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C0QTA7

- PDXA_PERMH

UniProt

C0QTA7 - PDXA_PERMH

Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Persephonella marina (strain DSM 14350 / EX-H1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (05 May 2009)
      Previous versions | rss
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    Functioni

    Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).UniRule annotation

    Catalytic activityi

    4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH.

    Cofactori

    Binds 1 divalent metal cation per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei129 – 1291SubstrateUniRule annotation
    Binding sitei130 – 1301SubstrateUniRule annotation
    Metal bindingi159 – 1591Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi204 – 2041Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi257 – 2571Divalent metal cation; shared with dimeric partnerUniRule annotation
    Binding sitei265 – 2651SubstrateUniRule annotation
    Binding sitei274 – 2741SubstrateUniRule annotation
    Binding sitei283 – 2831SubstrateUniRule annotation

    GO - Molecular functioni

    1. 4-hydroxythreonine-4-phosphate dehydrogenase activity Source: UniProtKB-HAMAP
    2. metal ion binding Source: UniProtKB-HAMAP
    3. NAD binding Source: InterPro

    GO - Biological processi

    1. pyridoxal phosphate biosynthetic process Source: UniProtKB-HAMAP
    2. pyridoxine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pyridoxine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, NADP

    Enzyme and pathway databases

    BioCyciPMAR123214:GIZP-124-MONOMER.
    UniPathwayiUPA00244; UER00312.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotation (EC:1.1.1.262UniRule annotation)
    Alternative name(s):
    4-(phosphohydroxy)-L-threonine dehydrogenaseUniRule annotation
    Gene namesi
    Name:pdxAUniRule annotation
    Ordered Locus Names:PERMA_0123
    OrganismiPersephonella marina (strain DSM 14350 / EX-H1)
    Taxonomic identifieri123214 [NCBI]
    Taxonomic lineageiBacteriaAquificaeAquificalesHydrogenothermaceaePersephonella
    ProteomesiUP000001366: 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 – 3193194-hydroxythreonine-4-phosphate dehydrogenasePRO_1000146491Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi123214.PERMA_0123.

    Structurei

    3D structure databases

    ProteinModelPortaliC0QTA7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PdxA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1995.
    HOGENOMiHOG000221591.
    KOiK00097.
    OMAiAPINKHN.
    OrthoDBiEOG6GN6ZC.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    HAMAPiMF_00536. PdxA.
    InterProiIPR024084. IsoPropMal-DH-like_dom.
    IPR005255. PdxA.
    [Graphical view]
    PfamiPF04166. PdxA. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00557. pdxA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    C0QTA7-1 [UniParc]FASTAAdd to Basket

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    MKKIGITLGD PSGISPEILI KSIDKLKKAI YVIYGSYKII EKVSSILDKK    50
    TEINIIDSPE EAEKEGVYLI NVYDRDFCVG KPDKETGKAS VLFLERAVKD 100
    ILSKKLDAIV TLPISKEYVM KAGFRYAGHT DYLADITKTE DYLMMLLCEK 150
    MKVALVTTHI PLKDVPENIK PEILESKIRL LNRELQSKFG IKKPKIAVLG 200
    LNPHAGDGGN IGREEIDIIN PVVQKLKSEG IDLEGSLSAD TAFNRYREFD 250
    AYLAMYHDQG LIPLKLLCFK KAVNITLGIP FIRTSPDHGT GFDIAGKGIA 300
    DPSSFIEAVK LALKLSKQY 319
    Length:319
    Mass (Da):35,461
    Last modified:May 5, 2009 - v1
    Checksum:i547F5F5A236D08C2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001230 Genomic DNA. Translation: ACO03563.1.
    RefSeqiYP_002729922.1. NC_012440.1.

    Genome annotation databases

    EnsemblBacteriaiACO03563; ACO03563; PERMA_0123.
    GeneIDi7675488.
    KEGGipmx:PERMA_0123.
    PATRICi22913725. VBIPerMar119911_0182.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001230 Genomic DNA. Translation: ACO03563.1 .
    RefSeqi YP_002729922.1. NC_012440.1.

    3D structure databases

    ProteinModelPortali C0QTA7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 123214.PERMA_0123.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACO03563 ; ACO03563 ; PERMA_0123 .
    GeneIDi 7675488.
    KEGGi pmx:PERMA_0123.
    PATRICi 22913725. VBIPerMar119911_0182.

    Phylogenomic databases

    eggNOGi COG1995.
    HOGENOMi HOG000221591.
    KOi K00097.
    OMAi APINKHN.
    OrthoDBi EOG6GN6ZC.

    Enzyme and pathway databases

    UniPathwayi UPA00244 ; UER00312 .
    BioCyci PMAR123214:GIZP-124-MONOMER.

    Family and domain databases

    Gene3Di 3.40.718.10. 1 hit.
    HAMAPi MF_00536. PdxA.
    InterProi IPR024084. IsoPropMal-DH-like_dom.
    IPR005255. PdxA.
    [Graphical view ]
    Pfami PF04166. PdxA. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00557. pdxA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 14350 / EX-H1.

    Entry informationi

    Entry nameiPDXA_PERMH
    AccessioniPrimary (citable) accession number: C0QTA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 40 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is located at the dimer interface.UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3