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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Helicobacter pylori (strain Shi470)
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. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  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 sitei126SubstrateUniRule annotation1
Binding sitei127SubstrateUniRule annotation1
Metal bindingi156Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi195Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi251Divalent metal cation; shared with dimeric partnerUniRule annotation1
Binding sitei259SubstrateUniRule annotation1
Binding sitei268SubstrateUniRule annotation1
Binding sitei277SubstrateUniRule 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:HPSH_08240
OrganismiHelicobacter pylori (strain Shi470)
Taxonomic identifieri512562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

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_10001282531 – 3074-hydroxythreonine-4-phosphate dehydrogenaseAdd BLAST307

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB2UVZ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000221591.
KOiK00097.
OMAiCELADDK.

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.

B2UVZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKKIAISC GDIQGVGLEL ILKSHKEVSA LCEPLYLIDS ELLERANQLL
60 70 80 90 100
NNAYETKTLN TLAINAPLPL LNSGTIGKVS AQSGAYSFES FKKACELADD
110 120 130 140 150
KEVDGICTLP INKLAWQQAQ IPFVGHTDFL KQRYKDHQII MMLGCFRLFV
160 170 180 190 200
GLFSDHVPLG AVSQLIQVKA LVRFLLAFQK STQAKIIQVC GFNPHAGEEG
210 220 230 240 250
LFGKEDAKIL KAIQKSNQTL GFECFLGPLP ADSAFAPNKR KITPFYVSMS
260 270 280 290 300
HDVGLAPLKA LYFDESINVS LNAPILRAST DHGTAFDIAY QNKANNKSYV

NAIKYLA
Length:307
Mass (Da):33,697
Last modified:July 1, 2008 - v1
Checksum:i1EB9C7A27FB55C79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001072 Genomic DNA. Translation: ACD49031.1.
RefSeqiWP_001075034.1. NC_010698.2.

Genome annotation databases

EnsemblBacteriaiACD49031; ACD49031; HPSH_08240.
KEGGihps:HPSH_08240.
PATRICi20614629. VBIHelPyl23559_1600.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001072 Genomic DNA. Translation: ACD49031.1.
RefSeqiWP_001075034.1. NC_010698.2.

3D structure databases

ProteinModelPortaliB2UVZ9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACD49031; ACD49031; HPSH_08240.
KEGGihps:HPSH_08240.
PATRICi20614629. VBIHelPyl23559_1600.

Phylogenomic databases

HOGENOMiHOG000221591.
KOiK00097.
OMAiCELADDK.

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_HELPS
AccessioniPrimary (citable) accession number: B2UVZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: November 2, 2016
This is version 55 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

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.