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Conserved domains on  [gi|446276443|ref|WP_000354298|]
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MULTISPECIES: acetyl-CoA carboxylase biotin carboxyl carrier protein [Streptococcus]

Protein Classification

acetyl-CoA carboxylase biotin carboxyl carrier protein( domain architecture ID 11423502)

acetyl-CoA carboxylase biotin carboxyl carrier protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA

CATH:  2.40.50.100
Gene Ontology:  GO:0003989|GO:0006633|GO:0009317
PubMed:  1370469
SCOP:  4002909
TCDB:  3.B.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 9-166 4.49e-37

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: 124.24  E-value: 4.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443   9 LMTQFDESSLREFSFKTSDGELSFSKNEGKAplvptmspmsHQPEATPTIATPVSNEAGEQTKQATEvvseipestvtvA 88
Cdd:COG0511    1 LIELLEESGLTELEVEEGEYKVRIKRGGAAA----------AAPVAAPAAAAPAAAAPAAAAAAAAA------------S 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446276443  89 EGDVVESPLVGVAYLASGPDKPNFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:COG0511   59 GGGAVKSPMVGTFYRAPSPGAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
 
Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 9-166 4.49e-37

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: 124.24  E-value: 4.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443   9 LMTQFDESSLREFSFKTSDGELSFSKNEGKAplvptmspmsHQPEATPTIATPVSNEAGEQTKQATEvvseipestvtvA 88
Cdd:COG0511    1 LIELLEESGLTELEVEEGEYKVRIKRGGAAA----------AAPVAAPAAAAPAAAAPAAAAAAAAA------------S 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446276443  89 EGDVVESPLVGVAYLASGPDKPNFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:COG0511   59 GGGAVKSPMVGTFYRAPSPGAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
BCCP TIGR00531
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify ...
 1-166 9.75e-31

acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify biotin carboxyl carrier protein as a peptide of acetyl-CoA carboxylase. Scoring below the trusted cutoff is a related protein encoded in a region associated with polyketide synthesis in the prokaryote Saccharopolyspora hirsuta, and a reported chloroplast-encoded biotin carboxyl carrier protein that may be highly derived from the last common ancestral sequence. Scoring below the noise cutoff are biotin carboxyl carrier domains of other enzymes such as pyruvate carboxylase.The gene name is accB or fabE. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273123 [Multi-domain]  Cd Length: 155  Bit Score: 108.77  E-value: 9.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443    1 MDIQEIKDLMTQFDESSLREFSFKTSDGELSFSKNEGKAplVPTMSPMSHQPEATPTIATPvsneagEQTKQATEVVSEI 80
Cdd:TIGR00531   1 MNIREIKELIKLVEESGITELELKEEEFSVRLSKAAAAA--SFSVVQQAAAPVPAQVPAQS------SAAVPAPAPAAPA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443   81 PESTVTvaeGDVVESPLVGVAYLASGPDKPNFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGK 160
Cdd:TIGR00531  73 PAADIK---GHIVRSPMVGTFYRAPSPDAKPFVEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVENGQPVEYGE 149


                  ....*.
gi 446276443  161 GLVRIK 166
Cdd:TIGR00531 150 PLIVIE 155
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 47-166 9.05e-22

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 90.67  E-value: 9.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443  47 PMSHQPEATPTIATPVSNEAGEQTKQATEVVSEIPESTVtvaEGDVVeSPLVGVAYLAsgpdkpnFVSVGDSVKKGQTLM 126
Cdd:PRK09282 483 GVKAEGKRPFYLRVDGMPEEVVVEPLKEIVVGGRPRASA---PGAVT-SPMPGTVVKV-------KVKEGDKVKAGDTVL 551

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446276443 127 IIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:PRK09282 552 VLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 92-165 3.20e-19

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: 76.30  E-value: 3.20e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446276443  92 VVESPLVGVAYLasgpdkpNFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:cd06850    1 EVTAPMPGTVVK-------VLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 92-165 2.29e-14

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: 64.16  E-value: 2.29e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446276443   92 VVESPLVGVAYlaSGPDKPNFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:pfam00364   2 EIKSPMIGESV--REGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
 
Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 9-166 4.49e-37

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: 124.24  E-value: 4.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443   9 LMTQFDESSLREFSFKTSDGELSFSKNEGKAplvptmspmsHQPEATPTIATPVSNEAGEQTKQATEvvseipestvtvA 88
Cdd:COG0511    1 LIELLEESGLTELEVEEGEYKVRIKRGGAAA----------AAPVAAPAAAAPAAAAPAAAAAAAAA------------S 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446276443  89 EGDVVESPLVGVAYLASGPDKPNFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:COG0511   59 GGGAVKSPMVGTFYRAPSPGAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
BCCP TIGR00531
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify ...
 1-166 9.75e-31

acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify biotin carboxyl carrier protein as a peptide of acetyl-CoA carboxylase. Scoring below the trusted cutoff is a related protein encoded in a region associated with polyketide synthesis in the prokaryote Saccharopolyspora hirsuta, and a reported chloroplast-encoded biotin carboxyl carrier protein that may be highly derived from the last common ancestral sequence. Scoring below the noise cutoff are biotin carboxyl carrier domains of other enzymes such as pyruvate carboxylase.The gene name is accB or fabE. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273123 [Multi-domain]  Cd Length: 155  Bit Score: 108.77  E-value: 9.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443    1 MDIQEIKDLMTQFDESSLREFSFKTSDGELSFSKNEGKAplVPTMSPMSHQPEATPTIATPvsneagEQTKQATEVVSEI 80
Cdd:TIGR00531   1 MNIREIKELIKLVEESGITELELKEEEFSVRLSKAAAAA--SFSVVQQAAAPVPAQVPAQS------SAAVPAPAPAAPA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443   81 PESTVTvaeGDVVESPLVGVAYLASGPDKPNFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGK 160
Cdd:TIGR00531  73 PAADIK---GHIVRSPMVGTFYRAPSPDAKPFVEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVENGQPVEYGE 149


                  ....*.
gi 446276443  161 GLVRIK 166
Cdd:TIGR00531 150 PLIVIE 155
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 47-166 9.05e-22

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 90.67  E-value: 9.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443  47 PMSHQPEATPTIATPVSNEAGEQTKQATEVVSEIPESTVtvaEGDVVeSPLVGVAYLAsgpdkpnFVSVGDSVKKGQTLM 126
Cdd:PRK09282 483 GVKAEGKRPFYLRVDGMPEEVVVEPLKEIVVGGRPRASA---PGAVT-SPMPGTVVKV-------KVKEGDKVKAGDTVL 551

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446276443 127 IIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:PRK09282 552 VLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 2-149 1.15e-19

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 82.96  E-value: 1.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443   2 DIQEIKDLMTQF-------DESSLREFSFKTSDGELSFSKNEG------KAPLVPTMSPMSH----------QPEATPTI 58
Cdd:PLN02983  98 DEESISEFMTQVsslvklvDSRDIVELQLKQLDCELVIRKKEAlpqpppPAPVVMMQPPPPHamppasppaaQPAPSAPA 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443  59 ATPVSNEAgeQTKQATEVVSEIPEstvtvaegdvVESPLVGVAYLASGPDKPNFVSVGDSVKKGQTLMIIEAMKVMNEVP 138
Cdd:PLN02983 178 SSPPPTPA--SPPPAKAPKSSHPP----------LKSPMAGTFYRSPAPGEPPFVKVGDKVQKGQVVCIIEAMKLMNEIE 245

                        170
                 ....*....|.
gi 446276443 139 APHDGVVTEIL 149
Cdd:PLN02983 246 ADQSGTIVEIL 256
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 92-165 3.20e-19

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: 76.30  E-value: 3.20e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446276443  92 VVESPLVGVAYLasgpdkpNFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:cd06850    1 EVTAPMPGTVVK-------VLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
93-165 3.51e-15

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 66.57  E-value: 3.51e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446276443  93 VESPLVGVAYLASGPDKPNFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:PRK07051   6 IVSPLPGTFYRRPSPDAPPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 92-165 2.29e-14

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: 64.16  E-value: 2.29e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446276443   92 VVESPLVGVAYlaSGPDKPNFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:pfam00364   2 EIKSPMIGESV--REGVVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 52-166 4.51e-13

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 62.52  E-value: 4.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443  52 PEATPTIATPVSNEAGEQTKQATEVVSEIPeSTVTVAEGDVVESPLVGVAYLAsgpdkpnFVSVGDSVKKGQTLMIIEAM 131
Cdd:PRK06549  24 PAQAAAPAQPASTPVPVPTEASPQVEAQAP-QPAAAAGADAMPSPMPGTILKV-------LVAVGDQVTENQPLLILEAM 95

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446276443 132 KVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:PRK06549  96 KMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 112-165 5.09e-13

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: 65.87  E-value: 5.09e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446276443  112 FVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:COG1038  1091 LVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 113-166 4.27e-12

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 63.23  E-value: 4.27e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446276443  113 VSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:PRK12999 1092 VKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 52-165 9.75e-12

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


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 59.49  E-value: 9.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443  52 PEATPTIATPVSNEAGEQTKQATEVVSEIPESTVTVAEGDVVESPLVGVAYLAsgpdkpnFVSVGDSVKKGQTLMIIEAM 131
Cdd:PRK05641  46 SAVQEQVPTPAPAPAPAVPSAPTPVAPAAPAPAPASAGENVVTAPMPGKILRI-------LVREGQQVKVGQGLLILEAM 118

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446276443 132 KVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:PRK05641 119 KMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 112-165 3.30e-11

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: 55.87  E-value: 3.30e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446276443 112 FVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:cd06849   21 LVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 112-165 1.08e-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: 54.69  E-value: 1.08e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446276443 112 FVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:COG0508   23 LVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 112-165 1.92e-10

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: 53.98  E-value: 1.92e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446276443 112 FVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:cd06663   20 LKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 51-166 5.41e-10

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 56.75  E-value: 5.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443  51 QPEATPTIATPVSNEAGEQTKQATEVVSEIPEstVTVAE-GDVVESPLVGVaylasgpdkpnFVSVGDSVKKGQTLMIIE 129
Cdd:PRK11855  90 AAAPAAAAAAAPAPAAAAPAAAAAAAGGGVVE--VKVPDiGEITEVEVIEW-----------LVKVGDTVEEDQSLITVE 156

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446276443 130 AMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:PRK11855 157 TDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
81-150 2.02e-09

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 55.32  E-value: 2.02e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443  81 PESTVTVAEGDVVESPLVGVAYlasgpdKPNfVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILV 150
Cdd:PRK14040 515 AAAAPAAAAGEPVTAPLAGNIF------KVI-VTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAV 577
PRK11856 PRK11856
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
 112-165 3.12e-09

branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed


Pssm-ID: 237001 [Multi-domain]  Cd Length: 411  Bit Score: 54.41  E-value: 3.12e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446276443 112 FVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:PRK11856  23 LVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVEEGDVVPVGSVIAVI 76
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 113-166 5.86e-09

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 53.96  E-value: 5.86e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446276443 113 VSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:PRK14042 541 VSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 90-166 2.22e-08

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 52.13  E-value: 2.22e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446276443  90 GDVVESPLVGVaylasgpdkpnFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:PRK11855  11 GEVVEVEVIEW-----------LVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
73-166 3.07e-08

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 51.76  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443  73 ATEV-VSEIPEStvtVAEGDVVESplvgvaylasgpdkpnFVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVA 151
Cdd:PRK05704   2 MVEIkVPTLPES---VTEATIATW----------------HKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAE 62

                         90
                 ....*....|....*
gi 446276443 152 NEEVIEFGKGLVRIK 166
Cdd:PRK05704  63 EGDTVTVGQVLGRID 77
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 77-165 4.33e-08

2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]


Pssm-ID: 273565 [Multi-domain]  Cd Length: 403  Bit Score: 51.27  E-value: 4.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443   77 VSEIPEStvtVAEGDVVEsplvgvaYLASgpdkpnfvsVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVI 156
Cdd:TIGR01347   5 VPELAES---ITEGTVAE-------WHKK---------VGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTV 65


                  ....*....
gi 446276443  157 EFGKGLVRI 165
Cdd:TIGR01347  66 ESGQVLAIL 74
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 112-165 4.48e-08

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 51.10  E-value: 4.48e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446276443 112 FVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:PRK14875  23 LVQEGDEVEKGDELLDVETDKITNEVEAPAAGTLRRQVAQEGETLPVGALLAVV 76
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 52-165 1.74e-05

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 43.84  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443  52 PEATPTIATPVSNEAGEQTKQATEVvsEIPEstVTVAEGDVVESplvgvaylasgpdkpnFVSVGDSVKKGQTLMIIEAM 131
Cdd:PRK11854  84 APAQAEEKKEAAPAAAPAAAAAKDV--HVPD--IGSDEVEVTEI----------------LVKVGDTVEAEQSLITVEGD 143

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446276443 132 KVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:PRK11854 144 KASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVF 177
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 112-160 4.24e-05

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 42.68  E-value: 4.24e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446276443 112 FVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGK 160
Cdd:PRK11854  21 LVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGA 69
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 113-166 4.64e-05

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 42.36  E-value: 4.64e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446276443 113 VSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:PTZ00144  66 KKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID 119
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 113-166 7.53e-05

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 41.91  E-value: 7.53e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446276443 113 VSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRIK 166
Cdd:PRK11854 226 VKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRFE 279
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 113-150 2.25e-04

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: 40.63  E-value: 2.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446276443  113 VSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILV 150
Cdd:TIGR01348  21 VKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKV 58
GCS_H cd06848
Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage ...
 112-157 2.33e-04

Glycine cleavage H-protein. Glycine cleavage H-proteins are part of the glycine cleavage system (GCS) found in bacteria, archea and the mitochondria of eukaryotes. GCS is a multienzyme complex consisting of 4 different components (P-, H-, T- and L-proteins) which catalyzes the oxidative cleavage of glycine. The H-protein shuttles the methylamine group of glycine from the P-protein (glycine dehydrogenase) to the T-protein (aminomethyltransferase) via a lipoyl group, attached to a completely conserved lysine residue.


Pssm-ID: 133457 [Multi-domain]  Cd Length: 96  Bit Score: 38.28  E-value: 2.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446276443 112 FVSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEIlvaNEEVIE 157
Cdd:cd06848   36 LPEVGTEVKKGDPFGSVESVKAASDLYSPVSGEVVEV---NEALLD 78
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 52-150 3.25e-04

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: 39.86  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446276443   52 PEATPTIATPVSNEAGEQTKQATEVVSeipestVTVAE-GDVVESPLVGVaylasgpdkpnFVSVGDSVKKGQTLMIIEA 130
Cdd:TIGR01348  92 APTAGAPAPAAQAQAAPAAGQSSGVQE------VTVPDiGDIEKVTVIEV-----------LVKVGDTVSADQSLITLES 154

                          90       100
                  ....*....|....*....|
gi 446276443  131 MKVMNEVPAPHDGVVTEILV 150
Cdd:TIGR01348 155 DKASMEVPAPASGVVKSVKV 174
GCV_H pfam01597
Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the ...
 115-157 3.87e-04

Glycine cleavage H-protein; This is a family of glycine cleavage H-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. A lipoyl group is attached to a completely conserved lysine residue. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.


Pssm-ID: 396258  Cd Length: 122  Bit Score: 38.47  E-value: 3.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446276443  115 VGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEIlvaNEEVIE 157
Cdd:pfam01597  41 VGTKVKKGESLAAIESVKAASPIYAPVSGEVVEV---NEKLED 80
PRK01202 PRK01202
glycine cleavage system protein GcvH;
115-166 4.75e-04

glycine cleavage system protein GcvH;


Pssm-ID: 234918  Cd Length: 127  Bit Score: 38.22  E-value: 4.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446276443 115 VGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEIlvaNEEVIE---------FGKG-LVRIK 166
Cdd:PRK01202  47 VGDEVKAGETFGVVESVKAASDIYAPVSGEVVEV---NEALEDspelvnedpYGEGwLFKIK 105
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 113-165 1.47e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 35.53  E-value: 1.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446276443 113 VSVGDSVKKGQTLMIIEAMKVMNEVPAPHDGVVTEILVANEEVIEFGKGLVRI 165
Cdd:PRK08225  17 VKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEI 69
 
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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