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E7B6B6

- E7B6B6_YERE1

UniProt

E7B6B6 - E7B6B6_YERE1

Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Yersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 23 (01 Oct 2014)
      Sequence version 1 (08 Mar 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs 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.UniRule annotation
    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.UniRule annotation
    Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.UniRule annotation

    Catalytic activityi

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

    Cofactori

    Magnesium.UniRule annotationSAAS annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei312 – 3121Coenzyme AUniRule annotation
    Binding sitei336 – 3361Coenzyme AUniRule annotation
    Binding sitei388 – 3881Substrate; via nitrogen amideUniRule annotation
    Binding sitei501 – 5011SubstrateUniRule annotation
    Binding sitei516 – 5161SubstrateUniRule annotation
    Active sitei518 – 5181UniRule annotation
    Binding sitei524 – 5241Coenzyme AUniRule annotation
    Binding sitei527 – 5271SubstrateUniRule annotation
    Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi543 – 5431Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei585 – 5851Coenzyme AUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from acetate Source: UniProtKB-HAMAP
    2. chemotaxis Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    LigaseUniRule annotationImported

    Keywords - Ligandi

    ATP-bindingUniRule annotation, MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYENT930944:GLMU-3592-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-coenzyme A synthetaseUniRule annotation (EC:6.2.1.1UniRule annotation)
    Short name:
    AcCoA synthetaseUniRule annotation
    Short name:
    AcsUniRule annotation
    Alternative name(s):
    Acetate--CoA ligaseUniRule annotation
    Acyl-activating enzymeUniRule annotation
    Gene namesi
    Name:acsUniRule annotation
    Ordered Locus Names:Y11_35151Imported
    OrganismiYersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)Imported
    Taxonomic identifieri930944 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
    ProteomesiUP000008084: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei610 – 6101N6-acetyllysineUniRule annotation

    Post-translational modificationi

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

    Keywords - PTMi

    AcetylationUniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliE7B6B6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni192 – 1954Coenzyme AUniRule annotation
    Regioni412 – 4176Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the ATP-dependent AMP-binding enzyme family.UniRule annotation

    Phylogenomic databases

    KOiK01895.

    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.

    E7B6B6-1 [UniParc]FASTAAdd to Basket

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    MMSQIHKHPI PTAIAEHALI NPEQYHQYYQ QSVQNPDEFW GEHGKIIDWI    50
    KPYKTVKNTS FDPGHVSIRW FEDGTLNLAA NCLDRHLAER SDQTAIIWEG 100
    DDPNQSKTVT YKQLHHDVCQ FANVLKKLGI KKGDVVAIYM PMVPEAAVAM 150
    LACARIGAVH SVIFGGFSPD AVAGRIIDSN SKLVITADEG IRAGRAIPLK 200
    KNVDEALKNP AITSIKNVVV FQRTGNASYW KDGRDVWWHD LIENASADCP 250
    PEEMNAEDPL FILYTSGSTG KPKGVLHTTG GYLVYAALTF KYVFDYHPGD 300
    IYWCTADVGW VTGHSYLLYG PLACGAITLM FEGVPNYPGV NRLGQVIDKH 350
    QVNILYTAPT AIRALMAEGD KAIEDTKRTS LRIMGSVGEP INPEAWEWYY 400
    NKIGNSKCPI VDTWWQTETG GFMITPLPGA TELKAGSATR PFFGVQPALV 450
    DNLGNPQEGA AEGNLVITDS WPGQARTLFG DHDRFEQTYF STFKGMYFSG 500
    DGARRDEDGY YWITGRVDDV LNVSGHRLGT AEIESALVSH PKIAEAAVVG 550
    VPHNIKGQAI YAYITLNHGE EPTPELYTEV RNWVRKEIGP IATPDILHWT 600
    DSLPKTRSGK IMRRILRKIA AGDTSNLGDT STLADPGVVD KLLEEKQSMQ 650
    APS 653
    Length:653
    Mass (Da):72,214
    Last modified:March 8, 2011 - v1
    Checksum:i07271790E643740E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FR729477 Genomic DNA. Translation: CBY29015.1.
    RefSeqiYP_006007014.1. NC_017564.1.

    Genome annotation databases

    EnsemblBacteriaiCBY29015; CBY29015; Y11_35151.
    GeneIDi12602229.
    KEGGiyey:Y11_35151.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FR729477 Genomic DNA. Translation: CBY29015.1 .
    RefSeqi YP_006007014.1. NC_017564.1.

    3D structure databases

    ProteinModelPortali E7B6B6.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CBY29015 ; CBY29015 ; Y11_35151 .
    GeneIDi 12602229.
    KEGGi yey:Y11_35151.

    Phylogenomic databases

    KOi K01895.

    Enzyme and pathway databases

    BioCyci YENT930944:GLMU-3592-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. "Complete genome sequence of Y. enterocolitica subsp. palearctica serogroup O:3."
      Batzilla J., Hoeper D., Heesemann J., Rakin A.
      Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: Y11.
    2. "Complete genome sequence of Yersinia enterocolitica subsp. palearctica serogroup O:3."
      Batzilla J., Hoper D., Antonenka U., Heesemann J., Rakin A.
      J. Bacteriol. 193:2067-2067(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 13030 / CIP 106945 / Y11Imported.

    Entry informationi

    Entry nameiE7B6B6_YERE1
    AccessioniPrimary (citable) accession number: E7B6B6
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 8, 2011
    Last sequence update: March 8, 2011
    Last modified: October 1, 2014
    This is version 23 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3