Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

C0QBU5

- PDXA_DESAH

UniProt

C0QBU5 - PDXA_DESAH

Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (05 May 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei141 – 1411SubstrateUniRule annotation
    Binding sitei142 – 1421SubstrateUniRule annotation
    Metal bindingi171 – 1711Divalent 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
    Binding sitei288 – 2881SubstrateUniRule annotation
    Binding sitei297 – 2971SubstrateUniRule 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

    BioCyciDAUT177437:GHLR-1854-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:HRM2_18550
    OrganismiDesulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
    Taxonomic identifieri177437 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfobacterium
    ProteomesiUP000000442: 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 – 3403404-hydroxythreonine-4-phosphate dehydrogenasePRO_1000211912Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi177437.HRM2_18550.

    Structurei

    3D structure databases

    ProteinModelPortaliC0QBU5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PdxA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1995.
    HOGENOMiHOG000221593.
    KOiK00097.
    OMAiSIDIRTI.
    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.

    C0QBU5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDNRPVIGI TMGDPVGIGP EIIVSALDDP FVYTVCRPLV LGDEGVMERA    50
    IDLKSARMDV HTTDTPAGGK YCHGTMDIVP LSRLDAATLL AGHPTPGTGK 100
    AMIDYITTGV DLAMDGKIQA IATCPITKTA MKLAGSKFHG HTELIADRTH 150
    TPRVAMMMAG DRLRVVLVTI HIPLCEVSAR LNQAEILATI SLTSETLKTK 200
    FGIPEPRIAV AGLNPHGGED GMFGSEELEI IAPAVEQARS KGITVSGPFP 250
    PDTLFFNAAN HKFDAVVCMY HDQGLIPFKM IHFSDGVNTT LGLPIIRTSV 300
    DHGTAYDIAW RGTADPSSLI AAIKMAALQA TITGANRINR 340
    Length:340
    Mass (Da):36,215
    Last modified:May 5, 2009 - v1
    Checksum:iD10C3F53007C3BA4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001087 Genomic DNA. Translation: ACN14957.1.
    RefSeqiYP_002603121.1. NC_012108.1.

    Genome annotation databases

    EnsemblBacteriaiACN14957; ACN14957; HRM2_18550.
    GeneIDi7500958.
    KEGGidat:HRM2_18550.
    PATRICi21683381. VBIDesAut25181_1961.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001087 Genomic DNA. Translation: ACN14957.1 .
    RefSeqi YP_002603121.1. NC_012108.1.

    3D structure databases

    ProteinModelPortali C0QBU5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 177437.HRM2_18550.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACN14957 ; ACN14957 ; HRM2_18550 .
    GeneIDi 7500958.
    KEGGi dat:HRM2_18550.
    PATRICi 21683381. VBIDesAut25181_1961.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00244 ; UER00312 .
    BioCyci DAUT177437:GHLR-1854-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: ATCC 43914 / DSM 3382 / HRM2.

    Entry informationi

    Entry nameiPDXA_DESAH
    AccessioniPrimary (citable) accession number: C0QBU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 42 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