Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

4-hydroxythreonine-4-phosphate dehydrogenase 1

Gene

pdxA1

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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 2 (pdxA2), 4-hydroxythreonine-4-phosphate dehydrogenase 1 (pdxA1)
  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 sitei135SubstrateBy similarity1
Binding sitei136SubstrateBy similarity1
Metal bindingi165Divalent metal cation; shared with dimeric partner1
Metal bindingi210Divalent metal cation; shared with dimeric partner1
Metal bindingi265Divalent metal cation; shared with dimeric partner1
Binding sitei273SubstrateBy similarity1
Binding sitei282SubstrateBy similarity1
Binding sitei291SubstrateBy 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
Ordered Locus Names:PA0593
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA0593.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001888151 – 3284-hydroxythreonine-4-phosphate dehydrogenase 1Add BLAST328

Proteomic databases

PaxDbiQ9I5U4.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA0593.

Structurei

Secondary structure

1328
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Helixi16 – 23Combined sources8
Beta strandi32 – 36Combined sources5
Helixi38 – 48Combined sources11
Beta strandi53 – 56Combined sources4
Beta strandi71 – 76Combined sources6
Helixi90 – 92Combined sources3
Helixi93 – 108Combined sources16
Beta strandi113 – 117Combined sources5
Helixi122 – 127Combined sources6
Helixi135 – 142Combined sources8
Beta strandi149 – 154Combined sources6
Beta strandi157 – 163Combined sources7
Helixi168 – 170Combined sources3
Helixi171 – 174Combined sources4
Helixi177 – 193Combined sources17
Beta strandi201 – 205Combined sources5
Helixi209 – 212Combined sources4
Turni213 – 217Combined sources5
Helixi220 – 223Combined sources4
Helixi225 – 233Combined sources9
Turni234 – 236Combined sources3
Beta strandi238 – 243Combined sources6
Helixi245 – 248Combined sources4
Helixi251 – 254Combined sources4
Beta strandi258 – 264Combined sources7
Helixi265 – 276Combined sources12
Beta strandi281 – 289Combined sources9
Beta strandi291 – 294Combined sources4
Helixi300 – 302Combined sources3
Turni303 – 305Combined sources3
Helixi311 – 326Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YXOX-ray2.01A/B1-328[»]
ProteinModelPortaliQ9I5U4.
SMRiQ9I5U4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I5U4.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.Curated

Phylogenomic databases

eggNOGiENOG4105CEZ. Bacteria.
COG1995. LUCA.
InParanoidiQ9I5U4.
KOiK00097.
OMAiYVWDTPL.
PhylomeDBiQ9I5U4.

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.

Q9I5U4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLRFALTPG EPAGIGPDLC LLLARSAQPH PLIAIASRTL LQERAGQLGL
60 70 80 90 100
AIDLKDVSPA AWPERPAKAG QLYVWDTPLA APVRPGQLDR ANAAYVLETL
110 120 130 140 150
TRAGQGCLDG HFAGMITAPV HKGVINEAGI PFSGHTEFLA DLTHTAQVVM
160 170 180 190 200
MLATRGLRVA LATTHLPLRE VADAISDERL TRVARILHAD LRDKFGIAHP
210 220 230 240 250
RILVCGLNPH AGEGGHLGRE EIEVIEPCLE RLRGEGLDLI GPLPADTLFT
260 270 280 290 300
PKHLEHCDAV LAMYHDQGLP VLKYKGFGAA VNVTLGLPII RTSVDHGTAL
310 320
DLAGSGRIDS GSLQVALETA YQMAASRC
Length:328
Mass (Da):34,923
Last modified:March 1, 2001 - v1
Checksum:i2C666738F21D7B8C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG03982.1.
PIRiA83572.
RefSeqiNP_249284.1. NC_002516.2.
WP_003109023.1. NZ_ASJY01000101.1.

Genome annotation databases

EnsemblBacteriaiAAG03982; AAG03982; PA0593.
GeneIDi880733.
KEGGipae:PA0593.
PATRICi19835458. VBIPseAer58763_0629.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG03982.1.
PIRiA83572.
RefSeqiNP_249284.1. NC_002516.2.
WP_003109023.1. NZ_ASJY01000101.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YXOX-ray2.01A/B1-328[»]
ProteinModelPortaliQ9I5U4.
SMRiQ9I5U4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA0593.

Proteomic databases

PaxDbiQ9I5U4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG03982; AAG03982; PA0593.
GeneIDi880733.
KEGGipae:PA0593.
PATRICi19835458. VBIPseAer58763_0629.

Organism-specific databases

PseudoCAPiPA0593.

Phylogenomic databases

eggNOGiENOG4105CEZ. Bacteria.
COG1995. LUCA.
InParanoidiQ9I5U4.
KOiK00097.
OMAiYVWDTPL.
PhylomeDBiQ9I5U4.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.

Miscellaneous databases

EvolutionaryTraceiQ9I5U4.

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_PSEAE
AccessioniPrimary (citable) accession number: Q9I5U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 99 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.