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F4DQJ9

- F4DQJ9_PSEMN

UniProt

F4DQJ9 - F4DQJ9_PSEMN

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Pseudomonas mendocina (strain NK-01)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 19 (01 Oct 2014)
      Sequence version 1 (28 Jun 2011)
      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 annotation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciPMEN1001585:GIWS-3446-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:MDS_3395Imported
    OrganismiPseudomonas mendocina (strain NK-01)Imported
    Taxonomic identifieri1001585 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000008306: 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

    ProteinModelPortaliF4DQJ9.
    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.
    OMAiDISWING.

    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.

    F4DQJ9-1 [UniParc]FASTAAdd to Basket

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    MSAASLYPVR PEVAARTLTD EATYKAMYQQ SVVNPEGFWR EQGKRIDWIK    50
    PYTKVKQTTF DDHHVDIKWY ADGTLNVSYN CLDRHLEERG DQVAIIWEGD 100
    DPSEHREITY RQLHEEVSKF ANALRGQDVH RGDVVTIYMP MIPEAVVAML 150
    ACARIGAIHS VVFGGFSPEA LAGRIIDCES KVVITADEGL RGGRKVPLKA 200
    NVDDALTNPE TASVQKIIVV KRTGSDIKWN QHRDIWYEDL MKVAGSVCAP 250
    KEMGAEEALF ILYTSGSTGK PKGVLHTTGG YLTYASLTHE RVFDYRPGEV 300
    FWCTADIGWV TGHTYLVYGP LSNGATTLMF EGVPNYPDVR RVAQIVDKHK 350
    VNILYTAPTA IRAMMAEGKA AVEGADGSSL RLLGSVGEPI NPEAWQWYYE 400
    NVGQSRCPIV DTWWQTETGA CLMTPLPGAH GLKPGSAARP FFGVQPALVD 450
    NLGNIIEGPA EGNLVIIDSW PGQARTLYGD HDRFVDTYFK TFRGMYFTGD 500
    GARRDEDGYW WITGRVDDVL NVSGHRMGTA EVESAMVAHP KVAEAAVVGV 550
    PHDIKGQGIY VYVTLNAGEE SSEQLRQELK NWVRKEIGPI ATPDVIQWAP 600
    GLPKTRSGKI MRRILRKIAT AEYDSLGDIS TLADPGVVQH LIDTHRQMQA 650
    ACA 653
    Length:653
    Mass (Da):72,265
    Last modified:June 28, 2011 - v1
    Checksum:iFAD6AE26483A4D3D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002620 Genomic DNA. Translation: AEB59426.1.
    RefSeqiYP_004381178.1. NC_015410.1.

    Genome annotation databases

    EnsemblBacteriaiAEB59426; AEB59426; MDS_3395.
    GeneIDi10458177.
    KEGGipmk:MDS_3395.
    PATRICi54487546. VBIPseMen187712_3448.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002620 Genomic DNA. Translation: AEB59426.1 .
    RefSeqi YP_004381178.1. NC_015410.1.

    3D structure databases

    ProteinModelPortali F4DQJ9.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEB59426 ; AEB59426 ; MDS_3395 .
    GeneIDi 10458177.
    KEGGi pmk:MDS_3395.
    PATRICi 54487546. VBIPseMen187712_3448.

    Phylogenomic databases

    KOi K01895.
    OMAi DISWING.

    Enzyme and pathway databases

    BioCyci PMEN1001585:GIWS-3446-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 of Pseudomonas mendocina NK-01, which synthesizes medium-chain-length polyhydroxyalkanoates and alginate oligosaccharides."
      Guo W., Wang Y., Song C., Yang C., Li Q., Li B., Su W., Sun X., Song D., Yang X., Wang S.
      J. Bacteriol. 193:3413-3414(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NK-01Imported.

    Entry informationi

    Entry nameiF4DQJ9_PSEMN
    AccessioniPrimary (citable) accession number: F4DQJ9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 28, 2011
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 19 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