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Q02FT9

- Q02FT9_PSEAB

UniProt

Q02FT9 - Q02FT9_PSEAB

Protein

Acetyl-coenzyme A synthetase

Gene

acsB

Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (14 Nov 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 annotationSAAS annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei308 – 3081Coenzyme AUniRule annotation
    Binding sitei332 – 3321Coenzyme AUniRule annotation
    Binding sitei384 – 3841Substrate; via nitrogen amideUniRule annotation
    Binding sitei497 – 4971SubstrateUniRule annotation
    Binding sitei512 – 5121SubstrateUniRule annotation
    Active sitei514 – 5141UniRule annotation
    Binding sitei520 – 5201Coenzyme AUniRule annotation
    Binding sitei523 – 5231SubstrateUniRule annotation
    Metal bindingi534 – 5341Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi536 – 5361Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi539 – 5391Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei581 – 5811Coenzyme 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

    BioCyciPAER208963:GI5K-5113-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:acsBImported
    Synonyms:acsAUniRule annotation
    Ordered Locus Names:PA14_62630Imported
    OrganismiPseudomonas aeruginosa (strain UCBPP-PA14)Imported
    Taxonomic identifieri208963 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000000653: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei606 – 6061N6-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

    STRINGi208963.PA14_62630.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02FT9.
    SMRiQ02FT9. Positions 7-642.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni408 – 4136Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiRRIFEPT.
    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.

    Q02FT9-1 [UniParc]FASTAAdd to Basket

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    MFEISVHPVP DAVRQRAYLN DDDYQRLYRQ SVENPDEFWS EQAKAFLDWF    50
    KPWHSVHHGD LRKGQATWFK GGQLNVAYNC IDRHLERRGE QIAIVWEGDN 100
    PSESAHITYR KLHHNVCRLA NVLKSRGVEK GDRVCIYMPM IPEAAYAMLA 150
    CARIGAVHSV VFGGFSPDSL RDRILDADCR TVITADEGVR GGKYIPLKQN 200
    VEKALKDCPD VSTVVVVERT QGDIPWVEGR DIWYHEALHA ASADCPAEAM 250
    DAEDPLFILY TSGSTGKPKG VLHTTGGYLL GAAMTHKYVF DYHDGDVYWC 300
    TADVGWVTGH SYIVYGPLAN GATTLMFEGV PNYPDASRFW QVIDKHQVNI 350
    FYTAPTAIRA LMREGDAPVR QTSRSSLRLL GSVGEPINPE AWEWYYQVVG 400
    EKRCPIVDTW WQTETGSILI TPLPGATALK PGSATRPFFG VQPVLLDEKG 450
    KEIDGAGSGV LAIKASWPSQ IRSVYGDHQR MIDTYFKPYP GYYFSGDGAR 500
    RDEDGYYWIT GRVDDVINVS GHRIGTAEVE SALVLHDAVA EAAVVGCPHD 550
    VKGQAIYAFV TLMAGSQPSE ALQQELLALV GKEIGSFAKP DHLQWAPSLP 600
    KTRSGKIMRR ILRKIACNEL DSLGDTSTLA DPGVVQGLID NRLNR 645
    Length:645
    Mass (Da):71,640
    Last modified:November 14, 2006 - v1
    Checksum:iD3F63891F880B1EA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000438 Genomic DNA. Translation: ABJ14116.1.
    RefSeqiYP_793197.1. NC_008463.1.

    Genome annotation databases

    EnsemblBacteriaiABJ14116; ABJ14116; PA14_62630.
    GeneIDi4383182.
    KEGGipau:PA14_62630.
    PATRICi19856442. VBIPseAer79785_5138.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000438 Genomic DNA. Translation: ABJ14116.1 .
    RefSeqi YP_793197.1. NC_008463.1.

    3D structure databases

    ProteinModelPortali Q02FT9.
    SMRi Q02FT9. Positions 7-642.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208963.PA14_62630.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABJ14116 ; ABJ14116 ; PA14_62630 .
    GeneIDi 4383182.
    KEGGi pau:PA14_62630.
    PATRICi 19856442. VBIPseAer79785_5138.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PAER208963:GI5K-5113-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: UCBPP-PA14Imported.

    Entry informationi

    Entry nameiQ02FT9_PSEAB
    AccessioniPrimary (citable) accession number: Q02FT9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 14, 2006
    Last sequence update: November 14, 2006
    Last modified: October 1, 2014
    This is version 50 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