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Q5P9T3

- PANC_ANAMM

UniProt

Q5P9T3 - PANC_ANAMM

Protein

Pantothenate synthetase

Gene

panC

Organism
Anaplasma marginale (strain St. Maries)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 2 (02 Oct 2007)
      Previous versions | rss
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    • Comment

    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 sitei35 – 351Proton donorUniRule annotation
    Binding sitei59 – 591Beta-alanineUniRule annotation
    Binding sitei59 – 591PantoateUniRule annotation
    Binding sitei174 – 1741ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi28 – 358ATPUniRule annotation
    Nucleotide bindingi145 – 1484ATPUniRule annotation
    Nucleotide bindingi182 – 1854ATPUniRule 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

    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:AM1089
    OrganismiAnaplasma marginale (strain St. Maries)
    Taxonomic identifieri234826 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma
    ProteomesiUP000006557: 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 – 277277Pantothenate synthetasePRO_0000305391Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi234826.AM1089.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5P9T3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the pantothenate synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0414.
    HOGENOMiHOG000175516.
    KOiK01918.
    OMAiEIDYVEV.
    OrthoDBiEOG6Z6FZ4.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00158. PanC.
    InterProiIPR004821. Cyt_trans-like.
    IPR003721. Pantoate_ligase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
    PfamiPF02569. Pantoate_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
    TIGR00018. panC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q5P9T3-1 [UniParc]FASTAAdd to Basket

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    MEIVRDVESV RAVLRPFTNR KIGLVPTMGA LHSGHLSLVH EMKKHADVVI    50
    VSIFVNPLQF SPGEDYEKYP RCEEVDCEKC ASAGVDVVYI PSAEGMYPDG 100
    FSTSVDIGPM ARELCGASRQ NFINGIMVVL IKLVMQTNAH CMILGEKDYQ 150
    MLHLTRQLFR DLNIGVDVLQ GNTVRSAEGL ALSSRHQYLS SAEITKANFL 200
    YGFLLEVGQQ LSDDPHGQQE IIARGKLRLE QEGFEVDYLE VRDNNTLEHM 250
    QTFRKPARVF LAVYLGNCRL IDNVLLA 277
    Length:277
    Mass (Da):31,057
    Last modified:October 2, 2007 - v2
    Checksum:i29ADC2883893FD5E
    GO

    Sequence cautioni

    The sequence AAV86947.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000030 Genomic DNA. Translation: AAV86947.1. Different initiation.
    RefSeqiYP_154202.1. NC_004842.2.

    Genome annotation databases

    EnsemblBacteriaiAAV86947; AAV86947; AM1089.
    GeneIDi3171235.
    KEGGiama:AM1089.
    PATRICi20948069. VBIAnaMar46146_0947.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000030 Genomic DNA. Translation: AAV86947.1 . Different initiation.
    RefSeqi YP_154202.1. NC_004842.2.

    3D structure databases

    ProteinModelPortali Q5P9T3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 234826.AM1089.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV86947 ; AAV86947 ; AM1089 .
    GeneIDi 3171235.
    KEGGi ama:AM1089.
    PATRICi 20948069. VBIAnaMar46146_0947.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00028 ; UER00005 .

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    HAMAPi MF_00158. PanC.
    InterProi IPR004821. Cyt_trans-like.
    IPR003721. Pantoate_ligase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR21299:SF1. PTHR21299:SF1. 1 hit.
    Pfami PF02569. Pantoate_ligase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
    TIGR00018. panC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
      Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: St. Maries.

    Entry informationi

    Entry nameiPANC_ANAMM
    AccessioniPrimary (citable) accession number: Q5P9T3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 2, 2007
    Last sequence update: October 2, 2007
    Last modified: October 1, 2014
    This is version 59 of the entry and version 2 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