Biotin attachment domain

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1dczA:55-122 1dd2A:55-122 1o78A:55-122 1k67B:81-155 2bdoA:81-155 1k69B:81-155 3bdoA:81-155 1bdo :81-155 1a6x :81-155 1y8pB:186-260 1y8nB:186-260 1fyc :186-260 1y8oB:186-260 1ghk :3-76 1ghj :3-76 1gjxA:4-76 1qjoA:207-278 1iyu :3-73 1iyv :3-73 1lac :3-76 1lab :3-76 1k8mA:65-138 1k8oA:65-138

Biotin/lipoyl attachment domain
Biotin/lipoyl attachment domain
Identifiers
Symbol	Biotin_lipoyl
Pfam	PF00364
InterPro	IPR000089
PROSITE	PDOC00168
SCOP2	1lab / SCOPe / SUPFAM
CDD	cd06663
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1dczA:55-122 1dd2A:55-122 1o78A:55-122 1k67B:81-155 2bdoA:81-155 1k69B:81-155 3bdoA:81-155 1bdo :81-155 1a6x :81-155 1y8pB:186-260 1y8nB:186-260 1fyc :186-260 1y8oB:186-260 1ghk :3-76 1ghj :3-76 1gjxA:4-76 1qjoA:207-278 1iyu :3-73 1iyv :3-73 1lac :3-76 1lab :3-76 1k8mA:65-138 1k8oA:65-138

Biotin/lipoyl attachment domain has a conserved lysine residue that binds biotin or lipoic acid. Biotin plays a catalytic role in some carboxyl transfer reactions and is covalently attached, via an amide bond, to a lysine residue in enzymes requiring this coenzyme.^[1] Lipoamide acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via an amide linkage to a lysine group.^[2] The lipoic acid cofactor is found in a variety of proteins.

Human proteins containing this domain

ACACA; ACACB; DBT; DLAT; DLST; DLSTP; MCCC1; PC; PCCA; PDHX;

References

^ Kumar GK, Shenoy BC, Wood HG, Samols D, Xie Y, Park VL, Beegen H (1992). "The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis". J. Biol. Chem. 267 (26): 18407–18412. doi:10.1016/S0021-9258(19)36977-7. PMID 1526981.
^ Guest JR, Russell GC (1991). "Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme". Biochim. Biophys. Acta. 1076 (2): 225–232. doi:10.1016/0167-4838(91)90271-z. PMID 1825611.

This article incorporates text from the public domain Pfam and InterPro: IPR000089

[PUB00002740-1] Kumar GK, Shenoy BC, Wood HG, Samols D, Xie Y, Park VL, Beegen H (1992). "The importance of methionine residues for the catalysis of the biotin enzyme, transcarboxylase. Analysis by site-directed mutagenesis". J. Biol. Chem. 267 (26): 18407–18412. doi:10.1016/S0021-9258(19)36977-7. PMID 1526981.

[PUB00000614-2] Guest JR, Russell GC (1991). "Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme". Biochim. Biophys. Acta. 1076 (2): 225–232. doi:10.1016/0167-4838(91)90271-z. PMID 1825611.

[1]

[2]