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Conserved domains on  [gi|1207996448|ref|NP_001339541|]
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propionyl-CoA carboxylase alpha chain, mitochondrial isoform k [Homo sapiens]

Protein Classification

biotin carboxylase domain-containing protein( domain architecture ID 1903193)

biotin carboxylase domain-containing protein similar to Blastocladiella emersonii acetyl-coenzyme-A carboxylase converts acetyl-CoA to malonyl-CoA, which is converted to malonyl-acyl carrier protein (ACP), the building block of the fatty acid moieties of bacterial membrane lipids

PubMed:  31023230

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PccA super family cl44129
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-149 2.05e-68

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG4770:

Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 222.20  E-value: 2.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:COG4770   255 MGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQvehpvtemvtgidlveeqiriaageplpftqediklrgha 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 112
Cdd:COG4770   335 iecrinaeDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVI 412

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207996448 113 RGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 149
Cdd:COG4770   413 EGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
PCC_BT pfam18140
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ...
 162-290 1.07e-37

Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.


:

Pssm-ID: 465666 [Multi-domain]  Cd Length: 126  Bit Score: 131.60  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448 162 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 241
Cdd:pfam18140   1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207996448 242 VSVDGTQRTVQClSREAGGnMSIQFLGTVYKVNILTRLAAELNKFMLEK 290
Cdd:pfam18140  80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 298-364 2.02e-29

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


:

Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 107.89  E-value: 2.02e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207996448 298 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-149 2.05e-68

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 222.20  E-value: 2.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:COG4770   255 MGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQvehpvtemvtgidlveeqiriaageplpftqediklrgha 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 112
Cdd:COG4770   335 iecrinaeDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVI 412

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207996448 113 RGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 149
Cdd:COG4770   413 EGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-141 6.38e-46

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 162.66  E-value: 6.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:PRK08591  255 IGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQvehpvtemitgvdlvkeqiriaageplsikqedivfrgha 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQYqeplHLP---GVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDN 109
Cdd:PRK08591  335 iecrinaeDPAKNF-MPSPGKITRY----HPPggpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIARMKRALSE 409

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207996448 110 YVIRGVTHNIALLREVIINSRFVKGDISTKFL 141
Cdd:PRK08591  410 FVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 41-141 1.09e-44

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 214878 [Multi-domain]  Cd Length: 107  Bit Score: 149.10  E-value: 1.09e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   41 DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIA 120
Cdd:smart00878   8 DPANGF-LPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGVKTNIP 85

                           90       100
                   ....*....|....*....|.
gi 1207996448  121 LLREVIINSRFVKGDISTKFL 141
Cdd:smart00878  86 FLRALLRHPDFRAGDVDTGFL 106
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 41-143 2.53e-44

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 426981 [Multi-domain]  Cd Length: 108  Bit Score: 148.41  E-value: 2.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 DPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIA 120
Cdd:pfam02785   8 DPDNNF-LPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGVKTNIP 85

                          90       100
                  ....*....|....*....|...
gi 1207996448 121 LLREVIINSRFVKGDISTKFLSD 143
Cdd:pfam02785  86 FLRAILEHPDFRAGEVDTGFLEE 108
PCC_BT pfam18140
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ...
 162-290 1.07e-37

Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.


Pssm-ID: 465666 [Multi-domain]  Cd Length: 126  Bit Score: 131.60  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448 162 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 241
Cdd:pfam18140   1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207996448 242 VSVDGTQRTVQClSREAGGnMSIQFLGTVYKVNILTRLAAELNKFMLEK 290
Cdd:pfam18140  80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-141 2.21e-35

acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129605 [Multi-domain]  Cd Length: 449  Bit Score: 134.12  E-value: 2.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:TIGR00514 255 MGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQvehpvtemitgvdlikeqiriaageplslkqedvvvrgha 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 112
Cdd:TIGR00514 335 iecrinaeDPIKTF-LPSPGRITRYLPPGG-PGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIARMKRALSEFII 412

                         170       180
                  ....*....|....*....|....*....
gi 1207996448 113 RGVTHNIALLREVIINSRFVKGDISTKFL 141
Cdd:TIGR00514 413 DGIKTTIPFHQRILEDENFQHGGTNIHYL 441
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 298-364 2.02e-29

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 107.89  E-value: 2.02e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207996448 298 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 301-365 9.43e-23

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 99.83  E-value: 9.43e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996448  301 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK12999  1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 301-364 6.92e-22

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 97.46  E-value: 6.92e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207996448  301 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:COG1038   1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 298-364 2.55e-20

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 83.80  E-value: 2.55e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207996448 298 VLRSPMPGVVVA-----VSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:pfam00364   2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 301-365 3.79e-15

pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 77.17  E-value: 3.79e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996448  301 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:TIGR01235 1079 APMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
 
Name Accession Description Interval E-value
PccA COG4770
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
1-149 2.05e-68

Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 443802 [Multi-domain]  Cd Length: 466  Bit Score: 222.20  E-value: 2.05e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:COG4770   255 MGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQvehpvtemvtgidlveeqiriaageplpftqediklrgha 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 112
Cdd:COG4770   335 iecrinaeDPARGF-LPSPGTITRLRPPGG-PGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEAIARMRRALAEFVI 412

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207996448 113 RGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGF 149
Cdd:COG4770   413 EGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELL 449
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-141 6.38e-46

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 162.66  E-value: 6.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:PRK08591  255 IGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQvehpvtemitgvdlvkeqiriaageplsikqedivfrgha 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQYqeplHLP---GVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDN 109
Cdd:PRK08591  335 iecrinaeDPAKNF-MPSPGKITRY----HPPggpGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEAIARMKRALSE 409

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207996448 110 YVIRGVTHNIALLREVIINSRFVKGDISTKFL 141
Cdd:PRK08591  410 FVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYL 441
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
1-143 7.11e-46

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 163.62  E-value: 7.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVdSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:PRK08654  255 MGEAAVKAAKAINYENAGTVEFLY-SNGNFYFLEMNTRLQvehpitemvtgidivkeqikiaageelsfkqeditirgha 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 112
Cdd:PRK08654  334 iecrinaeDPLNDF-APSPGKIKRYRSPGG-PGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEAIARMRRALYEYVI 411

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1207996448 113 RGVTHNIALLREVIINSRFVKGDISTKFLSD 143
Cdd:PRK08654  412 VGVKTNIPFHKAVMENENFVRGNLHTHFIEE 442
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 1-159 3.73e-45

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 160.58  E-value: 3.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:PRK06111  255 MGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQvehpvteeitgidlveqqlriaageklsftqddikrsgha 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPyKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 112
Cdd:PRK06111  335 ievriyaeDP-KTF-FPSPGKITDLTLPGG-EGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKV 411

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1207996448 113 RGVTHNIALLREVIINSRFVKGDISTKFLSDvypdgfkgHMLTKSEK 159
Cdd:PRK06111  412 EGIKTNIPLLLQVLEDPVFKAGGYTTGFLTK--------QLVKKSTK 450
Biotin_carb_C smart00878
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 41-141 1.09e-44

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 214878 [Multi-domain]  Cd Length: 107  Bit Score: 149.10  E-value: 1.09e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   41 DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIA 120
Cdd:smart00878   8 DPANGF-LPSPGRITRYRFPGG-PGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGVKTNIP 85

                           90       100
                   ....*....|....*....|.
gi 1207996448  121 LLREVIINSRFVKGDISTKFL 141
Cdd:smart00878  86 FLRALLRHPDFRAGDVDTGFL 106
Biotin_carb_C pfam02785
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ...
 41-143 2.53e-44

Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.


Pssm-ID: 426981 [Multi-domain]  Cd Length: 108  Bit Score: 148.41  E-value: 2.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 DPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIA 120
Cdd:pfam02785   8 DPDNNF-LPSPGKVTRYRFP-GGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGVKTNIP 85

                          90       100
                  ....*....|....*....|...
gi 1207996448 121 LLREVIINSRFVKGDISTKFLSD 143
Cdd:pfam02785  86 FLRAILEHPDFRAGEVDTGFLEE 108
PCC_BT pfam18140
Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A ...
 162-290 1.07e-37

Propionyl-coenzyme A carboxylase BT domain; This domain is found in Propionyl-coenzyme A carboxylase (PCC), present in Roseobacter denitrificans. PCC is a mitochondrial biotin-dependent enzyme that is essential for the catabolism of certain amino acids, cholesterol, and fatty acids with an odd number of carbon atoms. Since this domain mediates biotin carboxylase-carboxyltransferase interactions it is referred to as the BT domain. The BT domain is located between biotin carboxylase and the biotin carboxyl carrier protein domains. The BT domain shares some structural similarity with the pyruvate carboxylase tetramerization domain of pyruvate carboxylase.


Pssm-ID: 465666 [Multi-domain]  Cd Length: 126  Bit Score: 131.60  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448 162 LLAIASSLFVAFQLRAQHFqENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLS 241
Cdd:pfam18140   1 LAAIAAAIHAVRELRARRI-SGQLRGHSRPVGDDWVVVVGGGDEPVTVVVEEDGDEFEVTVDGETVTVSSDWRPGDPLFR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207996448 242 VSVDGTQRTVQClSREAGGnMSIQFLGTVYKVNILTRLAAELNKFMLEK 290
Cdd:pfam18140  80 GTVDGEPVTVQV-ERRAGG-YRLRHRGTSFKVQVLTPRAAELAKLMPEK 126
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
1-143 2.17e-37

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 139.85  E-value: 2.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:PRK05586  255 MGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQvehpitemitgvdlvkeqikiaygeklsikqedikinghs 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQyqepLHLPG---VRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDN 109
Cdd:PRK05586  335 iecrinaeDPKNGF-MPCPGKIEE----LYIPGglgVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGE 409

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1207996448 110 YVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 143
Cdd:PRK05586  410 FIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEK 443
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 3-143 2.68e-36

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 139.89  E-value: 2.68e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448    3 EQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ------------------------------------------ 40
Cdd:PRK12999   261 EAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQvehtvteevtgidivqsqiliaegatlhdleigipsqedirl 340

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   41 ------------DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQ-PGSDISIYYDPMISKLITYGSDRTEALKRMADAL 107
Cdd:PRK12999   341 rgyaiqcritteDPANNF-MPDTGRITAYRSPGG-FGVRLDGGNAfAGAEITPYYDSLLVKLTAWGRTFEQAVARMRRAL 418

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1207996448  108 DNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSD 143
Cdd:PRK12999   419 REFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
accC TIGR00514
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ...
 1-141 2.21e-35

acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129605 [Multi-domain]  Cd Length: 449  Bit Score: 134.12  E-value: 2.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:TIGR00514 255 MGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQvehpvtemitgvdlikeqiriaageplslkqedvvvrgha 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 112
Cdd:TIGR00514 335 iecrinaeDPIKTF-LPSPGRITRYLPPGG-PGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVAIARMKRALSEFII 412

                         170       180
                  ....*....|....*....|....*....
gi 1207996448 113 RGVTHNIALLREVIINSRFVKGDISTKFL 141
Cdd:TIGR00514 413 DGIKTTIPFHQRILEDENFQHGGTNIHYL 441
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 5-140 3.89e-31

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 124.81  E-value: 3.89e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448    5 AVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ-------------------------------------------- 40
Cdd:COG1038    262 AVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQvehtvteevtgidivqsqiliaegyslddpeigipsqedirlng 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   41 ----------DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSG-IQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDN 109
Cdd:COG1038    342 yaiqcritteDPANNF-MPDTGRITAYRSAGG-FGIRLDGGnAYTGAVITPYYDSLLVKVTAWGRTFEEAIRKMRRALRE 419

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1207996448  110 YVIRGVTHNIALLREVIINSRFVKGDISTKF 140
Cdd:COG1038    420 FRIRGVKTNIPFLENVLNHPDFLAGECTTSF 450
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
1-141 1.21e-29

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 118.67  E-value: 1.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:PRK07178  254 IGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQvehtiteeitgidivreqiriasglplsykqediqhrgfa 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 112
Cdd:PRK07178  334 lqfrinaeDPKNDF-LPSFGKITRYYAPGG-PGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEALDRGRRALDDMRV 411

                         170       180
                  ....*....|....*....|....*....
gi 1207996448 113 RGVTHNIALLREVIINSRFVKGDISTKFL 141
Cdd:PRK07178  412 QGVKTTIPYYQEILRNPEFRSGQFNTSFV 440
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 298-364 2.02e-29

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 107.89  E-value: 2.02e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207996448 298 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:cd06850     1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
3-142 2.19e-28

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 114.84  E-value: 2.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   3 EQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ------------------------------------------ 40
Cdd:PRK08462  259 ETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQvehtvsemvsgldliewmikiaegeelpsqesiklkghaiec 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 -----DPyKSFgLPSIGRLSQYQeplhLPG---VRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 112
Cdd:PRK08462  339 ritaeDP-KKF-YPSPGKITKWI----APGgrnVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAIAKMKRALKEFKV 412

                         170       180       190
                  ....*....|....*....|....*....|
gi 1207996448 113 RGVTHNIALLREVIINSRFVKGDISTKFLS 142
Cdd:PRK08462  413 EGIKTTIPFHLEMMENADFINNKYDTKYLE 442
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 3-141 4.91e-27

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 111.39  E-value: 4.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   3 EQAVALARAVKYSSAGTVEFLVD-SKKNFYFLEMNTRLQ----------------------------------------- 40
Cdd:PRK12833  259 ASAVRLARQVGYRGAGTLEYLFDdARGEFYFIEMNTRIQvehpvteaitgidlvqemlriadgeplrfaqgdialrgaal 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 -------DPYKSFgLPSIGRLSQYQEPlHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIR 113
Cdd:PRK12833  339 ecrinaeDPLRDF-FPNPGRIDALVWP-QGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAALARAARALRELRID 416

                         170       180
                  ....*....|....*....|....*...
gi 1207996448 114 GVTHNIALLREVIINSRFVKGDISTKFL 141
Cdd:PRK12833  417 GMKTTAPLHRALLADADVRAGRFHTNFL 444
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
 1-141 6.25e-24

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 102.58  E-value: 6.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQ---------------------------------------- 40
Cdd:PRK08463  255 MGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQvehgvteeitgidlivrqiriaageildleqsdikprgfa 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448  41 --------DPYKSFgLPSIGRLSQYQEPLHlPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVI 112
Cdd:PRK08463  335 iearitaeNVWKNF-IPSPGKITEYYPALG-PSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYDLAVNKLERALKEFVI 412

                         170       180
                  ....*....|....*....|....*....
gi 1207996448 113 RGVTHNIALLREVIINSRFVKGDISTKFL 141
Cdd:PRK08463  413 DGIRTTIPFLIAITKTREFRRGYFDTSYI 441
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 301-365 9.43e-23

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 99.83  E-value: 9.43e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996448  301 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK12999  1081 APMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 301-364 6.92e-22

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 97.46  E-value: 6.92e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207996448  301 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:COG1038   1081 APMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 298-364 2.55e-20

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 83.80  E-value: 2.55e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207996448 298 VLRSPMPGVVVA-----VSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:pfam00364   2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 298-365 3.56e-20

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 85.33  E-value: 3.56e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996448 298 VLRSPMPGVV-------VAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:COG0511    62 AVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 218-365 7.99e-20

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 90.67  E-value: 7.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448 218 FSVEVDGSKLNV--TSTWNLASPLLSVSVDGTQRTVQclsreaggnmsiqflgtvykvniltrlAAELNKF-MLEKVTED 294
Cdd:PRK09282  468 FKVEVDGEKYEVkiEGVKAEGKRPFYLRVDGMPEEVV---------------------------VEPLKEIvVGGRPRAS 520

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996448 295 TSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK09282  521 APGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 297-365 2.89e-18

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 78.29  E-value: 2.89e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207996448 297 SVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK08225    2 TKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 298-362 1.35e-17

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 78.32  E-value: 1.35e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996448 298 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLV 362
Cdd:PRK06549   63 AMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLI 127
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 298-364 1.39e-15

putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 73.36  E-value: 1.39e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207996448 298 VLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:PRK05641   86 VVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
pyruv_carbox TIGR01235
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ...
 301-365 3.79e-15

pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 130302 [Multi-domain]  Cd Length: 1143  Bit Score: 77.17  E-value: 3.79e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207996448  301 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:TIGR01235 1079 APMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAPKDGTIKEVLVKAGEQIDAKDLLLVLE 1143
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
301-364 6.93e-13

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 69.57  E-value: 6.93e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207996448 301 SPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:PRK14040  529 APLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 305-364 6.98e-12

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 60.50  E-value: 6.98e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448 305 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:cd06849    15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 1-40 2.62e-11

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 62.32  E-value: 2.62e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1207996448   1 MGEQAVALARAVKYSSAGTVEFLVDSK-KNFYFLEMNTRLQ 40
Cdd:pfam02786 141 LREAAVKIARHLGYVGAGTVEFALDPFsGEYYFIEMNTRLQ 181
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 305-364 6.34e-10

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 55.07  E-value: 6.34e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448 305 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:COG0508    17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 303-365 7.60e-10

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 60.12  E-value: 7.60e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207996448 303 MPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK14042  532 IPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 305-364 2.89e-09

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


Pssm-ID: 133456 [Multi-domain]  Cd Length: 73  Bit Score: 53.21  E-value: 2.89e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448 305 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:cd06663    14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 305-365 4.50e-08

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 54.88  E-value: 4.50e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996448 305 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:TIGR01348  14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 300-344 4.90e-08

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 53.69  E-value: 4.90e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1207996448 300 RSPMPGVvvAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTV 344
Cdd:PLN02983  210 RSPAPGE--PPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTI 252
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 1-40 9.16e-08

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 52.57  E-value: 9.16e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1207996448   1 MGEQAVALARAVKYS-SAGTVEFLVDSKKNFYFLEMNTRLQ 40
Cdd:COG0439   190 IGELVARALRALGYRrGAFHTEFLLTPDGEPYLIEINARLG 230
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
299-365 2.50e-07

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 47.70  E-value: 2.50e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207996448 299 LRSPMPGVV-------VAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK07051    6 IVSPLPGTFyrrpspdAPPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARIE 79
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 307-365 3.74e-07

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 51.75  E-value: 3.74e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996448 307 VVAVSVKPGDAVAEGQEICVIEAMK--MQnsMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK11855  135 VIEWLVKVGDTVEEDQSLITVETDKatME--IPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 305-365 4.73e-07

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 51.41  E-value: 4.73e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996448 305 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:TIGR01348 130 VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
PRK05889 PRK05889
biotin/lipoyl-binding carrier protein;
299-361 1.95e-06

biotin/lipoyl-binding carrier protein;


Pssm-ID: 180306 [Multi-domain]  Cd Length: 71  Bit Score: 45.18  E-value: 1.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207996448 299 LRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLL 361
Cdd:PRK05889    5 VRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLI 67
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 307-365 2.70e-06

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 49.05  E-value: 2.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996448 307 VVAVSVKPGDAVAEGQEICVIEAMK--MQnsMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK11855   18 VIEWLVKEGDTVEEDQPLVTVETDKatME--IPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 305-364 2.05e-04

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 43.13  E-value: 2.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207996448 305 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVEL 364
Cdd:PTZ00144   59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI 118
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 305-361 2.15e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 43.01  E-value: 2.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1207996448 305 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLL 361
Cdd:PRK14875   17 GKVAGWLVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALL 73
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 305-365 8.13e-04

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 41.53  E-value: 8.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996448 305 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK11854  118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVFE 178
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 305-365 1.47e-03

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 40.37  E-value: 1.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996448 305 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK11854  219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 305-365 1.83e-03

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 40.37  E-value: 1.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207996448 305 GVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE 365
Cdd:PRK11854   15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 290-329 9.69e-03

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 37.62  E-value: 9.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1207996448 290 KVTEDTSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEA 329
Cdd:COG0845    17 TVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDP 56
 
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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