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Q9RC88

- PDXA_BACHD

UniProt

Q9RC88 - PDXA_BACHD

Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 May 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.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei140 – 1401SubstrateUniRule annotation
    Binding sitei141 – 1411SubstrateUniRule annotation
    Metal bindingi170 – 1701Divalent 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 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

    BioCyciBHAL272558:GJC5-862-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:BH0804
    OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
    Taxonomic identifieri272558 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001258: 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_0000188797Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272558.BH0804.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9RC88.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PdxA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1995.
    HOGENOMiHOG000040097.
    KOiK00097.
    OMAiAIPMGDP.
    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.

    Q9RC88-1 [UniParc]FASTAAdd to Basket

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    MNKKPIIAIP MGDPAGIGPE ITVGALNKKE LYDVANPVVI GHGDMLEKML    50
    PVMKADLTIN RITTVDEAMF EYGTIDVIHL DNLNVAEVKM GTVQAQCGKA 100
    AFEYIRHAVQ LANDKKVDAL ATTPINKESL KAAEVPYIGH TEMLADLTKT 150
    EDPLTMFEVH SMRIFFLTRH LSLKDAIDQM TKERVHDYLL RCDKALEKLG 200
    VKERRFAVAG LNPHSGENGL FGREEMDEIT PGIELAKKDG INAVGPVPAD 250
    SVFHHALNGR YDAVLSLYHD QGHIAAKMTD FERTISITNG LPFLRTSVDH 300
    GTAFDIAGKG IASTVSMEEC IKLAAKYAPH FVTA 334
    Length:334
    Mass (Da):36,632
    Last modified:May 1, 2000 - v1
    Checksum:i24436A1866079820
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024550 Genomic DNA. Translation: BAA83911.1.
    BA000004 Genomic DNA. Translation: BAB04523.1.
    PIRiD83750.
    RefSeqiNP_241670.1. NC_002570.2.
    WP_010896977.1. NC_002570.2.

    Genome annotation databases

    EnsemblBacteriaiBAB04523; BAB04523; BAB04523.
    GeneIDi892178.
    KEGGibha:BH0804.
    PATRICi18938608. VBIBacHal18977_0842.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024550 Genomic DNA. Translation: BAA83911.1 .
    BA000004 Genomic DNA. Translation: BAB04523.1 .
    PIRi D83750.
    RefSeqi NP_241670.1. NC_002570.2.
    WP_010896977.1. NC_002570.2.

    3D structure databases

    ProteinModelPortali Q9RC88.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272558.BH0804.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB04523 ; BAB04523 ; BAB04523 .
    GeneIDi 892178.
    KEGGi bha:BH0804.
    PATRICi 18938608. VBIBacHal18977_0842.

    Phylogenomic databases

    eggNOGi COG1995.
    HOGENOMi HOG000040097.
    KOi K00097.
    OMAi AIPMGDP.
    OrthoDBi EOG6GN6ZC.

    Enzyme and pathway databases

    UniPathwayi UPA00244 ; UER00312 .
    BioCyci BHAL272558:GJC5-862-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. "Genetic analysis of the chromosome of alkaliphilic Bacillus halodurans C-125."
      Takami H., Takaki Y., Nakasone K., Sakiyama T., Maeno G., Sasaki R., Hirama C., Fuji F., Masui N.
      Extremophiles 3:227-233(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
    2. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
      Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
      Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

    Entry informationi

    Entry nameiPDXA_BACHD
    AccessioniPrimary (citable) accession number: Q9RC88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 88 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