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Q9PN58

- PDXA_CAMJE

UniProt

Q9PN58 - PDXA_CAMJE

Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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
    Binding sitei148 – 1481SubstrateUniRule annotation
    Binding sitei149 – 1491SubstrateUniRule annotation
    Metal bindingi177 – 1771Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi216 – 2161Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi301 – 3011Divalent metal cation; shared with dimeric partnerUniRule annotation
    Binding sitei309 – 3091SubstrateUniRule annotation
    Binding sitei318 – 3181SubstrateUniRule annotation
    Binding sitei327 – 3271SubstrateUniRule 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

    BioCyciCJEJ192222:GJTS-1211-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:Cj1239
    OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
    Taxonomic identifieri192222 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
    ProteomesiUP000000799: 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_0000188802Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    IntActiQ9PN58. 2 interactions.
    STRINGi192222.Cj1239.

    Structurei

    Secondary structure

    1
    364
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75
    Turni11 – 144
    Helixi15 – 2612
    Turni27 – 293
    Beta strandi30 – 356
    Helixi38 – 4811
    Beta strandi54 – 629
    Beta strandi67 – 737
    Beta strandi75 – 8410
    Helixi103 – 12119
    Beta strandi124 – 1307
    Helixi135 – 1406
    Helixi148 – 1569
    Beta strandi161 – 1666
    Beta strandi169 – 1757
    Helixi180 – 1823
    Helixi183 – 1864
    Helixi189 – 20315
    Beta strandi206 – 2116
    Helixi215 – 2184
    Turni219 – 2224
    Helixi226 – 24419
    Helixi248 – 2547
    Helixi258 – 2669
    Helixi281 – 2844
    Helixi287 – 2926
    Beta strandi295 – 3006
    Helixi301 – 31111
    Turni313 – 3153
    Beta strandi317 – 3259
    Beta strandi327 – 3293
    Helixi348 – 35912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3TSNX-ray2.63A/B/C/D1-364[»]
    ProteinModelPortaliQ9PN58.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PdxA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1995.
    HOGENOMiHOG000221591.
    KOiK00097.
    OMAiISIKLAM.
    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.

    Q9PN58-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKLAISIGD INSIGLEILV RSHEELSKIC TPFYFIHESL LNKALKLLNL    50
    KLFNAKIVAF KDDKDYEFNF IKKENSLEIY SFCLPLGFKV DENFEIQAGE 100
    IDAKSGLYGF LSFKAASYFV YEKHAHALLT LPIHKKAWED AGLKYKGHTD 150
    ALRDFFKKNA IMMLGCKELF VGLFSEHIPL AKVSKKITFK NLSIFLKDFY 200
    KETHFKKMGL LGFNPHAGDY GVIGGEEEKI MEKAIAFVNA FLHSKKDEKF 250
    FKKALKDENL QKELLLNFKG KGVYLPYPLV ADTAFTKTGL KNCNRLVAMY 300
    HDLALAPLKA LYFDKSINVS LNLPIIRVSV DHGTAFDKAY KNAKINTKSY 350
    FEAAKFAINL HSKA 364
    Length:364
    Mass (Da):41,387
    Last modified:October 1, 2000 - v1
    Checksum:iDDD26465821FFC3E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL111168 Genomic DNA. Translation: CAL35354.1.
    PIRiA81331.
    RefSeqiYP_002344630.1. NC_002163.1.

    Genome annotation databases

    EnsemblBacteriaiCAL35354; CAL35354; Cj1239.
    GeneIDi905530.
    KEGGicje:Cj1239.
    PATRICi20059438. VBICamJej33762_1221.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL111168 Genomic DNA. Translation: CAL35354.1 .
    PIRi A81331.
    RefSeqi YP_002344630.1. NC_002163.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3TSN X-ray 2.63 A/B/C/D 1-364 [» ]
    ProteinModelPortali Q9PN58.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9PN58. 2 interactions.
    STRINGi 192222.Cj1239.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL35354 ; CAL35354 ; Cj1239 .
    GeneIDi 905530.
    KEGGi cje:Cj1239.
    PATRICi 20059438. VBICamJej33762_1221.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00244 ; UER00312 .
    BioCyci CJEJ192222:GJTS-1211-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: NCTC 11168.

    Entry informationi

    Entry nameiPDXA_CAMJE
    AccessioniPrimary (citable) accession number: Q9PN58
    Secondary accession number(s): Q0P917
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 86 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3