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Q2YLH5

- ACSA_BRUA2

UniProt

Q2YLH5 - ACSA_BRUA2

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Protein
Acetyl-coenzyme A synthetase
Gene
acsA, BAB1_1819
Organism
Brucella abortus (strain 2308)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA By similarity.UniRule annotation

Catalytic activityi

ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei311 – 3111Coenzyme A By similarity
Binding sitei335 – 3351Coenzyme A By similarity
Binding sitei387 – 3871Substrate; via amide nitrogen By similarity
Binding sitei500 – 5001Substrate By similarity
Binding sitei515 – 5151Substrate By similarity
Active sitei517 – 5171 By similarity
Binding sitei523 – 5231Coenzyme A By similarity
Binding sitei526 – 5261Substrate By similarity
Metal bindingi537 – 5371Magnesium; via carbonyl oxygen By similarity
Metal bindingi539 – 5391Magnesium; via carbonyl oxygen By similarity
Metal bindingi542 – 5421Magnesium; via carbonyl oxygen By similarity
Binding sitei586 – 5861Coenzyme A

GO - Molecular functioni

  1. AMP binding Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. acetate-CoA ligase activity Source: UniProtKB-HAMAP
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA biosynthetic process from acetate Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBABO359391:GKDV-1863-MONOMER.
BMEL359391:GJOQ-1863-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-coenzyme A synthetase (EC:6.2.1.1)
Short name:
AcCoA synthetase
Short name:
Acs
Alternative name(s):
Acetate--CoA ligase
Acyl-activating enzyme
Gene namesi
Name:acsA
Ordered Locus Names:BAB1_1819
OrganismiBrucella abortus (strain 2308)
Taxonomic identifieri359391 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000002719: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Acetyl-coenzyme A synthetaseUniRule annotation
PRO_1000065274Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei611 – 6111N6-acetyllysine By similarity

Post-translational modificationi

Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme By similarity.UniRule annotation

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ2YLH5.

Interactioni

Protein-protein interaction databases

STRINGi359391.BAB1_1819.

Structurei

3D structure databases

ProteinModelPortaliQ2YLH5.
SMRiQ2YLH5. Positions 17-648.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni411 – 4166Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0365.
HOGENOMiHOG000229981.
KOiK01895.
OMAiAWIWYRD.
OrthoDBiEOG68WR2H.

Family and domain databases

HAMAPiMF_01123. Ac_CoA_synth.
InterProiIPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2YLH5-1 [UniParc]FASTAAdd to Basket

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MSEKLYPVLP EAKKNTLIDN ETYLEWYEES VSDPDGFWAK HGRRIDWFKP    50
FTKVKNTDFN GDVTIKWYED GVTNVSYNCI DRHLKSRGDK VAIIWEGDNP 100
YIDKKITYRE LYENVCRMAN VLKKHGVKKG DRVTIYLPMI PEAAYAMLAC 150
ARIGAVHSVV FAGFSPEALA GRIVDCESTF VITADEGVRG GKPVALKENT 200
DTAIDIAAKQ YVMVNKVLVV RRTGGKVSWG RGRDLWYHQE VASVEPHCEP 250
EPMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHQ YVFDYHDGEI 300
YWCTADVGWV TGHSYIVYGP LANGATTLMF EGVPNFPDQG RFWEVVDKHH 350
VNIFYTAPTA LRALMGAGDE FVTRSSRSTL RLLGSVGEPI NPEAWEWYYN 400
VVGDQKCPIV DTWWQTENGG ILITPLPGAT DLKPGSATRP FFGVKPVLVD 450
NEGNVQEGVA DGNLCISDSW PGQMRTVYGD HKRFIETYFS TYKGMYFSGD 500
GCRRDEDGYY WITGRVDDVL NISGHRLGTA EIESALVSHH SVSEAAVVGY 550
PHPIKGQGIY CYVTLMTGAD AQDPDELRKE LVQHVRKEIG PIATPDKIQF 600
APGLPKTRSG KIMRRILRKI AEDEFGALGD TSTLADPGVV DDLIENRQNK 650
K 651
Length:651
Mass (Da):72,731
Last modified:February 7, 2006 - v1
Checksum:i7FB222A3EE6476CE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM040264 Genomic DNA. Translation: CAJ11775.1.
RefSeqiYP_415165.1. NC_007618.1.

Genome annotation databases

EnsemblBacteriaiCAJ11775; CAJ11775; BAB1_1819.
GeneIDi3788319.
KEGGibmf:BAB1_1819.
PATRICi17846672. VBIBruMel86222_1885.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM040264 Genomic DNA. Translation: CAJ11775.1 .
RefSeqi YP_415165.1. NC_007618.1.

3D structure databases

ProteinModelPortali Q2YLH5.
SMRi Q2YLH5. Positions 17-648.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 359391.BAB1_1819.

Proteomic databases

PRIDEi Q2YLH5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ11775 ; CAJ11775 ; BAB1_1819 .
GeneIDi 3788319.
KEGGi bmf:BAB1_1819.
PATRICi 17846672. VBIBruMel86222_1885.

Phylogenomic databases

eggNOGi COG0365.
HOGENOMi HOG000229981.
KOi K01895.
OMAi AWIWYRD.
OrthoDBi EOG68WR2H.

Enzyme and pathway databases

BioCyci BABO359391:GKDV-1863-MONOMER.
BMEL359391:GJOQ-1863-MONOMER.

Family and domain databases

HAMAPi MF_01123. Ac_CoA_synth.
InterProi IPR011904. Ac_CoA_lig.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02188. Ac_CoA_lig_AcsA. 1 hit.
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2308.

Entry informationi

Entry nameiACSA_BRUA2
AccessioniPrimary (citable) accession number: Q2YLH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 51 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

Documents

  1. Brucella abortus strain 2308
    Brucella abortus (strain 2308): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi