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H2IS18

- H2IS18_RAHAC

UniProt

H2IS18 - H2IS18_RAHAC

Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / CIP 78.65)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 15 (01 Oct 2014)
      Sequence version 1 (21 Mar 2012)
      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. Acs undergoes a two-step reaction. In the first half reaction, Acs 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
    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
    Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.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 sitei312 – 3121Coenzyme AUniRule annotation
    Binding sitei336 – 3361Coenzyme AUniRule annotation
    Binding sitei388 – 3881Substrate; via nitrogen amideUniRule annotation
    Binding sitei501 – 5011SubstrateUniRule annotation
    Binding sitei516 – 5161SubstrateUniRule annotation
    Active sitei518 – 5181UniRule annotation
    Binding sitei524 – 5241Coenzyme AUniRule annotation
    Binding sitei527 – 5271SubstrateUniRule annotation
    Metal bindingi538 – 5381Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi540 – 5401Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi543 – 5431Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei585 – 5851Coenzyme 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: UniProtKB-HAMAP
    2. chemotaxis Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    LigaseUniRule annotationImported

    Keywords - Ligandi

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

    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:acsUniRule annotation
    Ordered Locus Names:Rahaq2_0411Imported
    OrganismiRahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / CIP 78.65)Imported
    Taxonomic identifieri745277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeRahnella
    ProteomesiUP000009010: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei610 – 6101N6-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

    ProteinModelPortaliH2IS18.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni192 – 1954Coenzyme AUniRule annotation
    Regioni412 – 4176Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK01895.

    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.

    H2IS18-1 [UniParc]FASTAAdd to Basket

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    MSHVYKHPIP ASVAERTLIT PEKYQQYYQQ SVEDPDAFWG EQAKVLDWIK    50
    PFTKVKNTSF APGNVDIRWF EDGTLNLAAN CLDRHLTDKG DQTALVWEGD 100
    DPKAENKYVT YKQLHHDVCQ FANVLKGLGV KKGDVVAIYM PMVPEAAVAM 150
    LACARIGAVH SVIFAGFSPE AVAGRIVDSN AKLVITADEG LRAGRTIPLK 200
    QNVDDALKNP AVTSITHSII FKRTGKQGEW KEGRDIWWHD AIEGVSADCP 250
    PEEMKAEDPL FILYTSGSTG KPKGVLHTTG GYLVYAALTF KYTFDYHDGD 300
    IYWCTADVGW VTGHSYLLYG PLACGAISLM FEGVPNYPTP ARMAQVIDKH 350
    KVNILYTAPT AIRALMAEGD KAIEGTSRAS LRIMGSVGEP INPEAWEWYY 400
    KTIGNSQCPI VDTWWQTETG GFMITPLPGA TELKAGSATR PFFGVQPALV 450
    DNEGVPQEGA CEGNLVITDS WPGQARTLFG DHERFEQTYF STFKNMYFSG 500
    DGARRDEDGY YWITGRVDDV LNISGHRLGT AEIESALVSH PKIAEAAVVG 550
    IPHNIKGQAI YAYITLNHGE EPSPELYTEV RNWVRKEIGS IATPDILHWT 600
    DSLPKTRSGK IMRRILRKIA AGDTSNLGDT STLADPGVVD KLLEEKQSMK 650
    VPS 653
    Length:653
    Mass (Da):72,038
    Last modified:March 21, 2012 - v1
    Checksum:iE00B70418C59D169
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003244 Genomic DNA. Translation: AEX50349.1.
    RefSeqiYP_005198489.1. NC_016818.1.

    Genome annotation databases

    EnsemblBacteriaiAEX50349; AEX50349; Rahaq2_0411.
    GeneIDi11790113.
    KEGGiraq:Rahaq2_0411.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003244 Genomic DNA. Translation: AEX50349.1 .
    RefSeqi YP_005198489.1. NC_016818.1.

    3D structure databases

    ProteinModelPortali H2IS18.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEX50349 ; AEX50349 ; Rahaq2_0411 .
    GeneIDi 11790113.
    KEGGi raq:Rahaq2_0411.

    Phylogenomic databases

    KOi K01895.

    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 sequence of chromosome of Rahnella aquatilis CIP 78.65."
      Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P., Martinez R., Woyke T.
      Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / CIP 78.65Imported.

    Entry informationi

    Entry nameiH2IS18_RAHAC
    AccessioniPrimary (citable) accession number: H2IS18
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 21, 2012
    Last sequence update: March 21, 2012
    Last modified: October 1, 2014
    This is version 15 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