Reviewed, UniProtKB/Swiss-Prot Q9PI62 (ACCA_CAMJE)

Names and origin

Protein names

Recommended name:
    Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
      Short name=Acetyl-CoA carboxylase carboxyltransferase subunit alpha
      Short name=ACCase subunit alpha
    EC=6.4.1.2

Gene names

Name:	accA
Ordered Locus Names:	Cj0443

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

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 CO2 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. HAMAP MF_00823
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP MF_00823
Subunit structure	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.
Sequence similarities	Belongs to the accA family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 312	312	Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823		PRO_0000223747

Sequences

	Sequence		Length	Mass (Da)
	Q9PI62-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 8DDE111C042DADA4	FASTA	312	34,253
	10 20 30 40 50 60 MASYLDFEKN IQQIDEDIIN AQIKGDTEAV SILKKNLEKE ISKTYKNLSD FQRLQLARHP 70 80 90 100 110 120 DRPYALDYIE LILNDAHEIH GDRAFRDDPA IVCFMGYLGE KKIIVIGEQK GRGTKDKIAR 130 140 150 160 170 180 NFGMPHPEGY RKALRVAGLA EKFQIPILFL IDTPGAYPGI GAEERGQSEA IARNLYELSD 190 200 210 220 230 240 LKIPTIAIVI GEGGSGGALA IGVADKLAMM KNSVFSVISP EGCAAILWND PAKSEAATKA 250 260 270 280 290 300 MKVTADDLKS QGLIDDVIDE PTNGAHRNKE AAAVAIADYV KKSLNELENI DVRELSANRM 310 QKILKLGAYQ EA

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL111168 Genomic DNA. Translation: CAL34593.1.
PIR	A81389.
RefSeq	YP_002343880.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PI62. 37 interactions.
Genome annotation databases
GeneID	904768.
GenomeReviews	Gene locus Cj0443 in contig AL111168_GR.
KEGG	cje:Cj0443.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q9PI62. HSVYTVA.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0443-MON.
BRENDA	6.4.1.2. 255835.
Family and domain databases
HAMAP	MF_00823. [Tree]
InterPro	IPR001095. Acetyl_CoA_COase_a_su. IPR011763. COA_CT_C. [Graphical view]
PANTHER	PTHR22855:SF3. Ac-CoA_carboxylA. 1 hit.
Pfam	PF03255. ACCA. 1 hit. [Graphical view]
PRINTS	PR01069. ACCCTRFRASEA.
TIGRFAMs	TIGR00513. accA. 1 hit.
PROSITE	PS50989. COA_CT_CTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCA_CAMJE

Accession

Primary (citable) accession number: Q9PI62
Secondary accession number(s): Q0PB67

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)