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UniProtKB/Swiss-Prot entry Q8U9U5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information

Entry name

ACCA_AGRT5

Primary accession number

Q8U9U5

Secondary accession number

Q7CSY5

Integrated into Swiss-Prot on

February 21, 2006

Sequence was last modified on

June 1, 2002 (Sequence version 1)

Annotations were last modified on

November 25, 2008 (Entry version 37)

Name and origin of the protein

Protein name

Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha

Synonyms

Acetyl-CoA carboxylase carboxyltransferase subunit alpha
ACCase subunit alpha
EC 6.4.1.2

Gene name

	Name:	accA
	OrderedLocusNames:	Atu3630
	ORFNames:	AGR_L_2394

From

Agrobacterium tumefaciens (strain C58 / ATCC 33970)

[TaxID: 176299]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1066804; PubMed=11743193 [NCBI, ExPASy, EBI, Israel, Japan]
Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W.;
"The genome of the natural genetic engineer Agrobacterium tumefaciens C58.";
Science 294:2317-2323(2001).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1066803; PubMed=11743194 [NCBI, ExPASy, EBI, Israel, Japan]
Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58.";
Science 294:2323-2328(2001).

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 CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA (By similarity).
CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA.
PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1 .
SUBUNIT: Acetyl-CoA carboxylase is an 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).
SIMILARITY: Belongs to the accA family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE007870; AAK89767.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

AD3003; AD3003.
E98280; E98280.

RefSeq

NP_356982.1; -.

3D structure databases

ModBase

Q8U9U5.

Ontologies

GO:0009317;	Cellular component: acetyl-CoA carboxylase complex (inferred from electronic annotation from InterPro).
GO:0003989;	Molecular function: acetyl-CoA carboxylase activity (inferred from electronic annotation from HAMAP).
GO:0006633;	Biological process: fatty acid biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00823; -; 1.
PBIL [Tree]

InterPro

IPR001095; Acetyl_CoA_COase_a_su.
IPR011763; COA_CT_C.
Graphical view of domain structure.

PANTHER

PTHR22855:SF3; Ac-CoA_carboxylA; 1.

Pfam

PF03255; ACCA; 1.
Pfam graphical view of domain structure.

PRINTS

PR01069; ACCCTRFRASEA.

TIGRFAMs

TIGR00513; accA; 1.

PROSITE

PS50989; COA_CT_CTER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8U9U5.

Genome annotation databases

GeneID

1135504; -.

GenomeReviews

AE007870_GR; Atu3630.

KEGG

atc:AGR_L_2394; -.
atu:Atu3630; -.

Phylogenomic databases

HOGENOM

Q8U9U5; -.

Genome annotation databases

CMR

Q8U9U5; Atu3630.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Fatty acid biosynthesis; Ligase; Lipid synthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 317`	`317`		`Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha.`	`PRO_0000223724`

Sequence information

Length: 317 AA [This is the length of the unprocessed precursor]

Molecular weight: 34542 Da [This is the MW of the unprocessed precursor]

CRC64: F226EF4717846846 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHNYLDFEKP ISDLEGKIIE LKKLADEDES IDTSEEINRL ESRVNDAMQD IYSKLNAWQK 

        70         80         90        100        110        120 
TQVARHPQRP HFVDYAKSLF TDFTPLAGDR KFSEDAAIQA GLARFNGQPV AIIGQEKGND 

       130        140        150        160        170        180 
TKSRLKHNFG SARPEGYRKA IRVLELADRF SLPVVTLIDT AGAYPGVGAE ERGQAEAIAR 

       190        200        210        220        230        240 
STEMCLNVKV PIVSVVIGEG GSGGAIAIAT GNRVYMLEHS VYSVISPEGA ASILWRDSTR 

       250        260        270        280        290        300 
AKEAATNMKI TSEDLKSLGV IDGIIPEPIG GAHRAPETVI SATGDVIAKA LADLSQRSGT 

       310 
QLRAERRQKF LDIGRNL

Q8U9U5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools