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Conserved domains on  [gi|488377131|ref|WP_002446516|]
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MULTISPECIES: acetyl-CoA carboxylase biotin carboxyl carrier protein [Staphylococcus]

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 ...
 9-157 9.07e-50

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: 156.21  E-value: 9.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131   9 LIEILDQSNLTEINIEDNKGSVVnLKKEKETEiVTPQVTQQPTQPITHAQIDNETQQKPSHsyndeqssdnnYNTINAPM 88
Cdd:COG0511    1 LIELLEESGLTELEVEEGEYKVR-IKRGGAAA-AAPVAAPAAAAPAAAAPAAAAAAAAASG-----------GGAVKSPM 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377131  89 VGTFYKSPSPDEEAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:COG0511   68 VGTFYRAPSPGAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
 
Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 9-157 9.07e-50

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: 156.21  E-value: 9.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131   9 LIEILDQSNLTEINIEDNKGSVVnLKKEKETEiVTPQVTQQPTQPITHAQIDNETQQKPSHsyndeqssdnnYNTINAPM 88
Cdd:COG0511    1 LIELLEESGLTELEVEEGEYKVR-IKRGGAAA-AAPVAAPAAAAPAAAAPAAAAAAAAASG-----------GGAVKSPM 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377131  89 VGTFYKSPSPDEEAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:COG0511   68 VGTFYRAPSPGAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
BCCP TIGR00531
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify ...
 1-157 6.59e-47

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: 149.60  E-value: 6.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131    1 MNFKEIKELIEILDQSNLTEINIEDNKGSVvnlKKEKETEIVTPQVTQQPTQPITHAQIDNETQQKPSHSYNDE-QSSDN 79
Cdd:TIGR00531   1 MNIREIKELIKLVEESGITELELKEEEFSV---RLSKAAAAASFSVVQQAAAPVPAQVPAQSSAAVPAPAPAAPaPAADI 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488377131   80 NYNTINAPMVGTFYKSPSPDEEAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:TIGR00531  78 KGHIVRSPMVGTFYRAPSPDAKPFVEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVENGQPVEYGEPLIVIE 155
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 75-154 6.74e-29

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 106.85  E-value: 6.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131  75 QSSDNNYNTINAPMVGTFYKSPSPDEEAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLF 154
Cdd:PLN02983 191 KAPKSSHPPLKSPMAGTFYRSPAPGEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPLF 270
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 83-156 1.25e-24

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: 90.17  E-value: 1.25e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488377131  83 TINAPMVGTFYKSpspdeeaYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:cd06850    1 EVTAPMPGTVVKV-------LVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 82-156 4.36e-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: 78.80  E-value: 4.36e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488377131   82 NTINAPMVGTFYKSPspDEEAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:pfam00364   1 TEIKSPMIGESVREG--VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
 
Name Accession Description Interval E-value
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 9-157 9.07e-50

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: 156.21  E-value: 9.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131   9 LIEILDQSNLTEINIEDNKGSVVnLKKEKETEiVTPQVTQQPTQPITHAQIDNETQQKPSHsyndeqssdnnYNTINAPM 88
Cdd:COG0511    1 LIELLEESGLTELEVEEGEYKVR-IKRGGAAA-AAPVAAPAAAAPAAAAPAAAAAAAAASG-----------GGAVKSPM 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377131  89 VGTFYKSPSPDEEAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:COG0511   68 VGTFYRAPSPGAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
BCCP TIGR00531
acetyl-CoA carboxylase, biotin carboxyl carrier protein; This model is designed to identify ...
 1-157 6.59e-47

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: 149.60  E-value: 6.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131    1 MNFKEIKELIEILDQSNLTEINIEDNKGSVvnlKKEKETEIVTPQVTQQPTQPITHAQIDNETQQKPSHSYNDE-QSSDN 79
Cdd:TIGR00531   1 MNIREIKELIKLVEESGITELELKEEEFSV---RLSKAAAAASFSVVQQAAAPVPAQVPAQSSAAVPAPAPAAPaPAADI 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488377131   80 NYNTINAPMVGTFYKSPSPDEEAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:TIGR00531  78 KGHIVRSPMVGTFYRAPSPDAKPFVEVGDKVNKGQTVCIVEAMKMMNEIEAEKAGTVVAILVENGQPVEYGEPLIVIE 155
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 75-154 6.74e-29

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 106.85  E-value: 6.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131  75 QSSDNNYNTINAPMVGTFYKSPSPDEEAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLF 154
Cdd:PLN02983 191 KAPKSSHPPLKSPMAGTFYRSPAPGEPPFVKVGDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPLF 270
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 83-156 1.25e-24

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: 90.17  E-value: 1.25e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488377131  83 TINAPMVGTFYKSpspdeeaYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:cd06850    1 EVTAPMPGTVVKV-------LVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 19-157 3.29e-24

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 97.22  E-value: 3.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131  19 TEINIEDNkGSVVNLKKEKETEIvtpqvtQQPTQPITHAQIDNETQQKPSHSYNDEQSSD-NNYNTINAPMVGTFYKsps 97
Cdd:PRK09282 466 TEFKVEVD-GEKYEVKIEGVKAE------GKRPFYLRVDGMPEEVVVEPLKEIVVGGRPRaSAPGAVTSPMPGTVVK--- 535

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131  98 pdeeAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:PRK09282 536 ----VKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
83-156 3.21e-23

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 86.99  E-value: 3.21e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488377131  83 TINAPMVGTFYKSPSPDEEAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:PRK07051   5 EIVSPLPGTFYRRPSPDAPPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 82-156 4.36e-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: 78.80  E-value: 4.36e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488377131   82 NTINAPMVGTFYKSPspDEEAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:pfam00364   1 TEIKSPMIGESVREG--VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 40-157 3.12e-12

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 59.83  E-value: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131  40 EIVTPQVTQQPTQPITHAQIDNETQQKPSHSYNDEQSSDNNYNTINAPMVGTFYKspspdeeAYVQVGDKVTNDSTVCIL 119
Cdd:PRK06549  20 EIGAPAQAAAPAQPASTPVPVPTEASPQVEAQAPQPAAAAGADAMPSPMPGTILK-------VLVAVGDQVTENQPLLIL 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488377131 120 EAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:PRK06549  93 EAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 83-156 2.28e-11

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: 56.30  E-value: 2.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131  83 TINAPM------VGTFYKspspdeeAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:cd06663    1 TILIPDlaqhlgDGTVVK-------WLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
83-156 7.97e-11

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 58.79  E-value: 7.97e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488377131  83 TINAPMVGTFYKspspdeeAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:PRK14040 526 PVTAPLAGNIFK-------VIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 37-153 4.40e-10

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


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 54.87  E-value: 4.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377131  37 KETEIVTPQVTQQPTQPITHAQIDNETQQKPSHSYNDeqssdnnyNTINAPMVGTFYKspspdeeAYVQVGDKVTNDSTV 116
Cdd:PRK05641  48 VQEQVPTPAPAPAPAVPSAPTPVAPAAPAPAPASAGE--------NVVTAPMPGKILR-------ILVREGQQVKVGQGL 112

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488377131 117 CILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPL 153
Cdd:PRK05641 113 LILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPL 149
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 79-156 7.24e-10

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: 56.24  E-value: 7.24e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488377131   79 NNYNTINAPMVGTFYKspspdeeAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:COG1038  1074 GNPGHIGAPMPGTVVK-------VLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 79-157 6.56e-08

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 50.52  E-value: 6.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488377131   79 NNYNTINAPMVGTFYKspspdeeAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:PRK12999 1074 GNPGHVGAPMPGSVVT-------VLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 103-156 6.91e-08

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: 47.01  E-value: 6.91e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377131 103 YVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:cd06849   21 LVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 104-157 6.46e-07

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 47.75  E-value: 6.46e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377131 104 VQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:PTZ00144  66 KKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEID 119
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 103-156 1.01e-06

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: 43.90  E-value: 1.01e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377131 103 YVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:COG0508   23 LVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 82-153 2.19e-06

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 43.24  E-value: 2.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488377131  82 NTINAPMVGTFYKspspdeeAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPL 153
Cdd:PRK08225   2 TKVYASMAGNVWK-------IVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVL 66
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 103-157 8.87e-06

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 44.33  E-value: 8.87e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488377131 103 YVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:PRK14042 540 HVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 104-157 9.68e-06

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 44.04  E-value: 9.68e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377131 104 VQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:PRK11855 140 VKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
128-156 3.05e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 42.73  E-value: 3.05e-05
                         10        20
                 ....*....|....*....|....*....
gi 488377131 128 IQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:COG1566   48 VAAKVSGRVTEVLVKEGDRVKKGQVLARL 76
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 127-156 2.39e-04

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: 39.93  E-value: 2.39e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 488377131 127 EIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:COG0845   25 EVRARVSGRVEEVLVDEGDRVKKGQVLARL 54
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 106-156 2.56e-04

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: 40.10  E-value: 2.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488377131  106 VGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:TIGR01347  24 VGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL 74
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 104-157 1.61e-03

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 37.88  E-value: 1.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488377131 104 VQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:PRK11855  23 VKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
103-151 2.64e-03

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 37.12  E-value: 2.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 488377131 103 YVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYGQ 151
Cdd:PRK05704  23 HKKPGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQ 71
PRK05889 PRK05889
biotin/lipoyl-binding carrier protein;
101-150 6.07e-03

biotin/lipoyl-binding carrier protein;


Pssm-ID: 180306 [Multi-domain]  Cd Length: 71  Bit Score: 34.01  E-value: 6.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488377131 101 EAYVQVGDKVTNDSTVCILEAMKLFNEIQAETTGEIVEILVEDGQMVEYG 150
Cdd:PRK05889  15 EVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAG 64
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 127-155 6.24e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 35.86  E-value: 6.24e-03
                          10        20
                  ....*....|....*....|....*....
gi 488377131  127 EIQAETTGEIVEILVEDGQMVEYGQPLFK 155
Cdd:pfam00529  22 AVQPQVSGIVTRVLVKEGDRVKAGDVLFQ 50
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 127-156 7.53e-03

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 35.75  E-value: 7.53e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 488377131  127 EIQAETTGEIVEILVEDGQMVEYGQPLFKV 156
Cdd:TIGR01730  28 DLAAEVAGKITKISVREGQKVKKGQVLARL 57
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
127-157 9.34e-03

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 32.80  E-value: 9.34e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 488377131  127 EIQAETTGEIVEILVEDGQMVEYGQPLFKVK 157
Cdd:pfam13533   4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLD 34
 
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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