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B4U9A1 (B4U9A1_HYDS0) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha HAMAP MF_00823

Short name=ACCase subunit alpha HAMAP MF_00823
Short name=Acetyl-CoA carboxylase carboxyltransferase subunit alpha HAMAP MF_00823
EC=6.4.1.2 HAMAP MF_00823
Gene names
Name:accA HAMAP MF_00823
Ordered Locus Names:HY04AAS1_1026
OrganismHydrogenobaculum sp. (strain Y04AAS1) [Complete proteome] [HAMAP]
Taxonomic identifier380749 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeHydrogenobaculum

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP MF_00823 SAAS SAAS011763

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. HAMAP MF_00823 SAAS SAAS011763

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. HAMAP MF_00823 SAAS SAAS011763

Subunit structure

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. HAMAP MF_00823 SAAS SAAS011763

Subcellular location

Cytoplasm By similarity HAMAP MF_00823 SAAS SAAS011763.

Sequence similarities

Belongs to the AccA family. HAMAP MF_00823

Sequences

Sequence LengthMass (Da)Tools
B4U9A1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 2388381235F5D66A

FASTA31335,513
        10         20         30         40         50         60 
MTIKDVQELK TKIDQLKILY KQGKTDVEKD LRAFQRESKQ ISKEFCKNLS PWDRVSIARH 

        70         80         90        100        110        120 
NERPQTLDYI KAVFKNFVEL HGDRCYGDDP AIISGFAKFY NKSVCIMGHQ KGRDTKDKIY 

       130        140        150        160        170        180 
RNFGMAHPEG YRKAQRIMKL AEKFQIPIIT FVDTAGAYPG IGAEERGQAQ AIATSIELMG 

       190        200        210        220        230        240 
SLKTHIITII IGEGGSGGAL ALAVADKVLM LENAWYSVIS PEGCAAILYK DQSKVQEATK 

       250        260        270        280        290        300 
SLKITAQDLY ELGVIDCIIP EPYCGAHMSH RLTFYNVKFF LRKALNEVLK YNIDEIVQKR 

       310 
HDRYLNIGFY ENA 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed: 19136599] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001130 Genomic DNA. Translation: ACG57712.1.
RefSeqYP_002121690.1. NC_011126.1.

3D structure databases

ProteinModelPortalB4U9A1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4U9A1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6743841.
GenomeReviewsGene locus HY04AAS1_1026 in contig CP001130_GR.
KEGGhya:HY04AAS1_1026.
PATRIC22136748. VBIHydSp64203_1034.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG286557.
OMAGRDTKDN.

Family and domain databases

HAMAPMF_00823. AcetylCoA_CT_alpha.
[Tree]
InterProIPR001095. Acetyl_CoA_COase_a_su.
IPR011763. COA_CT_C.
[Graphical view]
KOK01962.
PANTHERPTHR22855:SF3. Ac-CoA_carboxylA. 1 hit.
PfamPF03255. ACCA. 1 hit.
[Graphical view]
PRINTSPR01069. ACCCTRFRASEA.
TIGRFAMsTIGR00513. AccA. 1 hit.
PROSITEPS50989. COA_CT_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB4U9A1_HYDS0
AccessionPrimary (citable) accession number: B4U9A1
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: December 14, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)