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Q0AFF1

- ACSA_NITEC

UniProt

Q0AFF1 - ACSA_NITEC

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Nitrosomonas eutropha (strain C91)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (17 Oct 2006)
      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 sitei316 – 3161Coenzyme AUniRule annotation
    Binding sitei508 – 5081ATPUniRule annotation
    Binding sitei523 – 5231ATPUniRule annotation
    Binding sitei531 – 5311Coenzyme A; via carbonyl oxygenUniRule annotation
    Binding sitei534 – 5341ATPUniRule annotation
    Metal bindingi545 – 5451Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi547 – 5471Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi550 – 5501Magnesium; via carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi392 – 3943ATPUniRule annotation
    Nucleotide bindingi416 – 4216ATPUniRule 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

    Ligase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciNEUT335283:GHT6-1724-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:acsAUniRule annotation
    Ordered Locus Names:Neut_1690
    OrganismiNitrosomonas eutropha (strain C91)
    Taxonomic identifieri335283 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
    ProteomesiUP000001966: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 655655Acetyl-coenzyme A synthetasePRO_1000065298Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei620 – 6201N6-acetyllysineUniRule annotation

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation

    Interactioni

    Protein-protein interaction databases

    STRINGi335283.Neut_1690.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0AFF1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni196 – 1994Coenzyme A bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiYNNDERF.
    OrthoDBiEOG68WR2H.

    Family and domain databases

    HAMAPiMF_01123. Ac_CoA_synth.
    InterProiIPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q0AFF1-1 [UniParc]FASTAAdd to Basket

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    MATIESILRE NRIFPPANEF VRHANITGMK TYEALRQEAE RDYAGFWAKL    50
    AKQYITWHKP FTRILDDTNP PFYKWFDDGE LNISWNCLDR HLTTQANKTA 100
    IIFESDEGEV IRCSYRELHQ RVCRFANGLK ALGIRQGDRI VIYMPMRIEA 150
    VVAMQACARI GVIHSVVFGG FSAKSVYERI IDAGASAVIT ADEQTRGGKR 200
    HALKATVDEA LAMGDTTSVH SVIVFRHTGT DIPWQPERDR WWHNLTASQS 250
    DECEPIWVNA EHPLFTLYTS GSTGKPKGVQ HSSAGYLLGA IVSMQWVFDY 300
    HSEDIFWCTA DVGWVTGHSY VTYGPLAIGA TQVIFEGTPT YPHAGRFWEI 350
    IQKHRVTTFY TAPTAIRSLI KLGPDLPEKY DLSSLRLLGS VGEPINPEAW 400
    MWYYTVIGQS RCPVVDTWWQ TETGSHMIAP IPGAIPAKPG SCTLPLPGID 450
    AAVVDETGLP AEQGKGGFLV IKRPFPSMLR TLWNDPERFR NTYFPADIAG 500
    GHYYLAGDSA HRDQDGYFWI MGRIDDVLNV SGHRLGTMEI ESALVAHPLV 550
    AEAAVVGKPH EIRGEVIVAF VVLRGKLPDD QQAAEIAETL REWVSSEIGA 600
    IARPEEIRFG ENLPKTRSGK LMRRLLRSLA RGETITQDIS TLENPVILEQ 650
    FSQTI 655
    Length:655
    Mass (Da):73,338
    Last modified:October 17, 2006 - v1
    Checksum:iB81E66505C045F43
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000450 Genomic DNA. Translation: ABI59931.1.
    RefSeqiWP_011634737.1. NC_008344.1.
    YP_747896.1. NC_008344.1.

    Genome annotation databases

    EnsemblBacteriaiABI59931; ABI59931; Neut_1690.
    GeneIDi4273573.
    KEGGinet:Neut_1690.
    PATRICi22720832. VBINitEut7577_2068.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000450 Genomic DNA. Translation: ABI59931.1 .
    RefSeqi WP_011634737.1. NC_008344.1.
    YP_747896.1. NC_008344.1.

    3D structure databases

    ProteinModelPortali Q0AFF1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 335283.Neut_1690.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABI59931 ; ABI59931 ; Neut_1690 .
    GeneIDi 4273573.
    KEGGi net:Neut_1690.
    PATRICi 22720832. VBINitEut7577_2068.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci NEUT335283:GHT6-1724-MONOMER.

    Family and domain databases

    HAMAPi MF_01123. Ac_CoA_synth.
    InterProi IPR011904. Ac_CoA_lig.
    IPR025110. AMP-bd_C.
    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.
    ProtoNeti Search...

    Publicationsi

    1. "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
      Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
      Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C91.

    Entry informationi

    Entry nameiACSA_NITEC
    AccessioniPrimary (citable) accession number: Q0AFF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 58 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3