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Q9KDS9 (ACCC_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biotin carboxylase

EC=6.3.4.14
Alternative name(s):
Acetyl-CoA carboxylase subunit A
Short name=ACC
EC=6.4.1.2
Gene names
Name:accC
Ordered Locus Names:BH1132
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA By similarity.

Catalytic activity

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.

Subunit structure

Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl carrier protein, biotin carboxylase and the two subunits of carboxyl transferase in a 2:2 complex By similarity.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Biotin carboxylase
PRO_0000146788

Regions

Domain1 – 445445Biotin carboxylation
Domain120 – 317198ATP-grasp

Sites

Active site2921 By similarity
Binding site1161ATP By similarity
Binding site2001ATP By similarity
Binding site2351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KDS9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4BCF230D1A44E880

FASTA45249,938
        10         20         30         40         50         60 
MFKKVLIANR GEIAVRIIRT CQKLNIRTVA IYSEADVDSL HVKHADEAFL IGKPPVAESY 

        70         80         90        100        110        120 
LKVDTILEVA KQAGVDAIHP GYGLLSENAR FARACVEAGI SFIGPSPEVI ERMGSKIAAR 

       130        140        150        160        170        180 
TAMQTAGVPV IPGSDVALAD EEEAVHLARK FGYPVMLKAS AGGGGIGMQL VRNDEEMRKA 

       190        200        210        220        230        240 
FAGNQKRATS FFGDGTMFLE KAVENPRHIE VQIAADHHGH VVHLWERDCS IQRRHQKVVE 

       250        260        270        280        290        300 
EAPSPFVDEA LREKIGQLAV KAAKAIDYRN LGTVECLVDG EKNIYFLEMN TRLQVEHPVT 

       310        320        330        340        350        360 
EEITGIDLVE WQLLIAAGEQ LPYAQHEIPL QGHAIEVRIY AEDPVTFFPS PGMIKRFTLP 

       370        380        390        400        410        420 
EGEGIRHEYA ISEGYKVTPF YDPMVAKLIV SADTRGEAIQ RLGRALKQYE IEGIKTNIPM 

       430        440        450 
LKQVINHPVF QAGEATTAFV TNHLKVKTGR NP 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB04851.1.
PIRD83791.
RefSeqNP_241998.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KDS9.
SMRQ9KDS9. Positions 1-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH1132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB04851; BAB04851; BAB04851.
GeneID894101.
KEGGbha:BH1132.
PATRIC18939326. VBIBacHal18977_1181.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0439.
HOGENOMHOG000008988.
KOK01961.
OMAAVILEFA.
OrthoDBEOG6CVV6Z.
ProtClustDBPRK06111.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-1210-MONOMER.
UniPathwayUPA00655; UER00711.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACCC_BACHD
AccessionPrimary (citable) accession number: Q9KDS9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: October 1, 2000
Last modified: November 13, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways