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Q9KDS9

- ACCC_BACHD

UniProt

Q9KDS9 - ACCC_BACHD

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Protein

Biotin carboxylase

Gene

accC

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
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

BioCyciBHAL272558:GJC5-1210-MONOMER.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin carboxylase (EC:6.3.4.14)
Alternative name(s):
Acetyl-CoA carboxylase subunit A (EC:6.4.1.2)
Short name:
ACC
Gene namesi
Name:accC
Ordered Locus Names:BH1132
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001258: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Biotin carboxylasePRO_0000146788Add
BLAST

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

STRINGi272558.BH1132.

Structurei

3D structure databases

ProteinModelPortaliQ9KDS9.
SMRiQ9KDS9. Positions 1-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 445445Biotin 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.
KOiK01961.
OMAiAVILEFA.
OrthoDBiEOG6CVV6Z.

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.

Q9KDS9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFKKVLIANR GEIAVRIIRT CQKLNIRTVA IYSEADVDSL HVKHADEAFL
60 70 80 90 100
IGKPPVAESY LKVDTILEVA KQAGVDAIHP GYGLLSENAR FARACVEAGI
110 120 130 140 150
SFIGPSPEVI ERMGSKIAAR TAMQTAGVPV IPGSDVALAD EEEAVHLARK
160 170 180 190 200
FGYPVMLKAS AGGGGIGMQL VRNDEEMRKA FAGNQKRATS FFGDGTMFLE
210 220 230 240 250
KAVENPRHIE VQIAADHHGH VVHLWERDCS IQRRHQKVVE EAPSPFVDEA
260 270 280 290 300
LREKIGQLAV KAAKAIDYRN LGTVECLVDG EKNIYFLEMN TRLQVEHPVT
310 320 330 340 350
EEITGIDLVE WQLLIAAGEQ LPYAQHEIPL QGHAIEVRIY AEDPVTFFPS
360 370 380 390 400
PGMIKRFTLP EGEGIRHEYA ISEGYKVTPF YDPMVAKLIV SADTRGEAIQ
410 420 430 440 450
RLGRALKQYE IEGIKTNIPM LKQVINHPVF QAGEATTAFV TNHLKVKTGR

NP
Length:452
Mass (Da):49,938
Last modified:October 1, 2000 - v1
Checksum:i4BCF230D1A44E880
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB04851.1.
PIRiD83791.
RefSeqiNP_241998.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB04851; BAB04851; BAB04851.
GeneIDi894101.
KEGGibha:BH1132.
PATRICi18939326. VBIBacHal18977_1181.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB04851.1 .
PIRi D83791.
RefSeqi NP_241998.1. NC_002570.2.

3D structure databases

ProteinModelPortali Q9KDS9.
SMRi Q9KDS9. Positions 1-444.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272558.BH1132.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB04851 ; BAB04851 ; BAB04851 .
GeneIDi 894101.
KEGGi bha:BH1132.
PATRICi 18939326. VBIBacHal18977_1181.

Phylogenomic databases

eggNOGi COG0439.
HOGENOMi HOG000008988.
KOi K01961.
OMAi AVILEFA.
OrthoDBi EOG6CVV6Z.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
BioCyci BHAL272558:GJC5-1210-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

  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.

Entry informationi

Entry nameiACCC_BACHD
AccessioniPrimary (citable) accession number: Q9KDS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: October 1, 2000
Last modified: October 1, 2014
This is version 89 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3