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O34544

- ACCC2_BACSU

UniProt

O34544 - ACCC2_BACSU

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Protein

Biotin carboxylase 2

Gene

accC2

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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 activityi

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].
ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161ATPBy similarity
Binding sitei200 – 2001ATPBy similarity
Binding sitei235 – 2351ATPBy similarity
Active sitei292 – 2921By similarity

GO - Molecular functioni

  1. acetyl-CoA carboxylase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. biotin carboxylase activity Source: UniProtKB-EC
  4. metal ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU18240-MONOMER.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin carboxylase 2 (EC:6.3.4.14)
Alternative name(s):
Acetyl-CoA carboxylase subunit A 2 (EC:6.4.1.2)
Short name:
ACC 2
Gene namesi
Name:accC2
Synonyms:accC, yngH
Ordered Locus Names:BSU18240
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU18240. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Biotin carboxylase 2PRO_0000360841Add
BLAST

Proteomic databases

PaxDbiO34544.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi224308.BSU18240.

Structurei

3D structure databases

ProteinModelPortaliO34544.
SMRiO34544. Positions 1-443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 444444Biotin carboxylationAdd
BLAST
Domaini120 – 317198ATP-graspPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated

Phylogenomic databases

eggNOGiCOG0439.
HOGENOMiHOG000008988.
InParanoidiO34544.
KOiK01961.
OMAiAVILEFA.
OrthoDBiEOG6CVV6Z.
PhylomeDBiO34544.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR011761. 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]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O34544-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFTKVLIANR GEIAMRIIRT CSRLGIKTVA VYSEADKDAP HTKAATEAYL
60 70 80 90 100
IGESRVSESY LNIERIIKTA KKAKADAIHP GYGLLSENSR FAERCKQENI
110 120 130 140 150
VFIGPSPDII AKMGSKIEAR KAMEAAGVPV VPGVSESLGD IEAACRTASQ
160 170 180 190 200
IGYPVMLKAS AGGGGIGMQR VENEEALKKA YEGNKKRAAD FFGDGSMYIE
210 220 230 240 250
KVIEHARHIE VQLLADQHGH TVHLFERDCS VQRRHQKVIE EAPSPFVDDE
260 270 280 290 300
LRMKIGQTAV KAAKAIGYTN AGTIEFIVDQ KQNFYFLEMN TRLQVEHPVT
310 320 330 340 350
EEITGLDLVE QQLRIAAGHT LTFSQKDIQR NGHAIEVRIY AEDPKTFFPS
360 370 380 390 400
PGTITAFSLP DQKGVRHECA VAKDSTVTPF YDPMIAKMIV KGQTRTEAIE
410 420 430 440
KLETALRDYR VEGIKTNLPL LIQAAATKAF KEGDVTTDFL KQHL
Length:444
Mass (Da):49,087
Last modified:January 1, 1998 - v1
Checksum:iC866DEB8B4177E3B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13917 Genomic DNA. Translation: CAA74216.1.
AL009126 Genomic DNA. Translation: CAB13707.1.
PIRiE69893.
RefSeqiNP_389706.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13707; CAB13707; BSU18240.
GeneIDi939474.
KEGGibsu:BSU18240.
PATRICi18975485. VBIBacSub10457_1934.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y13917 Genomic DNA. Translation: CAA74216.1 .
AL009126 Genomic DNA. Translation: CAB13707.1 .
PIRi E69893.
RefSeqi NP_389706.1. NC_000964.3.

3D structure databases

ProteinModelPortali O34544.
SMRi O34544. Positions 1-443.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU18240.

Proteomic databases

PaxDbi O34544.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13707 ; CAB13707 ; BSU18240 .
GeneIDi 939474.
KEGGi bsu:BSU18240.
PATRICi 18975485. VBIBacSub10457_1934.

Organism-specific databases

GenoListi BSU18240. [Micado ]

Phylogenomic databases

eggNOGi COG0439.
HOGENOMi HOG000008988.
InParanoidi O34544.
KOi K01961.
OMAi AVILEFA.
OrthoDBi EOG6CVV6Z.
PhylomeDBi O34544.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
BioCyci BSUB:BSU18240-MONOMER.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProi 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 ]
Pfami PF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view ]
SMARTi SM00878. Biotin_carb_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiACCC2_BACSU
AccessioniPrimary (citable) accession number: O34544
Secondary accession number(s): Q799L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3