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Protein

4-hydroxythreonine-4-phosphate dehydrogenase 2

Gene

pdxA2

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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).By similarity

Catalytic activityi

4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH.

Cofactori

Zn2+By similarity, Mg2+By similarity, Co2+By similarityNote: Binds 1 divalent metal cation per subunit. Can use ions such as Zn2+, Mg2+ or Co2+.By similarity

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.
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 1 (pdxA1), 4-hydroxythreonine-4-phosphate dehydrogenase 2 (pdxA2)
  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 sitei139SubstrateBy similarity1
Binding sitei140SubstrateBy similarity1
Metal bindingi169Divalent metal cation; shared with dimeric partnerBy similarity1
Metal bindingi213Divalent metal cation; shared with dimeric partnerBy similarity1
Metal bindingi268Divalent metal cation; shared with dimeric partnerBy similarity1
Binding sitei276SubstrateBy similarity1
Binding sitei285SubstrateBy similarity1
Binding sitei294SubstrateBy similarity1

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 dehydrogenase 2 (EC:1.1.1.262)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase 2
Gene namesi
Name:pdxA2
Ordered Locus Names:STM0163
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001888281 – 3274-hydroxythreonine-4-phosphate dehydrogenase 2Add BLAST327

Proteomic databases

PaxDbiP58718.
PRIDEiP58718.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM0163.

Structurei

Secondary structure

1327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 9Combined sources4
Turni13 – 16Combined sources4
Helixi17 – 25Combined sources9
Turni28 – 32Combined sources5
Beta strandi34 – 39Combined sources6
Helixi41 – 49Combined sources9
Beta strandi57 – 63Combined sources7
Helixi64 – 66Combined sources3
Beta strandi73 – 78Combined sources6
Helixi84 – 86Combined sources3
Helixi94 – 112Combined sources19
Beta strandi117 – 121Combined sources5
Helixi126 – 131Combined sources6
Helixi139 – 146Combined sources8
Beta strandi153 – 157Combined sources5
Beta strandi162 – 166Combined sources5
Helixi172 – 178Combined sources7
Helixi181 – 197Combined sources17
Beta strandi204 – 208Combined sources5
Helixi212 – 214Combined sources3
Helixi222 – 226Combined sources5
Helixi228 – 236Combined sources9
Turni237 – 239Combined sources3
Beta strandi241 – 246Combined sources6
Helixi248 – 256Combined sources9
Beta strandi261 – 267Combined sources7
Helixi268 – 277Combined sources10
Beta strandi283 – 288Combined sources6
Beta strandi290 – 298Combined sources9
Turni303 – 309Combined sources7
Helixi314 – 326Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HI1X-ray2.30A/B1-327[»]
ProteinModelPortaliP58718.
SMRiP58718.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58718.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.Curated

Phylogenomic databases

eggNOGiENOG4105CEZ. Bacteria.
COG1995. LUCA.
HOGENOMiHOG000221593.
KOiK00097.
OMAiMYPGHTE.
PhylomeDBiP58718.

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.

P58718-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METKTVAITM GDPAGIGPEI IVKALSEDGL NGAPLVVIGC LATLKRLQAK
60 70 80 90 100
GITPNVELRA IERVAEARFA PGIIHVIDEP LAQPEALEAG KVQAQAGDLA
110 120 130 140 150
YRCVKRATEL ALRGDVQAIA TAPLNKEALH LAGHNYPGHT ELLATLTHSR
160 170 180 190 200
DYAMVLYTDK LKVIHVSTHI ALRKFLDTLS TARVETVIGI ADTFLKRVGY
210 220 230 240 250
VKPRIAVAGV NPHAGENGLF GDEETRILTP AITDARAKGM DVYGPCPPDT
260 270 280 290 300
VFLQAYEGQY DMVVAMYHDQ GHIPLKLLGF YDGVNITAGL PFIRTSADHG
310 320
TAFDIAWTGK AKSESMAVSI KLAMQLA
Length:327
Mass (Da):35,065
Last modified:January 31, 2002 - v1
Checksum:i03BB6725F1896440
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL19127.1.
RefSeqiNP_459168.1. NC_003197.1.
WP_000448745.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19127; AAL19127; STM0163.
GeneIDi1251681.
KEGGistm:STM0163.
PATRICi32378607. VBISalEnt20916_0173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL19127.1.
RefSeqiNP_459168.1. NC_003197.1.
WP_000448745.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HI1X-ray2.30A/B1-327[»]
ProteinModelPortaliP58718.
SMRiP58718.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM0163.

Proteomic databases

PaxDbiP58718.
PRIDEiP58718.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL19127; AAL19127; STM0163.
GeneIDi1251681.
KEGGistm:STM0163.
PATRICi32378607. VBISalEnt20916_0173.

Phylogenomic databases

eggNOGiENOG4105CEZ. Bacteria.
COG1995. LUCA.
HOGENOMiHOG000221593.
KOiK00097.
OMAiMYPGHTE.
PhylomeDBiP58718.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.

Miscellaneous databases

EvolutionaryTraceiP58718.

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 nameiPDXA2_SALTY
AccessioniPrimary (citable) accession number: P58718
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: November 2, 2016
This is version 97 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.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.