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G2LZH4

- G2LZH4_9XANT

UniProt

G2LZH4 - G2LZH4_9XANT

Protein

Acetyl-coenzyme A synthetase

Gene

acsA

Organism
Xanthomonas axonopodis pv. citrumelo F1
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 19 (01 Oct 2014)
      Sequence version 1 (16 Nov 2011)
      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 sitei335 – 3351Coenzyme AUniRule annotation
    Binding sitei359 – 3591Coenzyme AUniRule annotation
    Binding sitei411 – 4111Substrate; via nitrogen amideUniRule annotation
    Binding sitei524 – 5241SubstrateUniRule annotation
    Binding sitei539 – 5391SubstrateUniRule annotation
    Active sitei541 – 5411UniRule annotation
    Binding sitei547 – 5471Coenzyme AUniRule annotation
    Binding sitei550 – 5501SubstrateUniRule annotation
    Metal bindingi561 – 5611Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi563 – 5631Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi566 – 5661Magnesium; via carbonyl oxygenUniRule annotation
    Binding sitei608 – 6081Coenzyme 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 annotation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciXALF981368:GH9H-4049-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
    ORF Names:XACM_4049Imported
    OrganismiXanthomonas axonopodis pv. citrumelo F1Imported
    Taxonomic identifieri981368 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    ProteomesiUP000001276: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei633 – 6331N6-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

    ProteinModelPortaliG2LZH4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni435 – 4406Substrate 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.

    G2LZH4-1 [UniParc]FASTAAdd to Basket

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    MRHTDCLPRA AATPSSDKFI ASEGAMADVY PVDPAFAADA RVTREQYAAL    50
    YRESIEHPEQ FWGKAAQRLE WFKQPTQIKD VSYALDDFHI RWFGDGELNA 100
    SVNCLDRQLA TRGDKTALLF EPDSPDAQSY PVTYRELYER VCKLGNALRN 150
    LGVKKGDRVT IYLPMIVDAA VAMLACARIG AVHSVVFGGF AANSIADRVI 200
    DCQSKLIITA DEGLRGGKKI PLKANVDAAL KIPGTDTVET VLVVRHTGGA 250
    VEMQAPRDRW FHDVVDGQPA ECTPERMNAE DPLFILYTSG STGKPKGVLH 300
    TTAGYLLFAS YTHEVVFDLR EDDIYWCTAD VGWVTGHSYI VYGPLANGAT 350
    AVMFEGVPNY PNVSRFWEVI DKHQVTIFYT APTAIRALMR DGAEPVKKTS 400
    RKSLRLLGSV GEPINPEAWR WYYEVVGDSR CPIVDTWWQT ETGGILISPL 450
    AGAVDLKPGS ATLPFFGVQP ALVDAEGKIL EGATEGNLVL LDSWPGQMRS 500
    VYGDHQRFID TYFRTYPGSY FTGDGCRRDA DGYYWITGRV DDVINVSGHR 550
    IGTAEVESAL VSHPKVAEAA VVGFPHDVKG QGIYAYVTLI AGQSPSEDLH 600
    KELVSWVRKE IGPIASPDHL QWAPGLPKTR SGKIMRRILR KIAENAPDQL 650
    GDTSTLADPS VVDSLVNERL AR 672
    Length:672
    Mass (Da):73,981
    Last modified:November 16, 2011 - v1
    Checksum:iC64B5C7E0CC4FDCF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002914 Genomic DNA. Translation: AEO44285.1.
    RefSeqiWP_014091438.1. NC_016010.1.
    YP_004853583.1. NC_016010.1.

    Genome annotation databases

    EnsemblBacteriaiAEO44285; AEO44285; XACM_4049.
    GeneIDi11131323.
    KEGGixax:XACM_4049.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP002914 Genomic DNA. Translation: AEO44285.1 .
    RefSeqi WP_014091438.1. NC_016010.1.
    YP_004853583.1. NC_016010.1.

    3D structure databases

    ProteinModelPortali G2LZH4.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEO44285 ; AEO44285 ; XACM_4049 .
    GeneIDi 11131323.
    KEGGi xax:XACM_4049.

    Phylogenomic databases

    KOi K01895.

    Enzyme and pathway databases

    BioCyci XALF981368:GH9H-4049-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. "Comparative Genomic Analysis of Xanthomonas axonopodis pv. citrumelo F1, Which Causes Citrus Bacterial Spot Disease, and Related Strains Provides Insights into Virulence and Host Specificity."
      Jalan N., Aritua V., Kumar D., Yu F., Jones J.B., Graham J.H., Setubal J.C., Wang N.
      J. Bacteriol. 193:6342-6357(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: F1Imported.

    Entry informationi

    Entry nameiG2LZH4_9XANT
    AccessioniPrimary (citable) accession number: G2LZH4
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 16, 2011
    Last sequence update: November 16, 2011
    Last modified: October 1, 2014
    This is version 19 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