Q7CRB7 (ACCD_STRR6) 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:	spr0386

Organism

Streptococcus pneumoniae (strain ATCC BAA-255 / R6) [Reference proteome] [HAMAP]

Taxonomic identifier

171101 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus pneumoniae

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-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 Reference 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 – 288	288	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP-Rule MF_01395		PRO_0000389872
Regions
	Zinc finger	37 – 58	22	C4-type By similarity
Sites
	Metal binding	37	1	Zinc By similarity
	Metal binding	40	1	Zinc By similarity
	Metal binding	55	1	Zinc By similarity
	Metal binding	58	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7CRB7 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 42C29A8FC7BF21D5	FASTA	288	31,786
	10 20 30 40 50 60 MALFSKKDKY IRINPNRSVR EKPQAKPEVP DELFSQCPGC KHTIYQKDLG SERICPHCSY 70 80 90 100 110 120 TFRISAQERL ALTIDMGTFK ELFTGIESKD PLHFPGYQKK LASMREKTGL HEAVVTGTAL 130 140 150 160 170 180 IKGQTVALGI MDSNFIMASM GTVVGEKITR LFEYATVEKL PVVLFTASGG ARMQEGIMSL 190 200 210 220 230 240 MQMAKISAAV KRHSNAGLFY LTILTDPTTG GVTASFAMEG DIILAEPQSL VGFAGRRVIE 250 260 270 280 NTVRESLPED FQKAEFLLEH GFVDAIVKRR DLPDTIASLV RLHGGSPR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A triclosan-resistant bacterial enzyme." Heath R.J., Rock C.O. Nature 406:145-146(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome of the bacterium Streptococcus pneumoniae strain R6." Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., Lee L.N. , Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., Glass J.I. J. Bacteriol. 183:5709-5717(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-255 / R6.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF197933 Genomic DNA. Translation: AAF98280.1. AE007317 Genomic DNA. Translation: AAK99190.1.
RefSeq	NP_357980.1. NC_003098.1.
3D structure databases
ProteinModelPortal	Q7CRB7.
SMR	Q7CRB7. Positions 30-287.
ModBase	Search...
Protein-protein interaction databases
STRING	171101.spr0386.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK99190; AAK99190; spr0386.
GeneID	934669.
KEGG	spr:spr0386.
PATRIC	19700611. VBIStrPne107296_0427.
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_STRR6

Accession

Primary (citable) accession number: Q7CRB7
Secondary accession number(s): Q7D4F5, Q9FBB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2009
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program