Q9CHF2 (ACCD_LACLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	accD
Ordered Locus Names:	LL0779
ORF Names:	L018, L0180

Organism

Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)

Taxonomic identifier

272623 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO2 group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA By similarity. HAMAP MF_01395
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP MF_01395
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_01395
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP MF_01395
Subunit structure	Acetyl-CoA carboxylase is a 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 HAMAP MF_01395.
Sequence similarities	Belongs to the AccD/PCCB family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 288	288	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP MF_01395		PRO_0000389777
Regions
	Zinc finger	36 – 57	22	C4-type By similarity
Sites
	Metal binding	36	1	Zinc By similarity
	Metal binding	39	1	Zinc By similarity
	Metal binding	54	1	Zinc By similarity
	Metal binding	57	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9CHF2 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 765FA5189C0109D0	FASTA	288	31,770
	10 20 30 40 50 60 MALFQKKKYI KINPNRSIIE KQAEQPEVPD ELFAKCPACK HTIYQKDLGK NKVCPNCDYN 70 80 90 100 110 120 FRITAKERLA IVADKDSFVE MFTGIESKNP LDFPGYPEKL AATKARTGLD EAVITGTATI 130 140 150 160 170 180 KGQKTALAIM DSTFIMASMG TVVGEKLTRL FEYATTEKLP IIVFTASGGA RMQEGIMSLM 190 200 210 220 230 240 QMAKTSAAVK RHSNAGLFYI TVLTDPTTGG VTASFASLGD IILAEPQSLI GFAGRRVIEQ 250 260 270 280 TVRQTLPDDF QKAEFLLNHG FVDAIVKRTE LRQKLALLLE LHTEVENV

References

[1]

"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403." Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A. Genome Res. 11:731-753(2001) [PubMed: 11337471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IL1403.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005176 Genomic DNA. Translation: AAK04877.1.
PIR	C86722.
RefSeq	NP_266935.1. NC_002662.1.
3D structure databases
ProteinModelPortal	Q9CHF2.
SMR	Q9CHF2. Positions 29-286.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1114406.
GenomeReviews	Gene locus LL0779 in contig AE005176_GR.
KEGG	lla:L0180.
NMPDR	fig|272623.1.peg.799.
PATRIC	22293854. VBILacLac136773_0834.
Phylogenomic databases
HOGENOM	HBG285696.
OMA	FQTSEYL.
ProtClustDB	PRK05654.
Enzyme and pathway databases
BioCyc	LLAC272623:L0180-MONOMER.
Family and domain databases
HAMAP	MF_01395. AcetylCoA_CT_beta. [Tree]
InterPro	IPR000438. Acetyl_CoA_COase_Trfase_b_su. IPR000022. Carboxyl_trans. IPR011762. COA_CT_N. [Graphical view]
KO	K01963.
Pfam	PF01039. Carboxyl_trans. 1 hit. [Graphical view]
PRINTS	PR01070. ACCCTRFRASEB.
TIGRFAMs	TIGR00515. AccD. 1 hit.
PROSITE	PS50980. COA_CT_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCD_LACLA

Accession

Primary (citable) accession number: Q9CHF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2009
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program