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A6WXV8

- ACSA_OCHA4

UniProt

A6WXV8 - ACSA_OCHA4

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (21 Aug 2007)
      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 sitei586 – 5861Coenzyme 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

    BioCyciOANT439375:GJIT-1108-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:Oant_1092
    OrganismiOchrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168)
    Taxonomic identifieri439375 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum
    ProteomesiUP000002301: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 651651Acetyl-coenzyme A synthetasePRO_1000065300Add
    BLAST

    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

    Acetylation

    Interactioni

    Protein-protein interaction databases

    STRINGi439375.Oant_1092.

    Structurei

    3D structure databases

    ProteinModelPortaliA6WXV8.
    SMRiA6WXV8. Positions 17-648.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni189 – 1924Coenzyme A bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiAWIWYRD.
    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.

    A6WXV8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEKLYPVLA EAKRNTLIDN ATYLEWYQES VSDPDSFWAK HGRRIDWFKP    50
    FTKVKNTDFN GDVSIKWYED GVTNVSYNCI DRHLKSRGDQ VAIIWEGDNP 100
    YIDKKITYRE LHENVCRLAN VLKKHGVKKG DRVTIYLPMI PEAAYAMLAC 150
    ARIGAVHSVV FAGFSPEALA GRIVDCESTF VITADEGVRG GKPVPLKENT 200
    DTAIDIAAKQ YVMVNKVLTV RRTGGKVSWG PGRDLWYHQE VASVEPTCDP 250
    EPMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHQ YVFDYHDGDI 300
    YWCTADVGWV TGHSYIVYGP LANGATTLMF EGVPNFPDQG RFWEVVDKHH 350
    VNIFYTAPTA IRALMGAGDE FVTRSSRSTL RLLGSVGEPI NPEAWEWYYN 400
    VVGDQRSPIV DTWWQTETGG ILITPLPGAT DLKPGSATRP FFGIKPELVD 450
    NEGAVIEGAV DGNLCIIDSW PGQMRTLYGD HKRFIEAYFS TYKGKYFTGD 500
    GCRRDEDGYY WITGRVDDVL NISGHRLGTA EIESALVSHH SVSEAAVVGY 550
    PHPIKGQGIY CYVTLMTGEA VQDEDALRKE LTQHVRKEIG PIATPDKIQF 600
    SPGLPKTRSG KIMRRILRKI AEDEFGALGD TSTLADPGVV DDLIENRQNK 650
    K 651
    Length:651
    Mass (Da):72,591
    Last modified:August 21, 2007 - v1
    Checksum:i6B8B09BA21A762B7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000758 Genomic DNA. Translation: ABS13812.1.
    RefSeqiWP_010661479.1. NC_009667.1.
    YP_001369641.1. NC_009667.1.

    Genome annotation databases

    EnsemblBacteriaiABS13812; ABS13812; Oant_1092.
    GeneIDi5380140.
    KEGGioan:Oant_1092.
    PATRICi20467255. VBIOchAnt73124_1142.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000758 Genomic DNA. Translation: ABS13812.1 .
    RefSeqi WP_010661479.1. NC_009667.1.
    YP_001369641.1. NC_009667.1.

    3D structure databases

    ProteinModelPortali A6WXV8.
    SMRi A6WXV8. Positions 17-648.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 439375.Oant_1092.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABS13812 ; ABS13812 ; Oant_1092 .
    GeneIDi 5380140.
    KEGGi oan:Oant_1092.
    PATRICi 20467255. VBIOchAnt73124_1142.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci OANT439375:GJIT-1108-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. "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic pathogen and symbiont of several eukaryotic hosts."
      Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.
      J. Bacteriol. 193:4274-4275(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49188 / DSM 6882 / NCTC 12168.

    Entry informationi

    Entry nameiACSA_OCHA4
    AccessioniPrimary (citable) accession number: A6WXV8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 49 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