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)

Q2JSC8

- PDXA_SYNJA

UniProt

Q2JSC8 - PDXA_SYNJA

Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (07 Mar 2006)
      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.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei135 – 1351SubstrateUniRule annotation
    Metal bindingi170 – 1701Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi215 – 2151Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi276 – 2761Divalent metal cation; shared with dimeric partnerUniRule annotation
    Binding sitei284 – 2841SubstrateUniRule annotation
    Binding sitei293 – 2931SubstrateUniRule annotation
    Binding sitei302 – 3021SubstrateUniRule 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

    BioCyciSSP321327:GHFX-2317-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:CYA_2324
    OrganismiSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime)
    Taxonomic identifieri321327 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000008818: 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 – 3493494-hydroxythreonine-4-phosphate dehydrogenasePRO_1000051521Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi321327.CYA_2324.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2JSC8.
    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]
    TIGRFAMsiTIGR00557. pdxA. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q2JSC8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLLLPKLAL TLGDPAGIGP EIVLKALADP QVQACAQITV VGERQVLEAT    50
    YCLLRQRGAT DLADPAGIPV LEGGSGFYLE PSRVGRGDVA SGAASFAYLK 100
    TAIEEALRGQ FQGIVTAPIA KYLWHQAGYP FPGQTEVLAQ LSGSERYGML 150
    FVARSPHSGW QIRVLLATTH IPLSQVPLTL TPELVRAKLD LLVGSLRKLF 200
    GIVNPVIAVA GLNPHAGEQG QLGQEEKTWL AELLRTYPHA KIWGPLPPDT 250
    MWLAPAQAWY GQGAPAVADA YLALYHDQGL IPVKLLAFDR AVNLTLGLPF 300
    IRTSPDHGTA FDLAGQGVAR AESLKQAILL AAELALSSAA ASRSLQAQR 349
    Length:349
    Mass (Da):37,136
    Last modified:March 7, 2006 - v1
    Checksum:iEFC1717F80A0341E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000239 Genomic DNA. Translation: ABD00453.1.
    RefSeqiWP_011431126.1. NC_007775.1.
    YP_475716.1. NC_007775.1.

    Genome annotation databases

    EnsemblBacteriaiABD00453; ABD00453; CYA_2324.
    GeneIDi3897323.
    KEGGicya:CYA_2324.
    PATRICi23812908. VBISynSp90045_2281.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000239 Genomic DNA. Translation: ABD00453.1 .
    RefSeqi WP_011431126.1. NC_007775.1.
    YP_475716.1. NC_007775.1.

    3D structure databases

    ProteinModelPortali Q2JSC8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 321327.CYA_2324.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABD00453 ; ABD00453 ; CYA_2324 .
    GeneIDi 3897323.
    KEGGi cya:CYA_2324.
    PATRICi 23812908. VBISynSp90045_2281.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00244 ; UER00312 .
    BioCyci SSP321327:GHFX-2317-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. "Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
      Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
      ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JA-3-3Ab.

    Entry informationi

    Entry nameiPDXA_SYNJA
    AccessioniPrimary (citable) accession number: Q2JSC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 60 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