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B1KVV5

- PDXA_CLOBM

UniProt

B1KVV5 - PDXA_CLOBM

Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Clostridium botulinum (strain Loch Maree / Type A3)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      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 sitei141 – 1411SubstrateUniRule annotation
    Binding sitei142 – 1421SubstrateUniRule annotation
    Metal bindingi171 – 1711Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi215 – 2151Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi270 – 2701Divalent metal cation; shared with dimeric partnerUniRule annotation
    Binding sitei278 – 2781SubstrateUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule 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

    BioCyciCBOT498214:GH05-2303-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:CLK_1647
    OrganismiClostridium botulinum (strain Loch Maree / Type A3)
    Taxonomic identifieri498214 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000000722: 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 – 3343344-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128238Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi498214.CLK_1647.

    Structurei

    3D structure databases

    ProteinModelPortaliB1KVV5.
    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]
    TIGRFAMsiTIGR00557. pdxA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    B1KVV5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MINNKPIIGI PIGDPAGVGP EIVVKSLTEA EVYEKCNPIL IGDAKVIKQA    50
    MGFCNVNLNI NSIKKADEGK FTLGTIDLID LNNIDIDELK IGKVQGIAGK 100
    AAFEYIKKSV EMAKEGELDA IATTPINKES LREGNVNYIG HTEILADLTD 150
    TEDPLTMFEV RGMRVFFLTR HVSLRKACDL VTKERVLDYI IRCSEALEKL 200
    GVKDGKMAVA GLNPHSGEHG LFGDEEMKAV VPAIEEAQKM GYKVEGPIGA 250
    DSVFHLALKG RYNSVLSLYH DQGHIATKTL DFERTIAVTN GMPILRTSVD 300
    HGTAFDIAGT GQASSVSMVE AIILAAKYSP KFKK 334
    Length:334
    Mass (Da):36,273
    Last modified:April 29, 2008 - v1
    Checksum:iD48D3A5B50A457F6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000962 Genomic DNA. Translation: ACA55182.1.
    RefSeqiYP_001787584.1. NC_010520.1.

    Genome annotation databases

    EnsemblBacteriaiACA55182; ACA55182; CLK_1647.
    GeneIDi6153953.
    KEGGicbl:CLK_1647.
    PATRICi19389898. VBICloBot822_2562.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000962 Genomic DNA. Translation: ACA55182.1 .
    RefSeqi YP_001787584.1. NC_010520.1.

    3D structure databases

    ProteinModelPortali B1KVV5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 498214.CLK_1647.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACA55182 ; ACA55182 ; CLK_1647 .
    GeneIDi 6153953.
    KEGGi cbl:CLK_1647.
    PATRICi 19389898. VBICloBot822_2562.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00244 ; UER00312 .
    BioCyci CBOT498214:GH05-2303-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. "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
      Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
      PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Loch Maree / Type A3.

    Entry informationi

    Entry nameiPDXA_CLOBM
    AccessioniPrimary (citable) accession number: B1KVV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 47 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

    Documents

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

    External Data

    Dasty 3