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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Zn2+UniRule annotation, Mg2+UniRule annotation, Co2+UniRule annotationNote: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co2+.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361SubstrateUniRule annotation
Binding sitei137 – 1371SubstrateUniRule annotation
Metal bindingi173 – 1731Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi218 – 2181Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi273 – 2731Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei281 – 2811SubstrateUniRule annotation
Binding sitei290 – 2901SubstrateUniRule annotation
Binding sitei299 – 2991SubstrateUniRule 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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

Cobalt, Magnesium, Metal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

BioCyciRSOL267608:GCVU-519-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:RSc0517
ORF Names:RS04975
OrganismiRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
Taxonomic identifieri267608 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia
ProteomesiUP000001436: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3383384-hydroxythreonine-4-phosphate dehydrogenasePRO_0000188819Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi267608.RSc0517.

Structurei

3D structure databases

ProteinModelPortaliP58714.
SMRiP58714. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiRAGQGCL.
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.

P58714-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNIAITTGE PAGIGPDITV TALLRLLRQP APRHADVRWH VIGDAALLQA
60 70 80 90 100
RADAIGLGDA WRDAAAALTV VARPLGAPVR TGVLDAANGR YVLDLLDAAI
110 120 130 140 150
DGCLPDAAGM ARYDAMVTAP VQKSTINDAG VPFTGHTEYL AERSRTPRVV
160 170 180 190 200
MMLAGPQPAH GNAMLRVALA TTHLPLREVP DAITPAVLDE TLDIVQRDLR
210 220 230 240 250
ARFGMAAPRI LVTGLNPHAG EAGHLGREEI EVIEPAVVRA RARGIDARGP
260 270 280 290 300
YPADTLFQPR LLADADCVLA MYHDQGLAPL KYGTFGHGVN ITLGLPFVRT
310 320 330
SVDHGTALDL AGTGRAEAGS LLEAIDTAVE MARHAAHS
Length:338
Mass (Da):35,592
Last modified:January 31, 2002 - v1
Checksum:iCEC913DD30D77B3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL646052 Genomic DNA. Translation: CAD14045.1.
RefSeqiNP_518638.1. NC_003295.1.
WP_011000476.1. NC_003295.1.

Genome annotation databases

EnsemblBacteriaiCAD14045; CAD14045; RSc0517.
GeneIDi1219321.
KEGGirso:RSc0517.
PATRICi20259611. VBIRalSol70888_0539.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL646052 Genomic DNA. Translation: CAD14045.1.
RefSeqiNP_518638.1. NC_003295.1.
WP_011000476.1. NC_003295.1.

3D structure databases

ProteinModelPortaliP58714.
SMRiP58714. Positions 2-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi267608.RSc0517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD14045; CAD14045; RSc0517.
GeneIDi1219321.
KEGGirso:RSc0517.
PATRICi20259611. VBIRalSol70888_0539.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiRAGQGCL.
OrthoDBiEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.
BioCyciRSOL267608:GCVU-519-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GMI1000.

Entry informationi

Entry nameiPDXA_RALSO
AccessioniPrimary (citable) accession number: P58714
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: February 4, 2015
This is version 85 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.