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Q89ZK3

- PDXA_BACTN

UniProt

Q89ZK3 - PDXA_BACTN

Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 sitei138 – 1381SubstrateUniRule annotation
    Binding sitei139 – 1391SubstrateUniRule annotation
    Metal bindingi169 – 1691Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi214 – 2141Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi269 – 2691Divalent metal cation; shared with dimeric partnerUniRule annotation
    Binding sitei277 – 2771SubstrateUniRule annotation
    Binding sitei286 – 2861SubstrateUniRule annotation
    Binding sitei295 – 2951SubstrateUniRule 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

    BioCyciBTHE226186:GJXV-4454-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:BT_4374
    OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
    Taxonomic identifieri226186 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
    ProteomesiUP000001414: 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 – 3643644-hydroxythreonine-4-phosphate dehydrogenasePRO_1000051491Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi226186.BT_4374.

    Structurei

    3D structure databases

    ProteinModelPortaliQ89ZK3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PdxA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1995.
    HOGENOMiHOG000221591.
    KOiK00097.
    OMAiKALAMED.
    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.

    Q89ZK3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEENKIRIGI TQGDINGVGY EVILKTFSDP TMLELCTPII YGSPKVAAYH    50
    RKALDVQANF SIVNTASEAG YNRLSVVNCT DDEVKVEFSK PDPEAGKAAL 100
    GALERAIEEY REGLIDVIVT APINKHTIQS EEFSFPGHTE YIEERLGNGN 150
    KSLMILMKND FRVALVTTHI PVREIATTIT KELIQEKLMI FHRCLKQDFG 200
    IGAPRIAVLS LNPHAGDGGL LGMEEQEIII PAMKEMEEKG IICYGPYAAD 250
    GFMGSGNYTH FDGILAMYHD QGLAPFKALA MEDGVNYTAG LPVVRTSPAH 300
    GTAYDIAGKG LASEDSFRQA IYVAIDVFRN RQREKAARVN PLRKQYYEKR 350
    DDSDKLKLDT VDED 364
    Length:364
    Mass (Da):40,325
    Last modified:June 1, 2003 - v1
    Checksum:iFD60351E6D30985A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015928 Genomic DNA. Translation: AAO79479.1.
    RefSeqiNP_813285.1. NC_004663.1.

    Genome annotation databases

    EnsemblBacteriaiAAO79479; AAO79479; BT_4374.
    GeneIDi1071722.
    KEGGibth:BT_4374.
    PATRICi21063810. VBIBacThe70966_4451.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015928 Genomic DNA. Translation: AAO79479.1 .
    RefSeqi NP_813285.1. NC_004663.1.

    3D structure databases

    ProteinModelPortali Q89ZK3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 226186.BT_4374.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO79479 ; AAO79479 ; BT_4374 .
    GeneIDi 1071722.
    KEGGi bth:BT_4374.
    PATRICi 21063810. VBIBacThe70966_4451.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00244 ; UER00312 .
    BioCyci BTHE226186:GJXV-4454-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. "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
      Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
      Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

    Entry informationi

    Entry nameiPDXA_BACTN
    AccessioniPrimary (citable) accession number: Q89ZK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 74 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