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Protein
Submitted name:

Acetyl-CoA carboxylase

Gene

accC

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151ATP analogCombined sources
Binding sitei157 – 1571ATP analogCombined sources
Binding sitei164 – 1641ATP analog; via amide nitrogenCombined sources
Binding sitei231 – 2311ATP analogCombined sources
Metal bindingi274 – 2741MagnesiumCombined sources
Binding sitei274 – 2741ATP analogCombined sources
Metal bindingi288 – 2881MagnesiumCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi199 – 2024ATP analogCombined sources
Nucleotide bindingi288 – 2903ATP analogCombined sources

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. biotin carboxylase activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

MagnesiumCombined sources, Metal-bindingCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1542-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Acetyl-CoA carboxylaseImported
Gene namesi
Name:accCImported
Ordered Locus Names:SAV1526Imported
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)Imported
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000002481 Componenti: Chromosome

PTM / Processingi

2D gel databases

World-2DPAGE0002:Q99TW7.

Interactioni

Protein-protein interaction databases

STRINGi158878.SAV1526.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VPQX-ray2.10A/B1-451[»]
ProteinModelPortaliQ99TW7.
SMRiQ99TW7. Positions 2-449.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99TW7.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0439.
KOiK01961.
OMAiKDFYFME.
OrthoDBiEOG6CVV6Z.
PhylomeDBiQ99TW7.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR004549. 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]
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.
TIGRFAMsiTIGR00514. accC. 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.

Q99TW7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVLIANRG EIAVRIIRAC RDLGIQTVAI YSEGDKDALH TQIADEAYCV
60 70 80 90 100
GPTLSKDSYL NIPNILSIAT STGCDGVHPG YGFLAENADF AELCEACQLK
110 120 130 140 150
FIGPSYQSIQ KMGIKDVAKA EMIKANVPVV PGSDGLMKDV SEAKKIAKKI
160 170 180 190 200
GYPVIIKATA GGGGKGIRVA RDEKELETGF RMTEQEAQTA FGNGGLYMEK
210 220 230 240 250
FIENFRHIEI QIVGDSYGNV IHLGERDCTI QRRMQKLVEE APSPILDDET
260 270 280 290 300
RREMGNAAVR AAKAVNYENA GTIEFIYDLN DNKFYFMEMN TRIQVEHPVT
310 320 330 340 350
EMVTGIDLVK LQLQVAMGDV LPYKQEDIKL TGHAIEFRIN AENPYKNFMP
360 370 380 390 400
SPGKIEQYLA PGGYGVRIES ACYTNYTIPP YYDSMVAKLI IHEPTRDEAI
410 420 430 440 450
MAGIRALSEF VVLGIDTTIP FHIKLLNNDI FRSGKFNTNF LEQNSIMNDE

G
Length:451
Mass (Da):50,049
Last modified:June 1, 2001 - v1
Checksum:i8E8ED63980022092
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57688.1.
PIRiF89932.
RefSeqiNP_372050.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB57688; BAB57688; SAV1526.
KEGGisav:SAV1526.
PATRICi19563792. VBIStaAur52173_1573.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57688.1.
PIRiF89932.
RefSeqiNP_372050.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VPQX-ray2.10A/B1-451[»]
ProteinModelPortaliQ99TW7.
SMRiQ99TW7. Positions 2-449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV1526.

2D gel databases

World-2DPAGE0002:Q99TW7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB57688; BAB57688; SAV1526.
KEGGisav:SAV1526.
PATRICi19563792. VBIStaAur52173_1573.

Phylogenomic databases

eggNOGiCOG0439.
KOiK01961.
OMAiKDFYFME.
OrthoDBiEOG6CVV6Z.
PhylomeDBiQ99TW7.

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1542-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ99TW7.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR004549. 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]
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.
TIGRFAMsiTIGR00514. accC. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu50 / ATCC 700699Imported.
  2. "Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase."
    Mochalkin I., Miller J.R., Evdokimov A., Lightle S., Yan C., Stover C.K., Waldrop G.L.
    Protein Sci. 17:1706-1718(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND MAGNESIUM.

Entry informationi

Entry nameiQ99TW7_STAAM
AccessioniPrimary (citable) accession number: Q99TW7
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: April 29, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.