Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

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P0ABD5 (ACCA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Gene names

Name:	accA
Ordered Locus Names:	b0185, JW0180

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO₂ group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. HAMAP-Rule MF_00823
Catalytic activity	ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA. HAMAP-Rule MF_00823
Enzyme regulation	Competitively inhibited by pyrrolidine dione antibiotic moiramide B (CPD1). Ref.10
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP-Rule MF_00823
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-Rule MF_00823.
Sequence similarities	Belongs to the AccA family.
Biophysicochemical properties	Kinetic parameters: K_M=100 µM for malonyl-CoA Ref.10 K_M=10 mM for biocytin

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	long-chain fatty acid biosynthetic process Non-traceable author statement PubMed 18156466. Source: EcoliWiki malonyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	acetate CoA-transferase complex Inferred from direct assay Ref.1. Source: EcoCyc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
accD	P0A9Q5	5	EBI-542031,EBI-542064

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.9

Chain

2 – 319

318

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP-Rule MF_00823

PRO_0000146774

Secondary structure

319

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0ABD5 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A810DE891CEA2B4F
Show »

FASTA

319

35,242

        10         20         30         40         50         60 
MSLNFLDFEQ PIAELEAKID SLTAVSRQDE KLDINIDEEV HRLREKSVEL TRKIFADLGA 

        70         80         90        100        110        120 
WQIAQLARHP QRPYTLDYVR LAFDEFDELA GDRAYADDKA IVGGIARLDG RPVMIIGHQK 

       130        140        150        160        170        180 
GRETKEKIRR NFGMPAPEGY RKALRLMQMA ERFKMPIITF IDTPGAYPGV GAEERGQSEA 

       190        200        210        220        230        240 
IARNLREMSR LGVPVVCTVI GEGGSGGALA IGVGDKVNML QYSTYSVISP EGCASILWKS 

       250        260        270        280        290        300 
ADKAPLAAEA MGIIAPRLKE LKLIDSIIPE PLGGAHRNPE AMAASLKAQL LADLADLDVL 

       310 
STEDLKNRRY QRLMSYGYA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase." Li S.-J., Cronan J.E. Jr. J. Biol. Chem. 267:16841-16847(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme." Yamamoto Y., Miwa Y., Miyoshi K., Furuyama J., Ohmori H. Genes Genet. Syst. 72:167-172(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 24. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Characterization of a second lysine decarboxylase isolated from Escherichia coli." Kikuchi Y., Kojima H., Tanaka T., Takatsuka Y., Kamio Y. J. Bacteriol. 179:4486-4492(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-319. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Sequence analysis of the Escherichia coli dnaE gene." Tomasiewicz H.G., McHenry C.S. J. Bacteriol. 169:5735-5744(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[9]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[10]	"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] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M96394 Genomic DNA. Translation: AAA70370.1.
D49445 Genomic DNA. Translation: BAA08425.1.
U70214 Genomic DNA. Translation: AAB08614.1.
U00096 Genomic DNA. Translation: AAC73296.1.
AP009048 Genomic DNA. Translation: BAA77860.2.
D87518 Genomic DNA. Translation: BAA21655.1.
M19334 Genomic DNA. No translation available.

PIR

A43452.

RefSeq

NP_414727.1. NC_000913.2.
YP_488487.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F9Y	X-ray	3.20	A	1-319	[»]

ProteinModelPortal

P0ABD5.

SMR

P0ABD5. Positions 4-319.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35897N.

IntAct

P0ABD5. 27 interactions.

MINT

MINT-1228651.

STRING

511145.b0185.

Proteomic databases

PaxDb

P0ABD5.

PRIDE

P0ABD5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73296; AAC73296; b0185.
BAA77860; BAA77860; BAA77860.

GeneID

12930759.
944895.

KEGG

ecj:Y75_p0181.
eco:b0185.

PATRIC

32115481. VBIEscCol129921_0192.

Organism-specific databases

EchoBASE

EB1600.

EcoGene

EG11647. accA.

Phylogenomic databases

eggNOG

COG0825.

HOGENOM

HOG000273832.

K01962.

OMA

QLTKDIY.

ProtClustDB

PRK05724.

Enzyme and pathway databases

BioCyc

EcoCyc:CARBOXYL-TRANSFERASE-ALPHA-MONOMER.
ECOL316407:JW0180-MONOMER.
MetaCyc:CARBOXYL-TRANSFERASE-ALPHA-MONOMER.

SABIO-RK

P0ABD5.

UniPathway

UPA00655; UER00711.

Gene expression databases

Genevestigator

P0ABD5.

Family and domain databases

HAMAP

MF_00823. AcetylCoA_CT_alpha.

InterPro

IPR001095. Acetyl_CoA_COase_a_su.
IPR011763. COA_CT_C.
[Graphical view]

PANTHER

PTHR22855:SF3. PTHR22855:SF3. 1 hit.

Pfam

PF03255. ACCA. 1 hit.
[Graphical view]

PRINTS

PR01069. ACCCTRFRASEA.

TIGRFAMs

TIGR00513. accA. 1 hit.

PROSITE

PS50989. COA_CT_CTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0ABD5.

Entry information

Entry name

ACCA_ECOLI

Accession

Primary (citable) accession number: P0ABD5
Secondary accession number(s): P30867

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents