Reviewed, UniProtKB/Swiss-Prot P0A9Q5 (ACCD_ECOLI)

Names and origin

Protein names

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

Gene names

Name:	accD
Synonyms:	dedB, usg
Ordered Locus Names:	b2316, JW2313

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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. Ref.8
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP MF_01395
Cofactor	Binds 1 zinc ion per subunit. 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). HAMAP MF_01395
Subcellular location	Cytoplasm. 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	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
accA	P0ABD5	1	EBI-542064,EBI-542031

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 304	304	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta HAMAP MF_01395		PRO_0000199770
Regions
	Zinc finger	27 – 49	23	C4-type Probable
Sites
	Metal binding	27	1	Zinc HAMAP MF_01395
	Metal binding	30	1	Zinc HAMAP MF_01395
	Metal binding	46	1	Zinc HAMAP MF_01395
	Metal binding	49	1	Zinc HAMAP MF_01395
Experimental info
	Sequence conflict	76 – 77	2	EL → SV in AAA23965. Ref.2
	Sequence conflict	225 – 239	15	IGFAG…QTVRE → MALPVRVLSNRPFAK in AAA23807. Ref.1
	Sequence conflict	225 – 239	15	IGFAG…QTVRE → MALPVRVLSNRPFAK in AAA23801. Ref.1
	Sequence conflict	226 – 235	10	GFAGPRVIEQ → ALPVRVLSNR in AAA23965. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P0A9Q5-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 401FEC94D728F3CB	FASTA	304	33,322
	10 20 30 40 50 60 MSWIERIKSN ITPTRKASIP EGVWTKCDSC GQVLYRAELE RNLEVCPKCD HHMRMTARNR 70 80 90 100 110 120 LHSLLDEGSL VELGSELEPK DVLKFRDSKK YKDRLASAQK ETGEKDALVV MKGTLYGMPV 130 140 150 160 170 180 VAAAFEFAFM GGSMGSVVGA RFVRAVEQAL EDNCPLICFS ASGGARMQEA LMSLMQMAKT 190 200 210 220 230 240 SAALAKMQER GLPYISVLTD PTMGGVSASF AMLGDLNIAE PKALIGFAGP RVIEQTVREK 250 260 270 280 290 300 LPPGFQRSEF LIEKGAIDMI VRRPEMRLKL ASILAKLMNL PAPNPEAPRE GVVVPPVPDQ EPEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene." Bognar A.L., Osborne C., Shane B. J. Biol. Chem. 262:12337-12343(1987) [PubMed: 3040739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons." Nonet M.L., Marvel C.C., Tolan D.R. J. Biol. Chem. 262:12209-12217(1987) [PubMed: 3040734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis." Li S.-J., Cronan J.E. Jr. J. Bacteriol. 175:332-340(1993) [PubMed: 7678242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
[7]	"An essential gene of Escherichia coli that has sequence similarity to a chloroplast gene of unknown function." Nagano Y., Matsuno R., Sasaki Y. Mol. Gen. Genet. 228:62-64(1991) [PubMed: 1886618] [Abstract] Cited for: SIMILARITY TO ZFPA.
[8]	"The dedB (usg) open reading frame of Escherichia coli encodes a subunit of acetyl-coenzyme A carboxylase." Li S.-J., Rock C.O., Cronan J.E. Jr. J. Bacteriol. 174:5755-5757(1992) [PubMed: 1355086] [Abstract] Cited for: FUNCTION.
[9]	"The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme." Bilder P., Lightle S., Bainbridge G., Ohren J., Finzel B., Sun F., Holley S., Al-Kassim L., Spessard C., Melnick M., Newcomer M., Waldrop G.L. Biochemistry 45:1712-1722(2006) [PubMed: 16460018] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), ZINC-FINGER.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M32445 Genomic DNA. Translation: AAA23807.1.
J02808 Genomic DNA. Translation: AAA23801.1.
M68934 Genomic DNA. Translation: AAA23965.1.
U00096 Genomic DNA. Translation: AAC75376.1.
AP009048 Genomic DNA. Translation: BAA16173.1.
S53037 mRNA. Translation: AAB24894.2.

PIR

XMECBD. B65004.

RefSeq

AP_002916.1.
NP_416819.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F9Y	X-ray	3.20	B	1-304	[»]

SMR

P0A9Q5. Positions 23-285.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A9Q5. 18 interactions.

Genome annotation databases

GeneID

946796.

GenomeReviews

Gene locus JW2313 in contig AP009048_GR.
Gene locus b2316 in contig U00096_GR.

KEGG

ecj:JW2313.
eco:b2316.

Organism-specific databases

EchoBASE

EB0213.

EcoGene

EG10217. accD.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A9Q5.

OMA

P0A9Q5. ASLGDYN.

Enzyme and pathway databases

BioCyc

EcoCyc:CARBOXYL-TRANSFERASE-BETA-MON.
MetaCyc:CARBOXYL-TRANSFERASE-BETA-MON.

Family and domain databases

HAMAP

MF_01395.
[Tree]

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_ECOLI

Accession

Primary (citable) accession number: P0A9Q5
Secondary accession number(s): P08193, P76937, P78251

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	July 19, 2005
Last modified:	June 16, 2009
This is version 36 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)