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Q30QK3

- Q30QK3_SULDN

UniProt

Q30QK3 - Q30QK3_SULDN

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251))
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (06 Dec 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 annotationSAAS annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei307 – 3071Coenzyme AUniRule annotation
    Binding sitei383 – 3831Substrate; via nitrogen amideUniRule annotation
    Binding sitei500 – 5001SubstrateUniRule annotation
    Binding sitei515 – 5151SubstrateUniRule annotation
    Active sitei517 – 5171UniRule annotation
    Binding sitei523 – 5231Coenzyme AUniRule annotation
    Binding sitei526 – 5261SubstrateUniRule annotation
    Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei586 – 5861Coenzyme 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 annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSDEN326298:GH9P-1500-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:Suden_1451Imported
    OrganismiSulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251))Imported
    Taxonomic identifieri326298 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeSulfurimonas
    ProteomesiUP000002714: Chromosome

    PTM / Processingi

    Amino acid modifications

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

    STRINGi326298.Suden_1451.

    Structurei

    3D structure databases

    ProteinModelPortaliQ30QK3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiGGCEAVT.
    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.

    Q30QK3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNREVFKPNK EFSKSARIKN MCEYQDLQEY ALEDYEGFWG SYAKEKLEWM    50
    QPFTNVMNES NFPFVKWFEG GKLNVSVQCI DRHLKSRKNK AAIIFEGDRG 100
    DKQIITYLEL YYNVNKFANL LKNEFDVKKG DRVIIYMPMI PEAAYAMLAC 150
    ARIGAIHSIV FGGFSAEALK DRVIDAGAKV VITADGAYRK DKPYMLKPVV 200
    DEALRGETPV KKVLVVERNG EDVTWVAGRD YSYNELIKHQ SGKCEPEVMD 250
    SEDPLFLLYT SGSTGKPKGV QHNSAGYILW AQMTMEWVFD VKENDTYWCT 300
    ADVGWITGHT YIVYGPLAMG ATTIMFEGVP TYPDAGRPWK MVEEYKVNQF 350
    YTAPTAIRVL HKTGENEPAK YDLSSLKVLG TVGEPIDPPA WKWYYEAIGG 400
    SKCAIVDTYW QTETGGHIVS PLPGATPIKP ACATFPLPGI MAEILDENGN 450
    RAEVGEKGLM CVTRPWPAMI RGVWGDEERF VKSYFGDVKK DGKPVYFTGD 500
    GAIYDEDGYI TITGRTDDVI NVSGHRMGTA EVEAAIKKHP NVAEVAVVGK 550
    PHEIKGEGIF AYIVLKSDSG IADEVEEVKA INKVIQKEIG NIALCDDVVF 600
    VVGLPKTRSG KIMRRILRSI AKGEEITQDI STLEDPSIVA TIASAVQSCR 650
    L 651
    Length:651
    Mass (Da):72,616
    Last modified:December 6, 2005 - v1
    Checksum:i7A53E3EDCBB4CCC8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000153 Genomic DNA. Translation: ABB44728.1.
    RefSeqiYP_393963.1. NC_007575.1.

    Genome annotation databases

    EnsemblBacteriaiABB44728; ABB44728; Suden_1451.
    GeneIDi3763349.
    KEGGitdn:Suden_1451.
    PATRICi23771544. VBISulDen68967_1506.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000153 Genomic DNA. Translation: ABB44728.1 .
    RefSeqi YP_393963.1. NC_007575.1.

    3D structure databases

    ProteinModelPortali Q30QK3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 326298.Suden_1451.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB44728 ; ABB44728 ; Suden_1451 .
    GeneIDi 3763349.
    KEGGi tdn:Suden_1451.
    PATRICi 23771544. VBISulDen68967_1506.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci SDEN326298:GH9P-1500-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: ATCC 33889 / DSM 1251Imported.

    Entry informationi

    Entry nameiQ30QK3_SULDN
    AccessioniPrimary (citable) accession number: Q30QK3
    Entry historyi
    Integrated into UniProtKB/TrEMBL: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 63 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