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I4CUB2

- I4CUB2_PSEST

UniProt

I4CUB2 - I4CUB2_PSEST

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pseudomonas stutzeri CCUG 29243
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 15 (01 Oct 2014)
      Sequence version 1 (05 Sep 2012)
      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 sitei311 – 3111Coenzyme AUniRule annotation
    Binding sitei335 – 3351Coenzyme AUniRule annotation
    Binding sitei387 – 3871Substrate; 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 bindingi537 – 5371Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi542 – 5421Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei584 – 5841Coenzyme 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

    BioCyciPSTU1196835:GLIX-2444-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
    ORF Names:A458_12170Imported
    OrganismiPseudomonas stutzeri CCUG 29243Imported
    Taxonomic identifieri1196835 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000006063: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei609 – 6091N6-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

    ProteinModelPortaliI4CUB2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni411 – 4166Substrate 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.

    I4CUB2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAASVYPVR PEVAAQSLTN EASYKAMYQQ SVINPEGFWR EQAARLNWIR    50
    PFTEVKRTSF DDHHVDIKWF ADGTLNVSAN CLDRHLAERG DQLAIIWEGD 100
    DPSEHREITY RELHQEVSKF ANALRGQDVH RGDVVTIYMP MIPEAAVAML 150
    ACARIGAIHS VVFGGFSPEA LAGRIIDGQS KIVITADEGV RGGKPVPLKG 200
    NVDEALTNPQ TSCVKKIIVV RRTGADIRWH SHRDICYDDL MRVAGEVCAP 250
    KEMGAEEPLF ILYTSGSTGK PKGVLHTCGG YLLYAALTHE RVFDYRPGEV 300
    YWCTADIGWI TGHSYLIYGP LANGATTLMY EGVPNHPDVT RIARIIDKHK 350
    VNILYTAPTA IRAMMAEGAA AVEGADGSSL RLLGTVGEPI NPEAWHWYYE 400
    TVGQSRCPIV DTWWQTETGG ILISPLPGAT TLKPGSATRP MFGVVPGLVD 450
    NLGNLLEGPA EGNLVILDSW PGQMRTIYKD HDRFVDTYFK TFRGMYFTGD 500
    GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESAMVAHA KVAEAAAVGV 550
    PHKLKGQAIY VYVTLVSGVQ PSDALRQELQ QWVRKEIGPI AVPDVIQWAP 600
    GLPKTRSGKI MRRLLRKIAT DDYDALGDTS TLADPGVVDQ LIEAHEAVRK 650
    R 651
    Length:651
    Mass (Da):71,716
    Last modified:September 5, 2012 - v1
    Checksum:iD85BB766C8B3B657
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003677 Genomic DNA. Translation: AFM33669.1.
    RefSeqiWP_014820603.1. NC_018028.1.
    YP_006458092.1. NC_018028.1.

    Genome annotation databases

    EnsemblBacteriaiAFM33669; AFM33669; A458_12170.
    GeneIDi13145759.
    KEGGipsc:A458_12170.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003677 Genomic DNA. Translation: AFM33669.1 .
    RefSeqi WP_014820603.1. NC_018028.1.
    YP_006458092.1. NC_018028.1.

    3D structure databases

    ProteinModelPortali I4CUB2.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AFM33669 ; AFM33669 ; A458_12170 .
    GeneIDi 13145759.
    KEGGi psc:A458_12170.

    Phylogenomic databases

    KOi K01895.

    Enzyme and pathway databases

    BioCyci PSTU1196835:GLIX-2444-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 the Naphthalene-Degrading Bacterium Pseudomonas stutzeri AN10 (CCUG 29243)."
      Brunet-Galmes I., Busquets A., Pena A., Gomila M., Nogales B., Garcia-Valdes E., Lalucat J., Bennasar A., Bosch R.
      J. Bacteriol. 194:6642-6643(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CCUG 29243Imported.

    Entry informationi

    Entry nameiI4CUB2_PSEST
    AccessioniPrimary (citable) accession number: I4CUB2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: September 5, 2012
    Last sequence update: September 5, 2012
    Last modified: October 1, 2014
    This is version 15 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