Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta

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P0A9Q6 (ACCD_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. History...

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

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·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 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:	Z3578, ECs3200

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	304 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 MF_01395
Catalytic activity	ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA. HAMAP MF_01395
Cofactor	Binds 1 zinc ion per subunit By similarity. 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) By similarity.
Subcellular location	Cytoplasm By similarity 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	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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_0000199771

Regions

Zinc finger

27 – 49

C4-type Potential

Sites

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0A9Q6 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 401FEC94D728F3CB
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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

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References

[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG57445.1. BA000007 Genomic DNA. Translation: BAB36623.1.
PIR	A85873. H91028.
RefSeq	NP_288890.1. NC_002655.2. NP_311227.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0A9Q6.
SMR	P0A9Q6. Positions 23-285.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1234633.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000027824; EBESCP00000026717; EBESCG00000026876. EBESCT00000057858; EBESCP00000055686; EBESCG00000056906.
GeneID	916908. 957472.
GenomeReviews	Gene locus Z3578 in contig AE005174_GR. Gene locus ECs3200 in contig BA000007_GR.
KEGG	ece:Z3578. ecs:ECs3200.
PATRIC	18355790. VBIEscCol44059_3096.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000010915.
HOGENOM	HBG285696.
OMA	FQTSEYL.
ProtClustDB	PRK05654.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3200-MONOMER.
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_ECO57

Accession

Primary (citable) accession number: P0A9Q6
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 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents