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Q8X9B6 (ACCC_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. 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:Z4616, ECs4128
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length449 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.

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 – 449449Biotin carboxylase
PRO_0000146792

Regions

Domain1 – 445445Biotin carboxylation
Domain120 – 317198ATP-grasp

Sites

Active site2921 Potential
Binding site1161ATP By similarity
Binding site2011ATP By similarity
Binding site2361ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X9B6 [UniParc].

Last modified March 5, 2002. Version 1.
Checksum: BC5716323F6233ED

FASTA44949,337
        10         20         30         40         50         60 
MLDKIVIANR GEIALRILRA CKELGIKTVA VHSSADRDLK HVLLADETVC IGPAPSVKSY 

        70         80         90        100        110        120 
LNIPAIISAA EITGAVAIHP GYGFLSENAN FAEQVERSGF IFIGPKAETI RLMGDKVSAI 

       130        140        150        160        170        180 
AAMKKAGVPC VPGSDGPLGD DMDKNRAIAK RIGYPVIIKA SGGGGGRGMR VVRGDAELAQ 

       190        200        210        220        230        240 
SISMTRAEAK AAFSNDMVYM EKYLENPRHV EIQVLADGQG NSIYLAERDC SMQRRHQKVV 

       250        260        270        280        290        300 
EEAPAPGITP ELRRYIGERC AKACVDIGYR GAGTFEFLFE NGEFYFIEMN TRIQVEHPVT 

       310        320        330        340        350        360 
EMITGVDLIK EQLRIAAGQP LSIKQEEVHV RGHAVECRIN AEDPNTFLPS PGKITRFHAP 

       370        380        390        400        410        420 
GGFGVRWESH IYAGYTVPPY YDSMIGKLIC YGENRDVAIA RMKNALQELI IDGIKTNVDL 

       430        440 
QIRIMNDENF QHGGTNIHYL EKKLGLQEK 

« Hide

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. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [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. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG58384.1.
BA000007 Genomic DNA. Translation: BAB37551.1.
PIRD85990.
H91144.
RefSeqNP_289824.1. NC_002655.2.
NP_312155.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X9B6.
SMRQ8X9B6. Positions 1-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z4616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG58384; AAG58384; Z4616.
BAB37551; BAB37551; BAB37551.
GeneID916024.
958693.
KEGGece:Z4616.
ecs:ECs4128.
PATRIC18357786. VBIEscCol44059_4067.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0439.
HOGENOMHOG000008988.
KOK01961.
OMAIRRMQNA.
OrthoDBEOG6CVV6Z.

Enzyme and pathway databases

BioCycECOL386585:GJFA-4090-MONOMER.
ECOO157:ACCC-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.
InterProIPR004549. Acetyl_CoA_COase_biotin_COase.
IPR011761. 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.
TIGRFAMsTIGR00514. accC. 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_ECO57
AccessionPrimary (citable) accession number: Q8X9B6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: May 14, 2014
This is version 90 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