FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA (By similarity).
CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA.
PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1 .
SUBUNIT: Acetyl-CoA carboxylase is an heterohexamer composed of biotin carboxyl carrier protein (accB), biotin carboxylase (accC) and two subunits each of ACCase subunit alpha (accA) and ACCase subunit beta (accD) (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the accA family.

Copyright

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Cross-references

Sequence databases

EMBL

CP000141; ABB15723.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_359987.1; -.

3D structure databases

ModBase

Q3ACZ7.

Enzyme and pathway databases

BioCyc

CHYD246194:CHY_1142-MON; -.

Ontologies

GO:0009317;	Cellular component: acetyl-CoA carboxylase complex (inferred from electronic annotation from InterPro).
GO:0003989;	Molecular function: acetyl-CoA carboxylase activity (inferred from electronic annotation from HAMAP).
GO:0006633;	Biological process: fatty acid biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00823; -; 1.
PBIL [Tree]

InterPro

IPR001095; Acetyl_CoA_COase_a_su.
IPR011763; COA_CT_C.
Graphical view of domain structure.

PANTHER

PTHR22855:SF3; Ac-CoA_carboxylA; 1.

Pfam

PF03255; ACCA; 1.
Pfam graphical view of domain structure.

PRINTS

PR01069; ACCCTRFRASEA.

TIGRFAMs

TIGR00513; accA; 1.

PROSITE

PS50989; COA_CT_CTER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q3ACZ7.

Genome annotation databases

GeneID

3727831; -.

GenomeReviews

CP000141_GR; CHY_1142.

KEGG

chy:CHY_1142; -.

NMPDR

fig|246194.3.peg.1188; -.

TIGR

CHY_1142; -.

Phylogenomic databases

HOGENOM

Q3ACZ7; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Fatty acid biosynthesis; Ligase; Lipid synthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 323`	`323`		`Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha.`	`PRO_0000223749`

Sequence information

Length: 323 AA [This is the length of the unprocessed precursor]

Molecular weight: 35820 Da [This is the MW of the unprocessed precursor]

CRC64: 5B1AAC33062CF764 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MANFLFEFEK PLVELENKIS DLKKFAEEKN IDVSRELELL SAKAQQLAKE IYQNLTPWQR 

        70         80         90        100        110        120 
VLLARHPERP NTRDYINYLC DDFIELKGDR RFGDDPAMIG GIGIIENIPV TIVGNLKGKD 

       130        140        150        160        170        180 
TKENIMRNFG MAHPEGYRKA IRLFKQAEKF GRPVLTFIDT PGAFCGIGAE ERGQFQAIAE 

       190        200        210        220        230        240 
AIATLISLKT PVLAVITGEG GSGGALALAA GDKLLMLENA VFSVIAPESF AAILWKDSSR 

       250        260        270        280        290        300 
AQEASELLKL TSEHLLEFGL IDGIIPEPLG GAHRNPAETL KAVKEEVVKN LQILKETPVE 

       310        320 
ELLRRRYQRY RYIGSGIVEG GVS

Q3ACZ7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools