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Q3APY8

- Q3APY8_CHLCH

UniProt

Q3APY8 - Q3APY8_CHLCH

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Chlorobium chlorochromatii (strain CaD3)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (22 Nov 2005)
      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 sitei331 – 3311Coenzyme AUniRule annotation
    Binding sitei355 – 3551Coenzyme AUniRule annotation
    Binding sitei407 – 4071Substrate; via nitrogen amideUniRule annotation
    Binding sitei520 – 5201SubstrateUniRule annotation
    Binding sitei535 – 5351SubstrateUniRule annotation
    Active sitei537 – 5371UniRule annotation
    Binding sitei543 – 5431Coenzyme AUniRule annotation
    Binding sitei546 – 5461SubstrateUniRule annotation
    Metal bindingi557 – 5571Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi559 – 5591Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi562 – 5621Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei604 – 6041Coenzyme 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

    Enzyme and pathway databases

    BioCyciCCHL340177:GHBW-1701-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:Cag_1685Imported
    OrganismiChlorobium chlorochromatii (strain CaD3)Imported
    Taxonomic identifieri340177 [NCBI]
    Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium
    ProteomesiUP000002708: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei629 – 6291N6-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

    STRINGi340177.Cag_1685.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3APY8.
    SMRiQ3APY8. Positions 31-664.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni431 – 4366Substrate 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.
    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.

    Q3APY8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATETPSSSQ QEAAANPAED SISSVLTEKR KFPPPASFSE QAHLSTMEQY    50
    EKLYADAAAD PEGYWAGIAE QFHWFKKWDS VLEWNSPYAK WFNGGKTNIC 100
    YNALDVHVKS WRKNKAAVIW EGEQGDQRIL TYGELHRQVC KFANVLKIAG 150
    IKPGDRIAIY MGMVPELMIA VLACARVGAV HNVIFAGFSA HAITERVNDS 200
    RAKMVICADG TRRRGSTINL KNIVDEAIVN TPSVRNVIVL KTTGETIKMH 250
    DGMDHWWHDL MGLAVDESEA VELDAEHPLF VLYTSGSTGK PKGILHTTAG 300
    YMVHAASSFR YVFDIKDEDI YFCTADIGWI TGHSYMVYGP LLNGATLLMY 350
    EGAPNYPQWD RFWDIINRHK VTILYTAPTA IRAFIRAGNE WVTKHNLNSL 400
    RLLGTVGEPI NPEAWMWYHK VVGQEKCPIV DTWWQTETGG IMVSPMPGAT 450
    PTKPGTATRP LPGIMVDVVH KDGTPCGANE GGYLVIKKPW PSMLRTIYGD 500
    NERYEKTYWS EFKDMYFTGD GARKDDDGYI WIMGRVDDVV NVSGHRLGTS 550
    EVESALVSHE AVAEAAVVSR PDDIKGNSLV AFVTLKDEYE GDMKLRESLR 600
    NHVAREIGPI AKPDEIRWAK ALPKTRSGKI MRRLLRELAT SNEIKGDVTT 650
    LEDFGVLENL RDQENE 666
    Length:666
    Mass (Da):74,565
    Last modified:November 22, 2005 - v1
    Checksum:iBAC348AF52226EDF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000108 Genomic DNA. Translation: ABB28937.1.
    RefSeqiWP_011362699.1. NC_007514.1.
    YP_379980.1. NC_007514.1.

    Genome annotation databases

    EnsemblBacteriaiABB28937; ABB28937; Cag_1685.
    GeneIDi3746375.
    KEGGicch:Cag_1685.
    PATRICi21371113. VBIChlChl46571_1751.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000108 Genomic DNA. Translation: ABB28937.1 .
    RefSeqi WP_011362699.1. NC_007514.1.
    YP_379980.1. NC_007514.1.

    3D structure databases

    ProteinModelPortali Q3APY8.
    SMRi Q3APY8. Positions 31-664.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 340177.Cag_1685.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB28937 ; ABB28937 ; Cag_1685 .
    GeneIDi 3746375.
    KEGGi cch:Cag_1685.
    PATRICi 21371113. VBIChlChl46571_1751.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CCHL340177:GHBW-1701-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 sequence of Chlorobium chlorochromatii CaD3."
      US DOE Joint Genome Institute
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CaD3Imported.

    Entry informationi

    Entry nameiQ3APY8_CHLCH
    AccessioniPrimary (citable) accession number: Q3APY8
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 22, 2005
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3