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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Yersinia pseudotuberculosis serotype O:3 (strain YPIII)
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 Zn2+, Mg2+ or Co2+.UniRule annotation

Pathwayi: pyridoxine 5'-phosphate biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. D-erythrose-4-phosphate dehydrogenase (epd)
  2. Erythronate-4-phosphate dehydrogenase (pdxB)
  3. Phosphoserine aminotransferase (serC)
  4. 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
  5. Pyridoxine 5'-phosphate synthase (pdxJ)
This subpathway is part of the pathway pyridoxine 5'-phosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate, the pathway pyridoxine 5'-phosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei137SubstrateUniRule annotation1
Binding sitei138SubstrateUniRule annotation1
Metal bindingi167Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi212Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi267Divalent metal cation; shared with dimeric partnerUniRule annotation1
Binding sitei275SubstrateUniRule annotation1
Binding sitei284SubstrateUniRule annotation1
Binding sitei293SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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

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:YPK_3572
OrganismiYersinia pseudotuberculosis serotype O:3 (strain YPIII)
Taxonomic identifieri502800 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia
Proteomesi
  • UP000000721 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001282701 – 3314-hydroxythreonine-4-phosphate dehydrogenaseAdd BLAST331

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB1JKY2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000221592.
KOiK00097.
OMAiARNGPYV.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
HAMAPiMF_00536. PdxA. 1 hit.
InterProiIPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view]
PfamiPF04166. PdxA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00557. pdxA. 1 hit.

Sequencei

Sequence statusi: Complete.

B1JKY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHNHNNRLVI TPGEPAGVGP DLAIALAQQD WPVELVVCAD PALLLARASQ
60 70 80 90 100
LNLPLQLREY QADQPAIAQQ AGSLTILPVK TAVNVVPGKL DVGNSHYVVE
110 120 130 140 150
TLAKACDGAI SGEFAALVTG PVQKSIINDA GIPFIGHTEF FADRSHCQRV
160 170 180 190 200
VMMLATEELR VALATTHLPL LAVPGAITQA SLHEVITILD NDLKTKFGIT
210 220 230 240 250
QPQIYVCGLN PHAGEGGHMG HEEIDTIIPA LNTLRQQGIN LIGPLPADTL
260 270 280 290 300
FQPKYLQHAD AVLAMYHDQG LPVLKYQGFG RAVNITLGLP FIRTSVDHGT
310 320 330
ALELAATGTA DVGSFITALN LAIKMINNSN E
Length:331
Mass (Da):35,240
Last modified:April 29, 2008 - v1
Checksum:i9E7F0A5C87D0909C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000950 Genomic DNA. Translation: ACA69839.1.
RefSeqiWP_011191711.1. NZ_CP009792.1.

Genome annotation databases

EnsemblBacteriaiACA69839; ACA69839; YPK_3572.
KEGGiypy:YPK_3572.
PATRICi18664825. VBIYerPse127545_3865.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000950 Genomic DNA. Translation: ACA69839.1.
RefSeqiWP_011191711.1. NZ_CP009792.1.

3D structure databases

ProteinModelPortaliB1JKY2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA69839; ACA69839; YPK_3572.
KEGGiypy:YPK_3572.
PATRICi18664825. VBIYerPse127545_3865.

Phylogenomic databases

HOGENOMiHOG000221592.
KOiK00097.
OMAiARNGPYV.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
HAMAPiMF_00536. PdxA. 1 hit.
InterProiIPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view]
PfamiPF04166. PdxA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00557. pdxA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPDXA_YERPY
AccessioniPrimary (citable) accession number: B1JKY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: November 2, 2016
This is version 66 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

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 one 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.