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A5F3Q8

- A5F3Q8_VIBC3

UniProt

A5F3Q8 - A5F3Q8_VIBC3

Protein

Acetyl-coenzyme A synthetase

Gene

acs-1

Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (12 Jun 2007)
      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. 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

    Catalytic activityi

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

    Cofactori

    Magnesium.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei328 – 3281Coenzyme AUniRule annotation
    Binding sitei352 – 3521Coenzyme AUniRule annotation
    Binding sitei404 – 4041Substrate; via nitrogen amideUniRule annotation
    Binding sitei517 – 5171SubstrateUniRule annotation
    Binding sitei532 – 5321SubstrateUniRule annotation
    Active sitei534 – 5341UniRule annotation
    Binding sitei540 – 5401Coenzyme AUniRule annotation
    Binding sitei543 – 5431SubstrateUniRule annotation
    Metal bindingi554 – 5541Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi556 – 5561Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi559 – 5591Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei601 – 6011Coenzyme 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: InterPro

    Keywords - Molecular functioni

    LigaseUniRule annotationImported

    Keywords - Ligandi

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

    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:acs-1Imported
    Synonyms:acsAUniRule annotation
    Ordered Locus Names:VC0395_A2691Imported, VC395_0342Imported
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)Imported
    Taxonomic identifieri345073 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000249: Chromosome 2, UP000001630: Chromosome I

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei626 – 6261N6-acetyllysineUniRule annotation

    Post-translational modificationi

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

    Keywords - PTMi

    AcetylationUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi345073.VC0395_A2691.

    Structurei

    3D structure databases

    ProteinModelPortaliA5F3Q8.
    SMRiA5F3Q8. Positions 22-662.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni428 – 4336Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiAWIWYRD.

    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.

    A5F3Q8-1 [UniParc]FASTAAdd to Basket

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    MKRALSGNLP NSQGEPVMSE AHIYPVKQNI KAHTHADNDT YLAMYQQSIK    50
    DPEGFWSEHG KIVDWIKPFT KVKHTSFDPG HIDIRWFEDG TLNVSANCID 100
    RHLATRGDQV AIIWEGDDPT QDKTLTYKQL HQEVCRFANA LKEQGVRKGD 150
    VVCIYMPMVP EAAVAMLACT RIGAVHTIVF GGFSPEALAG RIIDSNAKLV 200
    ITADEGVRGG RAVPLKKNVD EALCNPEVKN ISKVMVLKRT GGNVAWHEHR 250
    DIWWHEATAK ASDNCPPEEM KAEDPLFILY TSGSTGKPKG VLHTTGGYLV 300
    YATMTFKYVF DYQPNEVFWC TADVGWITGH SYLVYGPLAN GAKTILFEGV 350
    PNYPTTARMS EVVDKHKVNI LYTAPTAIRA LMAKGDEAIK GTSRDSLRIM 400
    GSVGEPINPE AWEWYYRTIG NEESPIVDTW WQTETGGILI TPLPGATALK 450
    PGSATRPFFG VQPALVDNMG EIVEGATEGN LVLLDSWPGQ MRTVYGDHDR 500
    FEQTYFSTFK GMYFTGDGAR RDEDGYYWIT GRVDDVLNVS GHRMGTAEIE 550
    SALVAFNKIA EAAVVGVPHD IKGQAIYAYI TLNDGVYPSA ELHKEVKDWV 600
    RKEIGAIATP DVLHWTDALP KTRSGKIMRR ILRKIATGDT SNLGDTSTLA 650
    DPSVVDRLIA EKAQLK 666
    Length:666
    Mass (Da):73,676
    Last modified:June 12, 2007 - v1
    Checksum:iF88F13DB61BB7BE2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000627 Genomic DNA. Translation: ABQ21501.1.
    CP001235 Genomic DNA. Translation: ACP08367.1.
    RefSeqiYP_002818603.1. NC_012582.1.

    Genome annotation databases

    EnsemblBacteriaiABQ21501; ABQ21501; VC0395_A2691.
    ACP08367; ACP08367; VC395_0342.
    GeneIDi7774414.
    KEGGivcr:VC395_0342.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000627 Genomic DNA. Translation: ABQ21501.1 .
    CP001235 Genomic DNA. Translation: ACP08367.1 .
    RefSeqi YP_002818603.1. NC_012582.1.

    3D structure databases

    ProteinModelPortali A5F3Q8.
    SMRi A5F3Q8. Positions 22-662.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 345073.VC0395_A2691.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ21501 ; ABQ21501 ; VC0395_A2691 .
    ACP08367 ; ACP08367 ; VC395_0342 .
    GeneIDi 7774414.
    KEGGi vcr:VC395_0342.

    Phylogenomic databases

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

    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. Heidelberg J.
      Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39541 / Classical Ogawa 395 / O395Imported and O395Imported.
    2. "A recalibrated molecular clock and independent origins for the cholera pandemic clones."
      Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
      PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39541 / Classical Ogawa 395 / O395 and O395Imported.

    Entry informationi

    Entry nameiA5F3Q8_VIBC3
    AccessioniPrimary (citable) accession number: A5F3Q8
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 12, 2007
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 54 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