Reviewed, UniProtKB/Swiss-Prot Q8X9B6 (ACCC_ECO57)

Names and origin

Protein names

Recommended name:
    Biotin carboxylase
    EC=6.3.4.14
Alternative name(s):
    Acetyl-CoA carboxylase subunit A
      Short name=ACC
    EC=6.4.1.2

Gene names

Name:	accC
Ordered Locus Names:	Z4616, ECs4128

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	This 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.
Catalytic activity	ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein. ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subunit structure	Acetyl-CoA carboxylase is an heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex By similarity.
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain.

Ontologies

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 449	449	Biotin carboxylase		PRO_0000146792
Regions
	Domain	1 – 445	445	Biotin carboxylation
	Domain	120 – 317	198	ATP-grasp
Sites
	Active site	292	1	Potential
	Binding site	116	1	ATP By similarity
	Binding site	201	1	ATP By similarity
	Binding site	236	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8X9B6-1 [UniParc]. Last modified March 5, 2002. Version 1. Checksum: BC5716323F6233ED	FASTA	449	49,337
	10 20 30 40 50 60 MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY 70 80 90 100 110 120 LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI 130 140 150 160 170 180 AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ 190 200 210 220 230 240 SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NSIYLAERDC SMQRRHQKVV 250 260 270 280 290 300 EEAPAPGITP ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT 310 320 330 340 350 360 EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS PGKITRFHAP 370 380 390 400 410 420 GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA RMKNALQELI IDGIKTNVDL 430 440 QIRIMNDENF QHGGTNIHYL EKKLGLQEK

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG58384.1. BA000007 Genomic DNA. Translation: BAB37551.1.
PIR	D85990. H91144.
RefSeq	NP_289824.1. NP_312155.1.
3D structure databases
SMR	Q8X9B6. Positions 1-447.
ModBase	Search...
Genome annotation databases
GeneID	916024. 958693.
GenomeReviews	Gene locus Z4616 in contig AE005174_GR. Gene locus ECs4128 in contig BA000007_GR.
KEGG	ece:Z4616. ecs:ECs4128.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG535236.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS4128-MONOMER.
Family and domain databases
InterPro	IPR004549. Acetyl_CoA_COase_biotin_COase. IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR011764. Biotin_carboxylation_dom. IPR005482. Biotin_COase_C. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR011054. Rudment_hybrid_motif. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	PF02785. Biotin_carb_C. 1 hit. PF00289. CPSase_L_chain. 1 hit. PF02786. CPSase_L_D2. 1 hit. [Graphical view]
SMART	SM00878. Biotin_carb_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00514. accC. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS50979. BC. 1 hit. PS00866. CPSASE_1. 1 hit. PS00867. CPSASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCC_ECO57

Accession

Primary (citable) accession number: Q8X9B6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	March 5, 2002
Last modified:	February 9, 2010
This is version 61 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)