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Q9CKG8

- PDXA_PASMU

UniProt

Q9CKG8 - PDXA_PASMU

Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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. Can use ions such as zinc, magnesium or cobalt.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi172 – 1721Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi216 – 2161Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi271 – 2711Divalent metal cation; shared with dimeric partnerUniRule annotation
    Binding sitei279 – 2791SubstrateUniRule annotation

    GO - Molecular functioni

    1. 4-hydroxythreonine-4-phosphate dehydrogenase activity Source: UniProtKB-HAMAP
    2. cobalt ion binding Source: UniProtKB-HAMAP
    3. magnesium ion binding Source: UniProtKB-HAMAP
    4. NAD binding Source: InterPro
    5. zinc ion binding Source: UniProtKB-HAMAP

    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

    Cobalt, Magnesium, Metal-binding, NAD, NADP, Zinc

    Enzyme and pathway databases

    BioCyciPMUL272843:GC8W-1712-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:PM1650
    OrganismiPasteurella multocida (strain Pm70)
    Taxonomic identifieri272843 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
    ProteomesiUP000000809: 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 – 3373374-hydroxythreonine-4-phosphate dehydrogenasePRO_0000188814Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272843.PM1650.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CKG8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PdxA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1995.
    HOGENOMiHOG000221593.
    KOiK00097.
    OMAiNLRVFFL.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9CKG8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKSTVALTL GDPAGIGPEL VAKLLAKQNI REKANIVLVA DKDELEKGME    50
    IAKAQFVYEE VSFHQLGQYE FKTGVPVLIS HKSSHPKPFE YGKVTEQSGV 100
    YILETLKVAL NLAKMGYVQA ICFAPLNKQA MHKGGLRYRD ELHWFAEQTD 150
    FNEFVCELNV VDDIWAARVT SHIPFKDIVP NLSIKGVFDC IHLLYRSLVQ 200
    AGVENPKIAV QALNPHGGEG GVFGDEEMTI IQPGMEQARK AGIDVYGPFP 250
    GDTTMREVER LKINGVVSMY HDQFSTALKI LGFERGVTVQ GGIPIPITTA 300
    NHGTAFDLHG KNIAIPTAFE AAFNIAVRMG QGVLNQK 337
    Length:337
    Mass (Da):37,033
    Last modified:June 1, 2001 - v1
    Checksum:i7D0955556B98D657
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK03734.1.
    RefSeqiNP_246589.1. NC_002663.1.

    Genome annotation databases

    EnsemblBacteriaiAAK03734; AAK03734; PM1650.
    GeneIDi1244997.
    KEGGipmu:PM1650.
    PATRICi22872591. VBIPasMul88067_1669.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK03734.1 .
    RefSeqi NP_246589.1. NC_002663.1.

    3D structure databases

    ProteinModelPortali Q9CKG8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272843.PM1650.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK03734 ; AAK03734 ; PM1650 .
    GeneIDi 1244997.
    KEGGi pmu:PM1650.
    PATRICi 22872591. VBIPasMul88067_1669.

    Phylogenomic databases

    eggNOGi COG1995.
    HOGENOMi HOG000221593.
    KOi K00097.
    OMAi NLRVFFL.
    OrthoDBi EOG6GN6ZC.

    Enzyme and pathway databases

    UniPathwayi UPA00244 ; UER00312 .
    BioCyci PMUL272843:GC8W-1712-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 ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Pm70.

    Entry informationi

    Entry nameiPDXA_PASMU
    AccessioniPrimary (citable) accession number: Q9CKG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 76 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