Reviewed, UniProtKB/Swiss-Prot P43873 (ACCC_HAEIN)

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:	HI0972

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	448 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
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 – 448	448	Biotin carboxylase		PRO_0000146793
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)
	P43873-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 2B497E2A31ED96D1	FASTA	448	49,108
	10 20 30 40 50 60 MLEKVVIANR GEIALRILRA CKELGIKTVA VHSTADRDLK HVLLADETIC IGPAPSAKSY 70 80 90 100 110 120 LNIPAIIAAA EVTGADAIHP GYGFLSENAD FAEQVERSGF TFIGPTADVI RLMGDKVSAI 130 140 150 160 170 180 KAMKKAGVPC VPGSDGPVSN DIAKNKEIAK RIGYPIIIKA SGGGGGRGMR VVRSEDALEE 190 200 210 220 230 240 SIAMTKAEAK AAFNNDMVYM EKYLENPRHV EIQVLADTHG NAVYLAERDC SMQRRHQKVV 250 260 270 280 290 300 EEAPAPGITE EVRRDIGSRC ANACVEIGYR GAGTFEFLYE NGEFYFIEMN TRIQVEHPVT 310 320 330 340 350 360 EMITGVDLVK EQLRIAAGLP ISFKQEDIKV KGHAMECRIN AEDPKTFLPS PGKVNHLHSP 370 380 390 400 410 420 GGLGVRWDSH VYGGYTVPPH YDSMIAKLIT YGDTREVAIR RMQNALSETI IDGIKTNIPL 430 440 HELILEDENF QKGGTNIHYL EKKLGMNE

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC22632.1.
PIR	F64105.
RefSeq	NP_439133.1.
3D structure databases
HSSP	HSSP built from PDB template 1BNC based on UniProtKB P24182.
SMR	P43873. Positions 2-446.
ModBase	Search...
Genome annotation databases
GeneID	949398.
GenomeReviews	Gene locus HI0972 in contig L42023_GR.
KEGG	hin:HI0972.
NMPDR	fig|71421.1.peg.938.
TIGR	HI0972.
Phylogenomic databases
HOGENOM	P43873.
OMA	HIRLMGD.
Enzyme and pathway databases
BioCyc	HINF71421:HI_0972-MON.
BRENDA	6.3.4.14. 109. 6.4.1.2. 109.
Family and domain databases
InterPro	IPR004549. Acetyl_CoA_COase_biotin_COase. IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR011764. BC. IPR005482. Biotin_COase_C. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005481. CarbamoylP_synth_lsu_N. IPR013817. Pre-ATP_grasp. [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]
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_HAEIN

Accession

Primary (citable) accession number: P43873

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 73 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)