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O34544 (ACCC2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 2

EC=6.3.4.14
Alternative name(s):
Acetyl-CoA carboxylase subunit A 2
Short name=ACC 2
EC=6.4.1.2
Gene names
Name:accC2
Synonyms:accC, yngH
Ordered Locus Names:BSU18240
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length444 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 – 444444Biotin carboxylase 2
PRO_0000360841

Regions

Domain1 – 444444Biotin 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
O34544 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C866DEB8B4177E3B

FASTA44449,087
        10         20         30         40         50         60 
MFTKVLIANR GEIAMRIIRT CSRLGIKTVA VYSEADKDAP HTKAATEAYL IGESRVSESY 

        70         80         90        100        110        120 
LNIERIIKTA KKAKADAIHP GYGLLSENSR FAERCKQENI VFIGPSPDII AKMGSKIEAR 

       130        140        150        160        170        180 
KAMEAAGVPV VPGVSESLGD IEAACRTASQ IGYPVMLKAS AGGGGIGMQR VENEEALKKA 

       190        200        210        220        230        240 
YEGNKKRAAD FFGDGSMYIE KVIEHARHIE VQLLADQHGH TVHLFERDCS VQRRHQKVIE 

       250        260        270        280        290        300 
EAPSPFVDDE LRMKIGQTAV KAAKAIGYTN AGTIEFIVDQ KQNFYFLEMN TRLQVEHPVT 

       310        320        330        340        350        360 
EEITGLDLVE QQLRIAAGHT LTFSQKDIQR NGHAIEVRIY AEDPKTFFPS PGTITAFSLP 

       370        380        390        400        410        420 
DQKGVRHECA VAKDSTVTPF YDPMIAKMIV KGQTRTEAIE KLETALRDYR VEGIKTNLPL 

       430        440 
LIQAAATKAF KEGDVTTDFL KQHL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence completion, identification and definition of the fengycin operon in Bacillus subtilis 168."
Tosato V., Albertini A.M., Zotti M., Sonda S., Bruschi C.V.
Microbiology 143:3443-3450(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13917 Genomic DNA. Translation: CAA74216.1.
AL009126 Genomic DNA. Translation: CAB13707.1.
PIRE69893.
RefSeqNP_389706.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34544.
SMRO34544. Positions 1-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU18240.

Proteomic databases

PaxDbO34544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13707; CAB13707; BSU18240.
GeneID939474.
KEGGbsu:BSU18240.
PATRIC18975485. VBIBacSub10457_1934.

Organism-specific databases

GenoListBSU18240. [Micado]

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBSUB:BSU18240-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 nameACCC2_BACSU
AccessionPrimary (citable) accession number: O34544
Secondary accession number(s): Q799L8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: November 13, 2013
This is version 105 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList