Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

I2EEB1

- I2EEB1_CROSK

UniProt

I2EEB1 - I2EEB1_CROSK

Protein

Acetyl-coenzyme A synthetase

Gene

acs

Organism
Cronobacter sakazakii ES15
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 16 (01 Oct 2014)
      Sequence version 1 (11 Jul 2012)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei311 – 3111Coenzyme AUniRule annotation
    Binding sitei335 – 3351Coenzyme AUniRule annotation
    Binding sitei387 – 3871Substrate; via nitrogen amideUniRule annotation
    Binding sitei500 – 5001SubstrateUniRule annotation
    Binding sitei515 – 5151SubstrateUniRule annotation
    Active sitei517 – 5171UniRule annotation
    Binding sitei523 – 5231Coenzyme AUniRule annotation
    Binding sitei526 – 5261SubstrateUniRule 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

    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 annotation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciCSAK1138308:GLC5-451-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:acsUniRule annotationImported
    ORF Names:ES15_0440Imported
    OrganismiCronobacter sakazakii ES15Imported
    Taxonomic identifieri1138308 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter
    ProteomesiUP000002877: Chromosome

    PTM / Processingi

    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

    AcetylationUniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliI2EEB1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni191 – 1944Coenzyme AUniRule annotation
    Regioni411 – 4166Substrate 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.

    I2EEB1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQIHKHPIP AAIAERCLIT PEQYDAKYQQ SVHDPDAFWG EQGKILDWIT    50
    PYQTVKNTSF APGNISIKWY EDGTLNLAAN CLDRHLSERG DQTAIIWEGD 100
    DATQSKHISY RELHRDVCRF ANTLTSLGIK KGDVVAIYMP MVPEAAVAML 150
    ACARIGAVHS VIFGGFSPEA VAGRIIDSSA RLVITADEGV RAGRAIPLKK 200
    NVDDALKNPG VTSVEHVVVL KRTGGNIEWH EGRDLWWSEL VEKASAHHQP 250
    VEMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFL YAFDYHPGDI 300
    YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPSAN RMAQVVDKHK 350
    VNILYTAPTA IRALMAEGDK AIDGTDRSSL RILGSVGEPI NPEAWEWYWK 400
    KIGNEKCPVI DTWWQTETGG FMITPLPGAT ELKAGSATRP FFGVQPALVD 450
    NEGNPQQGAT EGNLVITDSW PGQARTLFGD HERFEQTYFS TFKNMYFSGD 500
    GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVSHP KIAEAAVVGI 550
    PHSIKGQAIY AYVTLNHGEE PSAELYSEVR NWVRKEIGPL ATPDVLHWTD 600
    SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQSIAM 650
    PS 652
    Length:652
    Mass (Da):71,733
    Last modified:July 11, 2012 - v1
    Checksum:iD14199F1015FBDFD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003312 Genomic DNA. Translation: AFJ98013.1.
    RefSeqiYP_006341524.1. NC_017933.1.

    Genome annotation databases

    EnsemblBacteriaiAFJ98013; AFJ98013; ES15_0440.
    GeneIDi13032260.
    KEGGicsk:ES15_0440.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP003312 Genomic DNA. Translation: AFJ98013.1 .
    RefSeqi YP_006341524.1. NC_017933.1.

    3D structure databases

    ProteinModelPortali I2EEB1.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AFJ98013 ; AFJ98013 ; ES15_0440 .
    GeneIDi 13032260.
    KEGGi csk:ES15_0440.

    Phylogenomic databases

    KOi K01895.

    Enzyme and pathway databases

    BioCyci CSAK1138308:GLC5-451-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. "Complete Genome Sequence of the Opportunistic Food-Borne Pathogen Cronobacter sakazakii ES15."
      Shin H., Lee J.H., Choi Y., Ryu S.
      J. Bacteriol. 194:4438-4439(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ES15Imported.

    Entry informationi

    Entry nameiI2EEB1_CROSK
    AccessioniPrimary (citable) accession number: I2EEB1
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 11, 2012
    Last sequence update: July 11, 2012
    Last modified: October 1, 2014
    This is version 16 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