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Q88EH6

- ACSA1_PSEPK

UniProt

Q88EH6 - ACSA1_PSEPK

Protein

Acetyl-coenzyme A synthetase 1

Gene

acsA1

Organism
Pseudomonas putida (strain KT2440)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 sitei311 – 3111Coenzyme AUniRule annotation
    Binding sitei335 – 3351Coenzyme AUniRule annotation
    Binding sitei500 – 5001ATPUniRule annotation
    Binding sitei515 – 5151ATPUniRule annotation
    Binding sitei523 – 5231Coenzyme A; via carbonyl oxygenUniRule annotation
    Binding sitei526 – 5261ATPUniRule 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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi387 – 3893ATPUniRule annotation
    Nucleotide bindingi411 – 4166ATPUniRule 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

    Ligase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciPPUT160488:GIXO-4574-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-coenzyme A synthetase 1UniRule annotation (EC:6.2.1.1UniRule annotation)
    Short name:
    AcCoA synthetase 1UniRule annotation
    Short name:
    Acs 1UniRule annotation
    Alternative name(s):
    Acetate--CoA ligase 1UniRule annotation
    Acyl-activating enzyme 1UniRule annotation
    Gene namesi
    Name:acsA1UniRule annotation
    Ordered Locus Names:PP_4487
    OrganismiPseudomonas putida (strain KT2440)
    Taxonomic identifieri160488 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000000556: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 653653Acetyl-coenzyme A synthetase 1PRO_0000208376Add
    BLAST

    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

    Acetylation

    Interactioni

    Protein-protein interaction databases

    STRINGi160488.PP_4487.

    Structurei

    3D structure databases

    ProteinModelPortaliQ88EH6.
    SMRiQ88EH6. Positions 7-647.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni191 – 1944Coenzyme A bindingUniRule annotation

    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.

    Q88EH6-1 [UniParc]FASTAAdd to Basket

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    MSAAPLYPVR PEVAATTLTD EATYKAMYQQ SVINPDGFWR EQAQRIDWIK    50
    PFTKVKQTSF DDHHVDIKWF ADGTLNVSSN CLDRHLEERG DQLAIIWEGD 100
    DPSEHRNITY RELHEQVCKF ANALRGQDVH RGDVVTIYMP MIPEAVVAML 150
    ACARIGAIHS VVFGGFSPEA LAGRIIDCKS KVVITADEGV RGGRRTPLKA 200
    NVDLALTNPE TSSVQKIIVC KRTGGDIAWH QHRDIWYEDL MKVASSHCAP 250
    KEMGAEEALF ILYTSGSTGK PKGVLHTTGG YLVYAALTHE RVFDYRPGEV 300
    YWCTADVGWV TGHSYIVYGP LANGATTLLF EGVPNYPDIT RVSKIVDKHK 350
    VNILYTAPTA IRAMMAEGQA AVEGADGSSL RLLGSVGEPI NPEAWNWYYK 400
    TVGKERCPIV DTWWQTETGG ILISPLPGAT GLKPGSATRP FFGVVPALVD 450
    NLGNLIDGAA EGNLVILDSW PGQSRSLYGD HDRFVDTYFK TFRGMYFTGD 500
    GARRDEDGYY WITGRVDDVL NVSGHRMGTA EIESAMVAHS KVAEAAVVGV 550
    PHDIKGQGIY VYVTLNAGIE ASEQLRLELK NWVRKEIGPI ASPDVIQWAP 600
    GLPKTRSGKI MRRILRKIAT GEYDALGDIS TLADPGVVQH LIDTHKAMNL 650
    ASA 653
    Length:653
    Mass (Da):71,797
    Last modified:June 1, 2003 - v1
    Checksum:iCE626C86C922E8F4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015451 Genomic DNA. Translation: AAN70062.1.
    RefSeqiNP_746598.1. NC_002947.3.

    Genome annotation databases

    EnsemblBacteriaiAAN70062; AAN70062; PP_4487.
    GeneIDi1042436.
    KEGGippu:PP_4487.
    PATRICi19947676. VBIPsePut30601_4775.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015451 Genomic DNA. Translation: AAN70062.1 .
    RefSeqi NP_746598.1. NC_002947.3.

    3D structure databases

    ProteinModelPortali Q88EH6.
    SMRi Q88EH6. Positions 7-647.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 160488.PP_4487.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN70062 ; AAN70062 ; PP_4487 .
    GeneIDi 1042436.
    KEGGi ppu:PP_4487.
    PATRICi 19947676. VBIPsePut30601_4775.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PPUT160488:GIXO-4574-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: KT2440.

    Entry informationi

    Entry nameiACSA1_PSEPK
    AccessioniPrimary (citable) accession number: Q88EH6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3