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Q1B2L8

- PANC_MYCSS

UniProt

Q1B2L8 - PANC_MYCSS

Protein

Pantothenate synthetase

Gene

panC

Organism
Mycobacterium sp. (strain MCS)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (11 Jul 2006)
      Previous versions | rss
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    Functioni

    Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.UniRule annotation

    Catalytic activityi

    ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei50 – 501Proton donorUniRule annotation
    Binding sitei75 – 751Beta-alanineUniRule annotation
    Binding sitei75 – 751PantoateUniRule annotation
    Binding sitei167 – 1671PantoateUniRule annotation
    Binding sitei190 – 1901ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi43 – 508ATPUniRule annotation
    Nucleotide bindingi161 – 1644ATPUniRule annotation
    Nucleotide bindingi198 – 2014ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. pantoate-beta-alanine ligase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. pantothenate biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Pantothenate biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMSP164756:GHQ8-4814-MONOMER.
    UniPathwayiUPA00028; UER00005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pantothenate synthetaseUniRule annotation (EC:6.3.2.1UniRule annotation)
    Short name:
    PSUniRule annotation
    Alternative name(s):
    Pantoate--beta-alanine ligaseUniRule annotation
    Pantoate-activating enzymeUniRule annotation
    Gene namesi
    Name:panCUniRule annotation
    Ordered Locus Names:Mmcs_4762
    OrganismiMycobacterium sp. (strain MCS)
    Taxonomic identifieri164756 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000001972: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Pantothenate synthetasePRO_0000305490Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi164756.Mmcs_4762.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1B2L8.
    SMRiQ1B2L8. Positions 9-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pantothenate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0414.
    HOGENOMiHOG000175516.
    KOiK01918.
    OMAiPTHFAGM.
    OrthoDBiEOG6Z6FZ4.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00158. PanC.
    InterProiIPR003721. Pantoate_ligase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF02569. Pantoate_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00018. panC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q1B2L8-1 [UniParc]FASTAAdd to Basket

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    MTARRPTRFA KGELNVYRAP RDVTDVTRAL RSTGRRVVLV PTMGALHEGH    50
    LTLIRAAKRV QGAVVVVSIF VNPLQFGAGE DLDAYPRTLD DDLAALRAEG 100
    VEIAFTPTVG DMYPDGTRTS VHPGPLGDDL EGASRPGHFA GVLTVVCKLL 150
    HIVRPDRAFF GEKDYQQLVL IRQMVTDLNI DTKIVGVPTV READGLALSS 200
    RNRYLDEVER EQAGALSAAL LAGMYAASNG AAATLDAARA VLDEVPAIEV 250
    DYLQVRDPML GPVPHEGAAR LLVAARLGQT RLLDNIAVDI GASDGIDGHP 300
    RVGSPDHQLP WRN 313
    Length:313
    Mass (Da):33,668
    Last modified:July 11, 2006 - v1
    Checksum:iF712971E5184A02D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000384 Genomic DNA. Translation: ABG10866.1.
    RefSeqiYP_641922.1. NC_008146.1.

    Genome annotation databases

    EnsemblBacteriaiABG10866; ABG10866; Mmcs_4762.
    GeneIDi4113591.
    KEGGimmc:Mmcs_4762.
    PATRICi18119920. VBIMycSp106721_4880.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000384 Genomic DNA. Translation: ABG10866.1 .
    RefSeqi YP_641922.1. NC_008146.1.

    3D structure databases

    ProteinModelPortali Q1B2L8.
    SMRi Q1B2L8. Positions 9-291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 164756.Mmcs_4762.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABG10866 ; ABG10866 ; Mmcs_4762 .
    GeneIDi 4113591.
    KEGGi mmc:Mmcs_4762.
    PATRICi 18119920. VBIMycSp106721_4880.

    Phylogenomic databases

    eggNOGi COG0414.
    HOGENOMi HOG000175516.
    KOi K01918.
    OMAi PTHFAGM.
    OrthoDBi EOG6Z6FZ4.

    Enzyme and pathway databases

    UniPathwayi UPA00028 ; UER00005 .
    BioCyci MSP164756:GHQ8-4814-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    HAMAPi MF_00158. PanC.
    InterProi IPR003721. Pantoate_ligase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF02569. Pantoate_ligase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00018. panC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MCS.

    Entry informationi

    Entry nameiPANC_MYCSS
    AccessioniPrimary (citable) accession number: Q1B2L8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: July 11, 2006
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The reaction proceeds by a bi uni uni bi ping pong mechanism.UniRule annotation

    Keywords - Technical termi

    Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3