRAEPAPP-ARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVANQPMV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 287 ASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDV 366
Cdd:COG4799   326 LAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYGAGYYA 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 367 MSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIFK----GHQDVEAAQAEYVEKF---ANPFPAAVRGFVDDIIQPSSTRAR 439
Cdd:COG4799   406 MCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRrelaAAEDPEALRAELIAEYeeqANPYYAAARGWIDDVIDPRDTRRV 485

                         490       500
                  ....*....|....*....|...
gi 1907199588 440 ICCDLEVLASKKVHRPWRKHANI 462
Cdd:COG4799   486 LARALEAAANKPEERPPKKHGVI 508
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 62-462 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: 566.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  62 KRFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADI 141
Cdd:pfam01039  40 KRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEKILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 142 F-------------------------------------LDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHR 184
Cdd:pfam01039 120 FgrnslasgvipqislimgpcagggaylpalgdfvimvEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 185 AFDNDVDALCNLREFFNFLPL---SSQDPAPIRECHDPSDRLVPeLDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSY 261
Cdd:pfam01039 200 TALDDEDALELIRKWLSYLPKpapNNREPVPIVPTKDPPDRDAP-LVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGY 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 262 AKNIVVGFARMNGRTVGIVGNQPNVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLL 341
Cdd:pfam01039 279 AKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLL 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 342 YAFAEATVPKITVITRKAYGGAYDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIF--------KGHQDVEAA----QA 409
Cdd:pfam01039 359 YALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAWPTARIAVMGPEGAVEIKFrkekaaaeMRGKDLAATrkqkIA 438

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907199588 410 EYVEKFANPFPAAVRGFVDDIIQPSSTRARICCDLEVLASKKVHRPWRKHANI 462
Cdd:pfam01039 439 EYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPRFFPWRKHGNI 491
mmdA TIGR01117
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA ...
 39-464 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: 536.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  39 ERIDNKRHAALLGGGQRRIDAQH--------------------------------------KRFPGDSVVTGRGRINGRL 80
Cdd:TIGR01117   4 EELHEKKEKIKQGGGEKRIEKQHaqgkmtarerlallfdpgsfveidqfvkhrctnfgmdkKELPAEGVVTGYGTIDGRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  81 VYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFL----------------- 143
Cdd:TIGR01117  84 VYAFAQDFTVMGGSLGEMHAAKIVKIMDLAMKMGAPVVGLNDSGGARIQEAVDALKGYGDIFYrntiasgvvpqisaimg 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 144 --------------------DTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHRAFDNDVDALCNLREFFNFL 203
Cdd:TIGR01117 164 pcaggavyspaltdfiymvdNTSQMFITGPQVIKTVTGEEVTAEQLGGAMAHNSVSGVAHFIAEDDDDCIMLIRRLLSFL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 204 PLSSQDPAPIRECHDPSDRLVPELDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSYAKNIVVGFARMNGRTVGIVGNQ 283
Cdd:TIGR01117 244 PSNNMEKAPLVKTGDDPTRETPELYDLLPDNPNKPYDMRDVITAIVDNGDYLEVQPYYAPNIITCFARINGQSVGIIANQ 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 284 PNVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGA 363
Cdd:TIGR01117 324 PKVMAGCLDIDSSDKIARFIRFCDAFNIPIVTFVDVPGFLPGVNQEYGGIIRHGAKVLYAYSEATVPKVTIITRKAYGGA 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 364 YDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIFKghQDVEAAQ----------AEYVEKFANPFPAAVRGFVDDIIQP 433
Cdd:TIGR01117 404 YLAMCSKHLGADQVYAWPTAEIAVMGPAGAANIIFR--KDIKEAKdpaatrkqkiAEYREEFANPYKAAARGYVDDVIEP 481

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1907199588 434 SSTRARICCDLEVLASKKVHRPWRKHANIPL 464
Cdd:TIGR01117 482 KQTRPKIVNALAMLESKREKLPPKKHGNIPL 512
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 65-437 7.92e-56

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 194.64  E-value: 7.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  65 PGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGA----------------RI 128
Cdd:PLN02820  115 PSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGAnlprqaevfpdrdhfgRI 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 129 --QEGVESLAGYADIFL----------------DTSYL-------FITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAH 183
Cdd:PLN02820  195 fyNQARMSSAGIPQIALvlgsctaggayvpamaDESVIvkgngtiFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 184 RAFDNDVDALCNLREFFNFLPLSSQDP------APIRECHDPsdrLVP--ELDTVVPLESSKAYNMLDIIHAVIDEREFF 255
Cdd:PLN02820  275 HFAQDELHALAIGRNIVKNLHLAAKQGmentlgSKNPEYKEP---LYDvkELRGIVPADHKQSFDVRSVIARIVDGSEFD 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 256 EIMPSYAKNIVVGFARMNGRTVGIVGNqpnvaSGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIR 335
Cdd:PLN02820  352 EFKKNYGTTLVTGFARIYGQPVGIIGN-----NGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAK 426

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 336 HGAKLLYAFAEATVPKITVITRKAYGGAYDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIF---------KGHQ---- 402
Cdd:PLN02820  427 AGAKMVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAqierenkkrQGIQwske 506

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1907199588 403 DVEAAQAEYVEKF---ANPFPAAVRGFVDDIIQPSSTR 437
Cdd:PLN02820  507 EEEAFKAKTVEAYereANPYYSTARLWDDGVIDPADTR 544
 
Name Accession Description Interval E-value
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
39-462 0e+00

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 632.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  39 ERIDNKRHAALLGGGQRRIDAQHKR-----------------------------------FPGDSVVTGRGRINGRLVYV 83
Cdd:COG4799     7 AELRARREEALLGGGEKAIERQHARgkltareridllldpgsflelgalaghrmyddddrVPGDGVVTGIGTVDGRPVVV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  84 FSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFL-------------------- 143
Cdd:COG4799    87 VANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGARLQEGVESFAGYGRIFYrnarssggipqisvimgpca 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 144 -----------------DTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHRAFDNDVDALCNLREFFNFLPLS 206
Cdd:COG4799   167 aggayspalsdfvimvkGTSQMFLGGPPVVKAATGEEVTAEELGGADVHARVSGVADYLAEDEEEALALARRLLSYLPSN 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 207 SQDPAPIRECHDPsDRLVPELDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSYAKNIVVGFARMNGRTVGIVGNQPNV 286
Cdd:COG4799   247 NLEDPPRAEPAPP-ARDPEELYGIVPEDPRKPYDMREVIARLVDGGSFFEFKPLYGPNIVTGFARIDGRPVGIVANQPMV 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 287 ASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDV 366
Cdd:COG4799   326 LAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILRKAYGAGYYA 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 367 MSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIFK----GHQDVEAAQAEYVEKF---ANPFPAAVRGFVDDIIQPSSTRAR 439
Cdd:COG4799   406 MCGKALGPDFLFAWPTAEIAVMGGEGAANVLYRrelaAAEDPEALRAELIAEYeeqANPYYAAARGWIDDVIDPRDTRRV 485

                         490       500
                  ....*....|....*....|...
gi 1907199588 440 ICCDLEVLASKKVHRPWRKHANI 462
Cdd:COG4799   486 LARALEAAANKPEERPPKKHGVI 508
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 62-462 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: 566.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  62 KRFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADI 141
Cdd:pfam01039  40 KRIPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGEKILRAMEIAIKTGLPLIGINDSGGARIQEGVENLRGSGKI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 142 F-------------------------------------LDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHR 184
Cdd:pfam01039 120 FgrnslasgvipqislimgpcagggaylpalgdfvimvEGTSPMFLTGPPVIKKVTGEEVTSEELGGATQHMTISGVSHL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 185 AFDNDVDALCNLREFFNFLPL---SSQDPAPIRECHDPSDRLVPeLDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSY 261
Cdd:pfam01039 200 TALDDEDALELIRKWLSYLPKpapNNREPVPIVPTKDPPDRDAP-LVSIVPDDPKKPYDVREVIAGIVDEGEFFEIKPGY 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 262 AKNIVVGFARMNGRTVGIVGNQPNVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLL 341
Cdd:pfam01039 279 AKTVVTGFARLGGIPVGVVANQPRVGAGVLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLL 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 342 YAFAEATVPKITVITRKAYGGAYDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIF--------KGHQDVEAA----QA 409
Cdd:pfam01039 359 YALAEATVPKITVIPRKAYGGAYVVMDSKINGADINFAWPTARIAVMGPEGAVEIKFrkekaaaeMRGKDLAATrkqkIA 438

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907199588 410 EYVEKFANPFPAAVRGFVDDIIQPSSTRARICCDLEVLASKKVHRPWRKHANI 462
Cdd:pfam01039 439 EYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPRFFPWRKHGNI 491
mmdA TIGR01117
methylmalonyl-CoA decarboxylase alpha subunit; This model describes methymalonyl-CoA ...
 39-464 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: 536.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  39 ERIDNKRHAALLGGGQRRIDAQH--------------------------------------KRFPGDSVVTGRGRINGRL 80
Cdd:TIGR01117   4 EELHEKKEKIKQGGGEKRIEKQHaqgkmtarerlallfdpgsfveidqfvkhrctnfgmdkKELPAEGVVTGYGTIDGRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  81 VYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFL----------------- 143
Cdd:TIGR01117  84 VYAFAQDFTVMGGSLGEMHAAKIVKIMDLAMKMGAPVVGLNDSGGARIQEAVDALKGYGDIFYrntiasgvvpqisaimg 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 144 --------------------DTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHRAFDNDVDALCNLREFFNFL 203
Cdd:TIGR01117 164 pcaggavyspaltdfiymvdNTSQMFITGPQVIKTVTGEEVTAEQLGGAMAHNSVSGVAHFIAEDDDDCIMLIRRLLSFL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 204 PLSSQDPAPIRECHDPSDRLVPELDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSYAKNIVVGFARMNGRTVGIVGNQ 283
Cdd:TIGR01117 244 PSNNMEKAPLVKTGDDPTRETPELYDLLPDNPNKPYDMRDVITAIVDNGDYLEVQPYYAPNIITCFARINGQSVGIIANQ 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 284 PNVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGA 363
Cdd:TIGR01117 324 PKVMAGCLDIDSSDKIARFIRFCDAFNIPIVTFVDVPGFLPGVNQEYGGIIRHGAKVLYAYSEATVPKVTIITRKAYGGA 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 364 YDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIFKghQDVEAAQ----------AEYVEKFANPFPAAVRGFVDDIIQP 433
Cdd:TIGR01117 404 YLAMCSKHLGADQVYAWPTAEIAVMGPAGAANIIFR--KDIKEAKdpaatrkqkiAEYREEFANPYKAAARGYVDDVIEP 481

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1907199588 434 SSTRARICCDLEVLASKKVHRPWRKHANIPL 464
Cdd:TIGR01117 482 KQTRPKIVNALAMLESKREKLPPKKHGNIPL 512
PLN02820 PLN02820
3-methylcrotonyl-CoA carboxylase, beta chain
 65-437 7.92e-56

3-methylcrotonyl-CoA carboxylase, beta chain


Pssm-ID: 178415 [Multi-domain]  Cd Length: 569  Bit Score: 194.64  E-value: 7.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  65 PGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGA----------------RI 128
Cdd:PLN02820  115 PSGGIVTGIGPVHGRLCMFVANDPTVKGGTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGAnlprqaevfpdrdhfgRI 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 129 --QEGVESLAGYADIFL----------------DTSYL-------FITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAH 183
Cdd:PLN02820  195 fyNQARMSSAGIPQIALvlgsctaggayvpamaDESVIvkgngtiFLAGPPLVKAATGEEVSAEDLGGADVHCKVSGVSD 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 184 RAFDNDVDALCNLREFFNFLPLSSQDP------APIRECHDPsdrLVP--ELDTVVPLESSKAYNMLDIIHAVIDEREFF 255
Cdd:PLN02820  275 HFAQDELHALAIGRNIVKNLHLAAKQGmentlgSKNPEYKEP---LYDvkELRGIVPADHKQSFDVRSVIARIVDGSEFD 351

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 256 EIMPSYAKNIVVGFARMNGRTVGIVGNqpnvaSGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIR 335
Cdd:PLN02820  352 EFKKNYGTTLVTGFARIYGQPVGIIGN-----NGILFTESALKGAHFIELCAQRGIPLLFLQNITGFMVGSRSEASGIAK 426

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 336 HGAKLLYAFAEATVPKITVITRKAYGGAYDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIF---------KGHQ---- 402
Cdd:PLN02820  427 AGAKMVMAVACAKVPKITIIVGGSFGAGNYGMCGRAYSPNFLFMWPNARIGVMGGAQAAGVLAqierenkkrQGIQwske 506

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1907199588 403 DVEAAQAEYVEKF---ANPFPAAVRGFVDDIIQPSSTR 437
Cdd:PLN02820  507 EEEAFKAKTVEAYereANPYYSTARLWDDGVIDPADTR 544
AccD COG0777
Acetyl-CoA carboxylase beta subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 67-135 7.04e-13

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: 68.55  E-value: 7.04e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907199588  67 DSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESL 135
Cdd:COG0777   107 DAVVTGTGTINGIPVVVAVMDFSFMGGSMGSVVGEKITRAIERAIEKKLPLIIFSASGGARMQEGILSL 175
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 242-363 1.42e-08

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 56.30  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 242 LDIIHAVIDEreFFEIMP--SYA--KNIVVGFARMNGRTVGIVGNQpnvaSGClDINSSV-------------KGARFVR 304
Cdd:PRK05724   73 LDYIELLFTD--FTELHGdrAFAddKAIVGGLARLNGRPVMVIGHQ----KGR-DTKEKIrrnfgmprpegyrKALRLMK 145

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907199588 305 FCDAFNIPLITFVDVPGFLPG-TAQEYG---GIirhgAKLLYAFAEATVPKI-TVITRKAYGGA 363
Cdd:PRK05724  146 MAEKFGLPIITFIDTPGAYPGiGAEERGqseAI----ARNLREMARLKVPIIcTVIGEGGSGGA 205
accD CHL00174
acetyl-CoA carboxylase beta subunit; Reviewed
 67-141 2.32e-07

acetyl-CoA carboxylase beta subunit; Reviewed


Pssm-ID: 214384 [Multi-domain]  Cd Length: 296  Bit Score: 52.21  E-value: 2.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907199588  67 DSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADI 141
Cdd:CHL00174  121 DAVQTGIGQLNGIPVALGVMDFQFMGGSMGSVVGEKITRLIEYATNESLPLIIVCASGGARMQEGSLSLMQMAKI 195
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 242-356 1.01e-06

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: 50.42  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 242 LDIIHAVIDEreFFEIM--PSYA--KNIVVGFARMNGRTVGIVGNQpnvasgcldinssvKGA----------------- 300
Cdd:COG0825    70 LDYIEAIFTD--FIELHgdRAFGddPAIVGGLARFDGRPVMVIGHQ--------------KGRdtkerikrnfgmphpeg 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907199588 301 -----RFVRFCDAFNIPLITFVDVPGFLPG-TAQEYG---GIirhgAKLLYAFAEATVPKITVIT 356
Cdd:COG0825   134 yrkalRLMKLAEKFGLPIITFIDTPGAYPGiGAEERGqseAI----ARNLREMARLKVPIISVVI 194
PRK07189 PRK07189
malonate decarboxylase subunit beta; Reviewed
 67-141 1.37e-06

malonate decarboxylase subunit beta; Reviewed


Pssm-ID: 235954  Cd Length: 301  Bit Score: 49.90  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588  67 DSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVG-----APVIGLNDSGGARIQEGVESLAGYADI 141
Cdd:PRK07189   56 DGVVVGKGTLDGRPVVVAAQEGRFMGGSVGEVHGAKLAGALELAAEDNrngipTAVLLLFETGGVRLQEANAGLAAIAEI 135
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 265-363 3.44e-04

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 43.01  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 265 IVVGFARMNGRTVGIVGNQPNVAS--------GCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPG-TAQEYGgiir 335
Cdd:PLN03230  168 IVCGIGSMEGMSFMFIGHQKGRNTkeniyrnfAMPQPNGYRKALRFMRHAEKFGFPILTFVDTPGAYAGiKAEELG---- 243

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907199588 336 HGAKLLYAFAEA---TVPKI-TVITRKAYGGA 363
Cdd:PLN03230  244 QGEAIAFNLREMfglRVPIIaTVIGEGGSGGA 275
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 265-363 4.85e-04

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 42.11  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 265 IVVGFARMNGRTVGIVGNQ------PNVAS--GCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRH 336
Cdd:CHL00198  101 LVGGIGKINGRTIVFLGHQrgrntkENVLRnfGMPSPGGYRKALRLMKHANKFGLPILTFIDTPGAWAGVKAEKLGQGEA 180

                          90       100
                  ....*....|....*....|....*...
gi 1907199588 337 GAKLLYAFAEATVPKI-TVITRKAYGGA 363
Cdd:CHL00198  181 IAVNLREMFSFEVPIIcTIIGEGGSGGA 208
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 265-408 6.62e-03

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 38.22  E-value: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907199588 265 IVVGFARMNGRTVGIVGNQP------NVAS--GCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRH 336
Cdd:PRK12319   45 VVGGIGYLAGQPVTVVGIQKgknlqdNLKRnfGQPHPEGYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEA 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907199588 337 GAKLLYAFAEATVPKITVITRKAYGG---AYDVMSSKHLLGDTNYawptaeiAVMGAKGAVEIIFK-GHQDVEAAQ 408
Cdd:PRK12319  125 IARNLMEMSDLKVPIIAIIIGEGGSGgalALAVADQVWMLENTMY-------AVLSPEGFASILWKdGSRATEAAE 193
 
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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