P0A9Q5 (ACCD_ECOLI) 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
Synonyms:	dedB, usg
Ordered Locus Names:	b2316, JW2313

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
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 Ref.10 Controls translation of mRNA for both itself and the alpha-subunit (accA) by binding to a probable hairpin in the 5' of the mRNA. Binding to mRNA inhibits translation; this is partially relieved by acetyl-CoA. Increasing amounts of mRNA also inhibit enzyme activity. Ref.8 Ref.10
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP MF_01395
Cofactor	Binds 1 zinc ion per subunit. The zinc is involved in both translation regulation via mRNA-binding and catalysis. Ref.10
Enzyme regulation	Competitively inhibited by pyrrolidine dione antibiotic moiramide B (CPD1). Ref.9
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).
Subcellular location	Cytoplasm HAMAP MF_01395.
Sequence similarities	Belongs to the AccD/PCCB family.
Biophysicochemical properties	Kinetic parameters: KM=40.0 µM for malonyl-CoA Ref.9 Ref.10 KM=11.4 mM for biocytin

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis Translation regulation
Cellular component	Cytoplasm
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from mutant phenotype. Source: EcoCyc negative regulation of translation Inferred from direct assay Ref.10. Source: EcoCyc
Cellular component	acetate CoA-transferase complex Inferred from direct assay. Source: EcoCyc cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from mutant phenotype Ref.10. Source: EcoCyc acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: EC mRNA binding Inferred from direct assay Ref.10. Source: EcoCyc protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from direct assay Ref.11Ref.10. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
accA	P0ABD5	5	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

Metal binding

30

1

Zinc

Metal binding

46

1

Zinc

Metal binding

49

1

Zinc

Experimental info

Mutagenesis

27

1

C → A: Vmax decreases 9-fold. Ref.10

Mutagenesis

30

1

C → A: Vmax decreases 140-fold. Loss of nucleic acid-binding. Ref.10

Mutagenesis

46

1

C → A: Vmax decreases 11-fold. Ref.10

Mutagenesis

49

1

C → A: Vmax decreases 8-fold. Ref.10

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

Secondary structure

1

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304

Helix Strand Turn

Details...

Turn

36 – 44

9

Turn

47 – 49

3

Helix

57 – 64

8

Helix

88 – 90

3

Beta strand

106 – 112

7

Beta strand

121 – 125

5

Helix

141 – 152

12

Beta strand

156 – 162

7

Helix

167 – 170

4

Helix

171 – 189

19

Beta strand

194 – 202

9

Turn

207 – 209

3

Helix

210 – 212

3

Beta strand

216 – 219

4

Helix

231 – 237

7

Helix

248 – 251

4

Beta strand

258 – 260

3

Helix

263 – 277

15

Sequences

	Sequence		Length	Mass (Da)
	P0A9Q5 [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]	"Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity." Freiberg C., Brunner N.A., Schiffer G., Lampe T., Pohlmann J., Brands M., Raabe M., Haebich D., Ziegelbauer K. J. Biol. Chem. 279:26066-26073(2004) [PubMed: 15066985] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[10]	"A tale of two functions: enzymatic activity and translational repression by carboxyltransferase." Meades G. Jr., Benson B.K., Grove A., Waldrop G.L. Nucleic Acids Res. 38:1217-1227(2010) [PubMed: 19965770] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, RNA-BINDING, SUGGESTED MECHANISM OF TRANSLATIONAL REGULATION, MUTAGENESIS OF CYS-27; CYS-30; CYS-46 AND CYS-49.
[11]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

NP_416819.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P0A9Q5.

SMR

P0A9Q5. Positions 23-285.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35878N.

IntAct

P0A9Q5. 20 interactions.

MINT

MINT-1234646.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000000402; EBESCP00000000402; EBESCG00000000332.
EBESCT00000016593; EBESCP00000015884; EBESCG00000015652.

GeneID

946796.

GenomeReviews

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

KEGG

ecj:JW2313.
eco:b2316.

PATRIC

32120003. VBIEscCol129921_2411.

Organism-specific databases

EchoBASE

EB0213.

EcoGene

EG10217. accD.

Phylogenomic databases

eggNOG

COG0777.

GeneTree

EBGT00050000010915.

HOGENOM

HBG285696.

OMA

FQTSEYL.

PhylomeDB

P0A9Q5.

ProtClustDB

PRK05654.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0A9Q5.

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_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:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program