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Conserved domains on  [gi|490227283|ref|WP_004125634|]
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MULTISPECIES: acetyl-CoA carboxylase biotin carboxyl carrier protein subunit [Klebsiella]

Protein Classification

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit( domain architecture ID 10160553)

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit participates in the carboxylation of the carrier protein and the transfer of the carboxyl group to form malonyl-CoA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 3-69 2.10e-18

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: 70.91  E-value: 2.10e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490227283  3 EVKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:cd06850   1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
 
Name Accession Description Interval E-value
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 3-69 2.10e-18

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: 70.91  E-value: 2.10e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490227283  3 EVKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:cd06850   1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 4-69 1.29e-17

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 74.88  E-value: 1.29e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490227283   4 VKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PRK09282 525 VTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 9-69 1.55e-15

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: 68.95  E-value: 1.55e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490227283    9 PGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:COG1038  1084 PGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 12-69 3.45e-10

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: 50.29  E-value: 3.45e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490227283  12 VDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:pfam00364 16 VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 10-63 7.72e-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: 47.18  E-value: 7.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 490227283   10 GVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPG 63
Cdd:TIGR01348 130 VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTG 183
 
Name Accession Description Interval E-value
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 3-69 2.10e-18

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: 70.91  E-value: 2.10e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490227283  3 EVKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:cd06850   1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 4-69 1.29e-17

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 74.88  E-value: 1.29e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490227283   4 VKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PRK09282 525 VTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEI 590
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 9-69 1.55e-15

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: 68.95  E-value: 1.55e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490227283    9 PGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:COG1038  1084 PGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 9-69 5.56e-14

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 64.39  E-value: 5.56e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490227283    9 PGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PRK12999 1084 PGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTITAPVDGTVKRVLVKAGDQVEAGDLLVEL 1144
PRK08225 PRK08225
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 1-69 1.57e-13

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 181304 [Multi-domain]  Cd Length: 70  Bit Score: 58.65  E-value: 1.57e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490227283  1 MSEVKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PRK08225  1 MTKVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEGDFVNEGDVLLEI 69
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 3-69 1.34e-11

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 57.81  E-value: 1.34e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490227283   3 EVKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PRK14042 527 DITVAIPGSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRV 593
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 3-69 3.04e-11

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: 54.52  E-value: 3.04e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490227283   3 EVKSKVPGVV-------DEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:COG0511   62 AVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVI 135
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
3-69 5.31e-11

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 56.09  E-value: 5.31e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490227283   3 EVKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PRK14040 526 PVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVKEGDAVAVGDTLLTL 592
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 12-69 3.45e-10

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: 50.29  E-value: 3.45e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490227283  12 VDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:pfam00364 16 VVEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
PRK05641 PRK05641
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 4-69 6.50e-08

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


Pssm-ID: 235540 [Multi-domain]  Cd Length: 153  Bit Score: 46.39  E-value: 6.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490227283   4 VKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PRK05641  87 VTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDTGQPLIEL 152
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 10-72 6.86e-08

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 47.30  E-value: 6.86e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490227283  10 GVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEIIAE 72
Cdd:PRK11854  15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFESA 77
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 10-63 7.72e-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: 47.18  E-value: 7.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 490227283   10 GVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPG 63
Cdd:TIGR01348 130 VTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTG 183
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
 10-69 1.17e-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: 46.41  E-value: 1.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490227283   10 GVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:TIGR01348  14 GEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATL 73
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 10-69 4.30e-07

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: 42.39  E-value: 4.30e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490227283 10 GVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:cd06849  15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
PRK05889 PRK05889
biotin/lipoyl-binding carrier protein;
3-63 4.93e-06

biotin/lipoyl-binding carrier protein;


Pssm-ID: 180306 [Multi-domain]  Cd Length: 71  Bit Score: 39.79  E-value: 4.93e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490227283  3 EVKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPG 63
Cdd:PRK05889  4 DVRAEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAG 64
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 10-70 5.69e-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: 39.66  E-value: 5.69e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490227283 10 GVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEII 70
Cdd:COG0508  17 GTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVIA 77
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 4-70 7.64e-06

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 40.57  E-value: 7.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490227283   4 VKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEII 70
Cdd:PRK06549  64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNPGDGLITIG 130
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 19-69 9.17e-06

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: 41.26  E-value: 9.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 490227283   19 AGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:TIGR01347  24 VGDTVKRDENIVEIETDKVVLEVPSPADGVLQEILFKEGDTVESGQVLAIL 74
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 10-66 2.06e-05

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 39.99  E-value: 2.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490227283  10 GVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVL 66
Cdd:PRK11854 219 VEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLI 275
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 10-66 3.87e-05

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 39.22  E-value: 3.87e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490227283  10 GVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVL 66
Cdd:PRK11854 118 VEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLI 174
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 12-72 4.53e-05

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 39.04  E-value: 4.53e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490227283  12 VDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEIIAE 72
Cdd:PRK11855 135 VIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVA 195
Biotinyl_lipoyl_domains cd06663
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 10-69 1.08e-04

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: 36.27  E-value: 1.08e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490227283 10 GVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:cd06663  14 GTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
PTZ00144 PTZ00144
dihydrolipoamide succinyltransferase; Provisional
 10-69 1.14e-04

dihydrolipoamide succinyltransferase; Provisional


Pssm-ID: 240289 [Multi-domain]  Cd Length: 418  Bit Score: 38.12  E-value: 1.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490227283  10 GVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PTZ00144  59 GTVVEWKKKVGDYVKEDEVICIIETDKVSVDIRAPASGVITKIFAEEGDTVEVGAPLSEI 118
PLN02983 PLN02983
biotin carboxyl carrier protein of acetyl-CoA carboxylase
 5-69 1.43e-04

biotin carboxyl carrier protein of acetyl-CoA carboxylase


Pssm-ID: 215533 [Multi-domain]  Cd Length: 274  Bit Score: 37.90  E-value: 1.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490227283   5 KSKVPGVVDEVKAsaGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PLN02983 210 RSPAPGEPPFVKV--GDKVQKGQVVCIIEAMKLMNEIEADQSGTIVEILAEDGKPVSVDTPLFVI 272
PLN02226 PLN02226
2-oxoglutarate dehydrogenase E2 component
 20-63 1.57e-04

2-oxoglutarate dehydrogenase E2 component


Pssm-ID: 177871 [Multi-domain]  Cd Length: 463  Bit Score: 37.81  E-value: 1.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490227283  20 GDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPG 63
Cdd:PLN02226 116 GERVQADEAIAQIETDKVTIDIASPASGVIQEFLVKEGDTVEPG 159
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 12-69 2.01e-04

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 37.49  E-value: 2.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490227283  12 VDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PRK11855  18 VIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVI 75
COG3608 COG3608
Predicted deacylase [General function prediction only];
4-67 2.07e-04

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 37.13  E-value: 2.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490227283   4 VKSKVPGVVdEVKASAGDKIEKGQVV--IVLEAMKMKMPVASPEAGIIktLALNTGDRVNPGMVLF 67
Cdd:COG3608  231 VRAPAGGLF-EPLVELGDRVKKGDVLgrITDPFGEEVEEVRAPVDGIV--IGRRTNPLVNPGDALF 293
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 39-69 2.31e-04

Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.


Pssm-ID: 435440 [Multi-domain]  Cd Length: 214  Bit Score: 37.10  E-value: 2.31e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 490227283   39 MPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:pfam16576 109 VTVYAPISGVVTELNVREGMYVQPGDTLFTI 139
PRK07051 PRK07051
biotin carboxyl carrier domain-containing protein;
1-69 5.99e-04

biotin carboxyl carrier domain-containing protein;


Pssm-ID: 180811 [Multi-domain]  Cd Length: 80  Bit Score: 34.60  E-value: 5.99e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490227283  1 MSEVKSKVPGVV------DE-VKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PRK07051  3 QHEIVSPLPGTFyrrpspDApPYVEVGDAVAAGDVVGLIEVMKQFTEVEAEAAGRVVEFLVEDGEPVEAGQVLARI 78
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 2-53 1.10e-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: 35.30  E-value: 1.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490227283   2 SEVKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLA 53
Cdd:COG0845   24 VEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQA 75
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
4-33 3.10e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 33.87  E-value: 3.10e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 490227283   4 VKSKVPGVVDEVKASAGDKIEKGQVVIVLE 33
Cdd:COG1566   48 VAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 4-33 3.37e-03

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 33.96  E-value: 3.37e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 490227283    4 VKSKVPGVVDEVKASAGDKIEKGQVVIVLE 33
Cdd:PRK12999 1116 ITAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
19-69 5.96e-03

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 33.27  E-value: 5.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490227283  19 AGDKIEKGQVVIVLEAMKMKMPVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:PRK05704  26 PGDAVKRDEVLVEIETDKVVLEVPAPAAGVLSEILAEEGDTVTVGQVLGRI 76
aceF PRK11854
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
 3-34 6.36e-03

pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated


Pssm-ID: 236999 [Multi-domain]  Cd Length: 633  Bit Score: 33.05  E-value: 6.36e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 490227283   3 EVKSKVPGVVDEVKASAGDKIEKGQVVIVLEA 34
Cdd:PRK11854  45 EVPSPQAGVVKEIKVKVGDKVETGALIMIFES 76
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
40-69 6.74e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 33.10  E-value: 6.74e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 490227283  40 PVASPEAGIIKTLALNTGDRVNPGMVLFEI 69
Cdd:COG1566   47 TVAAKVSGRVTEVLVKEGDRVKKGQVLARL 76
sucB TIGR01347
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ...
 3-50 8.01e-03

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: 32.78  E-value: 8.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 490227283    3 EVKSKVPGVVDEVKASAGDKIEKGQVVIVLEAMKMKMPVASPEAGIIK 50
Cdd:TIGR01347  45 EVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAAPPAKSGEEK 92
 
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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