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)

C8X4E2

- C8X4E2_DESRD

UniProt

C8X4E2 - C8X4E2_DESRD

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Desulfohalobium retbaense (strain DSM 5692)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 1 (03 Nov 2009)
      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. 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 sitei322 – 3221Coenzyme AUniRule annotation
    Binding sitei398 – 3981Substrate; via nitrogen amideUniRule annotation
    Binding sitei511 – 5111SubstrateUniRule annotation
    Binding sitei526 – 5261SubstrateUniRule annotation
    Active sitei528 – 5281UniRule annotation
    Binding sitei534 – 5341Coenzyme AUniRule annotation
    Binding sitei537 – 5371SubstrateUniRule annotation
    Metal bindingi548 – 5481Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi550 – 5501Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi553 – 5531Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei595 – 5951Coenzyme 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 annotation, Metal-bindingUniRule annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciDRET485915:GHRJ-2180-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:Dret_2132Imported
    OrganismiDesulfohalobium retbaense (strain DSM 5692)Imported
    Taxonomic identifieri485915 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfohalobiaceaeDesulfohalobium
    ProteomesiUP000001052: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei620 – 6201N6-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

    STRINGi485915.Dret_2132.

    Structurei

    3D structure databases

    ProteinModelPortaliC8X4E2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni203 – 2064Coenzyme AUniRule annotation
    Regioni422 – 4276Substrate 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.

    C8X4E2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGGSDEHIES MMHERRHFPP PRHGSERAHI PGPEAYDDLR DQAARDPEGF    50
    WAERAKALLD WDSEWDTVLE ADWETPEFKW FAGGKLNACA NCLDRHVASG 100
    RGEKTALIWQ GEPEDDVRQF TYAELRDEVV KFAKVLKKWG VGKGDRVAVY 150
    LPMIPELPIA MLACARIGAV HSVVFAGFSA HSLQNRIQDC EAKVLITADA 200
    VIRAGKQIPL KTNGDEALEA CPSVEHCIVV NRAGLDVAMH EGRDVWWHDA 250
    VAGDDGTDCP PESMDAEDLL FILYTSGSTG KPKGVVHTTG GYLTYTAQTT 300
    QWVFDIQEDD VYWCTADIGW ITGHSYILYG PLALGATTVM FEGVPSYPQP 350
    DRFWQVVEKF KVTIFYTAPT VIRALMREGP QWTETRDLSS LRLLGSVGEP 400
    INPEAWMWYH DHVGKGELPV LDTWWQTETG GIMISAVPYA TTLKPGSASQ 450
    PLPGIEADIV DRDGEPVGPN RGGHLVVKTP WPGMLRNVYG DPARYKSTYF 500
    ERFPGMYESG DSARMDEEGY FWIMGRLDDV INVSGHRLGT AEIESALVAH 550
    EAVAEAAVVG MPHEVKGQAI YAYVTLKSTF QENDELRKVL RQHVRTEIGA 600
    IATPEIIQFA PGLPKTRSGK IMRRILRKIA ADETNAFGDT STLADPTVIA 650
    DLIDGKNLLG K 661
    Length:661
    Mass (Da):73,245
    Last modified:November 3, 2009 - v1
    Checksum:i0B1F90A93F31B941
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001734 Genomic DNA. Translation: ACV69416.1.
    RefSeqiWP_015752557.1. NC_013223.1.
    YP_003198994.1. NC_013223.1.

    Genome annotation databases

    EnsemblBacteriaiACV69416; ACV69416; Dret_2132.
    GeneIDi8419982.
    KEGGidrt:Dret_2132.
    PATRICi21701382. VBIDesRet71890_2248.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001734 Genomic DNA. Translation: ACV69416.1 .
    RefSeqi WP_015752557.1. NC_013223.1.
    YP_003198994.1. NC_013223.1.

    3D structure databases

    ProteinModelPortali C8X4E2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 485915.Dret_2132.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACV69416 ; ACV69416 ; Dret_2132 .
    GeneIDi 8419982.
    KEGGi drt:Dret_2132.
    PATRICi 21701382. VBIDesRet71890_2248.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci DRET485915:GHRJ-2180-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: DSM 5692Imported.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 5692Imported.

    Entry informationi

    Entry nameiC8X4E2_DESRD
    AccessioniPrimary (citable) accession number: C8X4E2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 3, 2009
    Last sequence update: November 3, 2009
    Last modified: October 1, 2014
    This is version 35 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