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)

Q89MT9

- PDXA2_BRADU

UniProt

Q89MT9 - PDXA2_BRADU

Protein

4-hydroxythreonine-4-phosphate dehydrogenase 2

Gene

pdxA2

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 sitei148 – 1481SubstrateUniRule annotation
    Binding sitei149 – 1491SubstrateUniRule annotation
    Metal bindingi182 – 1821Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi227 – 2271Divalent metal cation; shared with dimeric partnerUniRule annotation
    Metal bindingi282 – 2821Divalent metal cation; shared with dimeric partnerUniRule annotation
    Binding sitei290 – 2901SubstrateUniRule annotation
    Binding sitei299 – 2991SubstrateUniRule annotation
    Binding sitei308 – 3081SubstrateUniRule 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

    BioCyciBJAP224911:GJEJ-4129-MONOMER.
    UniPathwayiUPA00244; UER00312.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxythreonine-4-phosphate dehydrogenase 2UniRule annotation (EC:1.1.1.262UniRule annotation)
    Alternative name(s):
    4-(phosphohydroxy)-L-threonine dehydrogenase 2UniRule annotation
    Gene namesi
    Name:pdxA2UniRule annotation
    Ordered Locus Names:bll4103
    OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
    Taxonomic identifieri224911 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
    ProteomesiUP000002526: 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 – 3453454-hydroxythreonine-4-phosphate dehydrogenase 2PRO_0000188799Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi224911.bll4103.

    Structurei

    3D structure databases

    ProteinModelPortaliQ89MT9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PdxA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1995.
    HOGENOMiHOG000221592.
    KOiK00097.
    OrthoDBiEOG6GN6ZC.
    PhylomeDBiQ89MT9.

    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.

    Q89MT9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANHAAKPLA LTLGEPAGIG PDITIAGWLR RRELNLPAFY LLGDEALIAR    50
    RAKTLDKTLG KALGAEIRIA SVSAHEAAAA FTEALPVVAT GERATAEPGQ 100
    PDASSAPAAL ASIRQAVADV RAGRAGAVVT NPIAKSVLYR AGFRHPGHTE 150
    FLAELAAKDG RVPQPVMMLW SPRLAVVPVT IHVSLRDALS QLTSELIVST 200
    VRIVATELKS RFGIARPRIA VSGLNPHAGE DGSLGHEEQT IIAPALKTLR 250
    NDGIDARGPL PADTMFHEAA RSSYDCAVCM YHDQALIPIK TVAFDDAVNV 300
    TLGLPFIRTS PDHGTAFDIA GTGKANPASL IAALELASRM AAAKT 345
    Length:345
    Mass (Da):36,145
    Last modified:June 1, 2003 - v1
    Checksum:i2E6FCD4B37B3DDE4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000040 Genomic DNA. Translation: BAC49368.1.
    RefSeqiNP_770743.1. NC_004463.1.

    Genome annotation databases

    EnsemblBacteriaiBAC49368; BAC49368; BAC49368.
    GeneIDi1049759.
    KEGGibja:bll4103.
    PATRICi21191712. VBIBraJap65052_4112.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000040 Genomic DNA. Translation: BAC49368.1 .
    RefSeqi NP_770743.1. NC_004463.1.

    3D structure databases

    ProteinModelPortali Q89MT9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224911.bll4103.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC49368 ; BAC49368 ; BAC49368 .
    GeneIDi 1049759.
    KEGGi bja:bll4103.
    PATRICi 21191712. VBIBraJap65052_4112.

    Phylogenomic databases

    eggNOGi COG1995.
    HOGENOMi HOG000221592.
    KOi K00097.
    OrthoDBi EOG6GN6ZC.
    PhylomeDBi Q89MT9.

    Enzyme and pathway databases

    UniPathwayi UPA00244 ; UER00312 .
    BioCyci BJAP224911:GJEJ-4129-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: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

    Entry informationi

    Entry nameiPDXA2_BRADU
    AccessioniPrimary (citable) accession number: Q89MT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 80 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