Q2JSX0 (ACCD_SYNJA) 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:	CYA_2104

Organism

Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime) [Complete proteome] [HAMAP]

Taxonomic identifier

321327 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus

Protein attributes

Sequence length	314 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-Rule MF_01395
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP-Rule MF_01395
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP-Rule 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.
Sequence similarities	Belongs to the AccD/PCCB family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP malonyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 zinc ion binding 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 – 314	314	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP-Rule MF_01395		PRO_0000359078
Regions
	Zinc finger	41 – 63	23	C4-type Potential
Sites
	Metal binding	41	1	Zinc By similarity
	Metal binding	44	1	Zinc By similarity
	Metal binding	60	1	Zinc By similarity
	Metal binding	63	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2JSX0 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: DF1568A7C06196D3	FASTA	314	34,785
	10 20 30 40 50 60 MSLLDWFAER RKQTSLNLTG SSPFDKERQV REIADGLWQK CPACDALTYT KDLQQNWQVC 70 80 90 100 110 120 PSCGYHHRIT APQRLQQLLD PGSWQPLDEH LAPTDPLHFF DQKPYAERLA SYQERTQLKD 130 140 150 160 170 180 AVLTGLGSLE GIPVAMGVMD FRFMGGSMGS VVGEKITRLT ERATRDHLPL VIFSASGGAR 190 200 210 220 230 240 MQEGILSLMQ MAKTAAALQR HREAGQLFIS VLTHPTYGGV TASFAMLGDL ILAEPGAQVG 250 260 270 280 290 300 FAGPNVIEQT IGKGKLPEGF QTAEYLLAHG LIDAIVPRTE LRRRLAQLLA MHRPRLRMSL 310 PALEPTYALD PARI

References

[1]

"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses." Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F. ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JA-3-3Ab.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000239 Genomic DNA. Translation: ABD00244.1.
RefSeq	YP_475507.1. NC_007775.1.
3D structure databases
ProteinModelPortal	Q2JSX0.
SMR	Q2JSX0. Positions 37-293.
ModBase	Search...
Protein-protein interaction databases
STRING	321327.CYA_2104.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD00244; ABD00244; CYA_2104.
GeneID	3899151.
KEGG	cya:CYA_2104.
PATRIC	23812480. VBISynSp90045_2075.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0777.
HOGENOM	HOG000021671.
KO	K01963.
OMA	GLWIKCP.
ProtClustDB	PRK05654.
Enzyme and pathway databases
UniPathway	UPA00655; UER00711.
Family and domain databases
HAMAP	MF_01395. AcetylCoA_CT_beta.
InterPro	IPR000438. Acetyl_CoA_COase_Trfase_b_su. IPR000022. Carboxyl_trans. IPR011762. COA_CT_N. [Graphical view]
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_SYNJA

Accession

Primary (citable) accession number: Q2JSX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program