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Protein

4-hydroxythreonine-4-phosphate dehydrogenase 1

Gene

pdxA1

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+1 Publication, Mg2+1 Publication, Co2+1 PublicationNote: Binds 1 divalent metal cation per subunit. Can probably use ions such as Zn2+, Mg2+ or Co2+.1 Publication

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 sitei136SubstrateBy similarity1
Binding sitei137SubstrateBy similarity1
Metal bindingi166Divalent metal cation; shared with dimeric partner1
Metal bindingi211Divalent metal cation; shared with dimeric partner1
Metal bindingi266Divalent metal cation; shared with dimeric partner1
Binding sitei274SubstrateBy similarity1
Binding sitei283SubstrateBy similarity1
Binding sitei292SubstrateBy 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 1 (EC:1.1.1.262)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase 1
Gene namesi
Name:pdxA1
Synonyms:pdxA
Ordered Locus Names:STM0091
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_00001888261 – 3294-hydroxythreonine-4-phosphate dehydrogenase 1Add BLAST329

Proteomic databases

PaxDbiP58717.
PRIDEiP58717.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM0091.

Structurei

Secondary structure

1329
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Helixi18 – 25Combined sources8
Beta strandi31 – 38Combined sources8
Helixi40 – 49Combined sources10
Beta strandi55 – 58Combined sources4
Beta strandi72 – 77Combined sources6
Helixi91 – 93Combined sources3
Helixi94 – 109Combined sources16
Beta strandi114 – 118Combined sources5
Helixi123 – 127Combined sources5
Turni128 – 130Combined sources3
Helixi136 – 143Combined sources8
Beta strandi150 – 154Combined sources5
Beta strandi159 – 164Combined sources6
Helixi169 – 171Combined sources3
Helixi172 – 175Combined sources4
Helixi178 – 194Combined sources17
Beta strandi202 – 206Combined sources5
Helixi210 – 216Combined sources7
Helixi221 – 224Combined sources4
Helixi226 – 234Combined sources9
Turni235 – 237Combined sources3
Beta strandi239 – 244Combined sources6
Helixi246 – 249Combined sources4
Helixi252 – 255Combined sources4
Beta strandi259 – 265Combined sources7
Helixi266 – 277Combined sources12
Beta strandi282 – 290Combined sources9
Beta strandi292 – 294Combined sources3
Turni301 – 306Combined sources6
Helixi312 – 327Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R8KX-ray2.10A/B1-329[»]
ProteinModelPortaliP58717.
SMRiP58717.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58717.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.Curated

Phylogenomic databases

eggNOGiENOG4105CEZ. Bacteria.
COG1995. LUCA.
HOGENOMiHOG000221592.
KOiK00097.
OMAiYVWDTPL.
PhylomeDBiP58717.

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.

P58717-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAQRVVIT PGEPAGSGPD LVVQLAQRAW PIELVVCADG ALLTERAAML
60 70 80 90 100
GLPLSLLPYS PDVPAAPQPA GTLTLLPVSL RAPAISGQLT VENGPYVVET
110 120 130 140 150
LARACDGCLN GEFAALITGP VHKGVINDAG ISFTGHTEFF EERSQAKKVV
160 170 180 190 200
MMLATEELRV ALATTHLPLR AIADAITPAL LHEVIAILHH DLRTKFGIAE
210 220 230 240 250
PRILVCGLNP HAGEGGHMGT EEIDTIIPVL DELRAQGMKL NGPLPADTLF
260 270 280 290 300
QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA
310 320
LELAGRGKAD VGSFITALNL AIKMIVNTQ
Length:329
Mass (Da):34,779
Last modified:January 31, 2002 - v1
Checksum:i054D9F4E0F34E43B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL19055.1.
RefSeqiNP_459096.1. NC_003197.1.
WP_000093016.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19055; AAL19055; STM0091.
GeneIDi1251609.
KEGGistm:STM0091.
PATRICi32378449. VBISalEnt20916_0094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL19055.1.
RefSeqiNP_459096.1. NC_003197.1.
WP_000093016.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R8KX-ray2.10A/B1-329[»]
ProteinModelPortaliP58717.
SMRiP58717.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM0091.

Proteomic databases

PaxDbiP58717.
PRIDEiP58717.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL19055; AAL19055; STM0091.
GeneIDi1251609.
KEGGistm:STM0091.
PATRICi32378449. VBISalEnt20916_0094.

Phylogenomic databases

eggNOGiENOG4105CEZ. Bacteria.
COG1995. LUCA.
HOGENOMiHOG000221592.
KOiK00097.
OMAiYVWDTPL.
PhylomeDBiP58717.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.

Miscellaneous databases

EvolutionaryTraceiP58717.

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 nameiPDXA1_SALTY
AccessioniPrimary (citable) accession number: P58717
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: November 2, 2016
This is version 103 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.