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Q16B70

- Q16B70_ROSDO

UniProt

Q16B70 - Q16B70_ROSDO

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (25 Jul 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 sitei298 – 2981Coenzyme AUniRule annotation
    Binding sitei374 – 3741Substrate; via nitrogen amideUniRule annotation
    Binding sitei489 – 4891SubstrateUniRule annotation
    Binding sitei504 – 5041SubstrateUniRule annotation
    Active sitei506 – 5061UniRule annotation
    Binding sitei512 – 5121Coenzyme AUniRule annotation
    Binding sitei515 – 5151SubstrateUniRule annotation
    Metal bindingi526 – 5261Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi528 – 5281Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi531 – 5311Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei573 – 5731Coenzyme 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

    BioCyciRDEN375451:GJIZ-1047-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 annotationImported
    Ordered Locus Names:RD1_1117Imported
    OrganismiRoseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans)Imported
    Taxonomic identifieri375451 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRoseobacter
    ProteomesiUP000007029: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei598 – 5981N6-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

    STRINGi375451.RD1_1117.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16B70.
    SMRiQ16B70. Positions 11-634.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni398 – 4036Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    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.

    Q16B70-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRTPHVTLS QYASLYSESV SDSEGFWRRE GGRVDWIKPF TKVRDVNFDL    50
    GSVSINWYGD GTLNVAANCV DRHLATRADQ TAIIWEPDDP KDAAKHITYK 100
    QLHVSVCKMA NVLESLGVRR GDRVVIYLPM IPEAAYAMLA CARIGAIHSI 150
    VFAGFSPDAL AARINGSDAK VVITADHAPR GGRATALKAN TDAALLHCKD 200
    SVKCLVVKRT GGQTTWIDGR DFDCGEMMLE ASDVSHPAEM NAEDPLFILY 250
    TSGSTGQPKG VVHTSGGYLT YAAMTHEIVF DYHDGDVFWC TADVGWVTGH 300
    SYIVYGPLAN GATTIMFEGV PTYPDASRFW QVCEKHKVNQ FYTAPTAIRA 350
    LMGQGKEFVE KCDLSDLKVL GTVGEPINPE AWNWYNDVVG KGKCPIVDTW 400
    WQTETGGHLM TPLPGAHTMK PGSAMKPFFG IKPMVLEPAS GEVLEGNDVE 450
    GVLVIADSWP GQMRTIWGDH ERFEKTYFSD YKGYYFTGDG CKRDADGDYW 500
    ITGRVDDVIN VSGHRMGTAE VESALVAHAK VAEAAVVGYP HDIKGQGIYC 550
    YVTLMNGEEP SDELYQELRK WVRAEIGPIA SPDLIQWAPG LPKTRSGKIM 600
    RRILRKIAED DFATLGDTST LADPTVVDDL IKNRMNKQDA 640
    Length:640
    Mass (Da):70,426
    Last modified:July 25, 2006 - v1
    Checksum:i892116E2437F2578
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000362 Genomic DNA. Translation: ABG30773.1.
    RefSeqiYP_681459.1. NC_008209.1.

    Genome annotation databases

    EnsemblBacteriaiABG30773; ABG30773; RD1_1117.
    GeneIDi4197563.
    KEGGirde:RD1_1117.
    PATRICi23360369. VBIRosDen86677_1079.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000362 Genomic DNA. Translation: ABG30773.1 .
    RefSeqi YP_681459.1. NC_008209.1.

    3D structure databases

    ProteinModelPortali Q16B70.
    SMRi Q16B70. Positions 11-634.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 375451.RD1_1117.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABG30773 ; ABG30773 ; RD1_1117 .
    GeneIDi 4197563.
    KEGGi rde:RD1_1117.
    PATRICi 23360369. VBIRosDen86677_1079.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci RDEN375451:GJIZ-1047-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: ATCC 33942 / OCh 114Imported.

    Entry informationi

    Entry nameiQ16B70_ROSDO
    AccessioniPrimary (citable) accession number: Q16B70
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 25, 2006
    Last sequence update: July 25, 2006
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3