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Q8KBY0

- ACSA_CHLTE

UniProt

Q8KBY0 - ACSA_CHLTE

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 2 (26 Sep 2003)
      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 sitei323 – 3231Coenzyme AUniRule annotation
    Binding sitei347 – 3471Coenzyme AUniRule annotation
    Binding sitei512 – 5121ATPUniRule annotation
    Binding sitei527 – 5271ATPUniRule annotation
    Binding sitei535 – 5351Coenzyme A; via carbonyl oxygenUniRule annotation
    Binding sitei538 – 5381ATPUniRule annotation
    Metal bindingi549 – 5491Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi551 – 5511Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi554 – 5541Magnesium; via carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi399 – 4013ATPUniRule annotation
    Nucleotide bindingi423 – 4286ATPUniRule 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

    BioCyciCTEP194439:GHN0-1691-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
    Synonyms:acs
    Ordered Locus Names:CT1652
    OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
    Taxonomic identifieri194439 [NCBI]
    Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
    ProteomesiUP000001007: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 659659Acetyl-coenzyme A synthetasePRO_0000208360Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei621 – 6211N6-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

    STRINGi194439.CT1652.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8KBY0.
    SMRiQ8KBY0. Positions 23-656.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni205 – 2084Coenzyme A bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0365.
    HOGENOMiHOG000229981.
    KOiK01895.
    OMAiGGCEAVT.
    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.

    Q8KBY0-1 [UniParc]FASTAAdd to Basket

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    MATEQTKGQS SESISSVLSE RRKFPPPEAF SSQSHISSME QYEKLYADAA    50
    ADPDKYWGDL AEQFHWFKKW DSVLEWNAPY AKWFNGGTTN IAYNCLDVHV 100
    GSWRKNKAAI IWEGEEGNER ILTYGELHRQ VSKFANVLKI AGIKPGDKVA 150
    IYMGMVPELV IAVLACARVG AVHNVIFAGF AAHAITERVN DSRAKIVICA 200
    DGTRRRGSTI NLKNIVDEAI INTPSVKNVI VLKVTGEEIH MHDGMDHWWH 250
    DLMGLAVDEC EPAQVDSEHP LFLLYTSGST GKPKGILHTT AGYMVHAASS 300
    FKYVFDIKDE DIYFCTADIG WITGHTYIIY GPLLNGATVF MYEGAPNYPQ 350
    WDRFWDIINR HKITILYTAP TAIRAFIRAG NEWVTKHDLS SLRLLGTVGE 400
    PINPEAWMWY HKYVGQEKCP IVDTWWQTET GGIMISPMPG ATPTKPGTAT 450
    RPLPGIMVDV VRKDGTPCNA NEGGYLVVKR PWPSMLRTIY GDNERYEKTY 500
    WSEFPGMYFT GDGARKDDDG YIWIMGRVDD VVNVSGHRLG TSEVESALVS 550
    HEAVAEAAVV SRPDEIKGNA LVAFVTLKDG YEGDAKLRDS LGKHVAKEIG 600
    AIAKPDEIRW AKGLPKTRSG KIMRRLLREL ATSNEIKGDV TTLEDLGVIE 650
    NLREQEDEG 659
    Length:659
    Mass (Da):73,576
    Last modified:September 26, 2003 - v2
    Checksum:i2BB84C9AB13EA034
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006470 Genomic DNA. Translation: AAM72877.1.
    RefSeqiNP_662535.2. NC_002932.3.

    Genome annotation databases

    EnsemblBacteriaiAAM72877; AAM72877; CT1652.
    GeneIDi1006138.
    KEGGicte:CT1652.
    PATRICi21401177. VBIChlTep116050_1493.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006470 Genomic DNA. Translation: AAM72877.1 .
    RefSeqi NP_662535.2. NC_002932.3.

    3D structure databases

    ProteinModelPortali Q8KBY0.
    SMRi Q8KBY0. Positions 23-656.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 194439.CT1652.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM72877 ; AAM72877 ; CT1652 .
    GeneIDi 1006138.
    KEGGi cte:CT1652.
    PATRICi 21401177. VBIChlTep116050_1493.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CTEP194439:GHN0-1691-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 49652 / DSM 12025 / TLS.

    Entry informationi

    Entry nameiACSA_CHLTE
    AccessioniPrimary (citable) accession number: Q8KBY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: September 26, 2003
    Last modified: October 1, 2014
    This is version 71 of the entry and version 2 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