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Protein

4-hydroxythreonine-4-phosphate dehydrogenase 2

Gene

pdxA2

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
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 Zn(2+), Mg(2+) or Co2+.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi173 – 1731Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi217 – 2171Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi274 – 2741Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei282 – 2821SubstrateUniRule annotation

GO - Molecular functioni

  1. 4-hydroxythreonine-4-phosphate dehydrogenase activity Source: UniProtKB-HAMAP
  2. cobalt ion binding Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP
  4. NAD binding Source: InterPro
  5. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. pyridoxal phosphate biosynthetic process Source: UniProtKB-HAMAP
  2. pyridoxine biosynthetic process Source: UniProtKB-HAMAP
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 2UniRule annotation (EC:1.1.1.262UniRule annotation)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase 2UniRule annotation
Gene namesi
Name:pdxA2UniRule annotation
Ordered Locus Names:PA2212
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA2212.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3373374-hydroxythreonine-4-phosphate dehydrogenase 2PRO_0000188816Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi208964.PA2212.

Structurei

3D structure databases

ProteinModelPortaliQ9I1Q5.
SMRiQ9I1Q5. Positions 6-331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221593.
InParanoidiQ9I1Q5.
KOiK00097.
OMAiCGREEID.
OrthoDBiEOG6GN6ZC.
PhylomeDBiQ9I1Q5.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9I1Q5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAPSLPRLA MVLGDPAGIG PELIARLLAD TEVREKAHIV LIADEAEMRR
60 70 80 90 100
GMRIAGCEFP YRRIDALETL DFADATPLLH PWLSQGGDEF PRSEASAVGG
110 120 130 140 150
RYSLETLALA LELTRSGRTD AILFGPLNKT SLHMAGMDHS DELHWFAERL
160 170 180 190 200
GFGGPFCEFN VLDDLWTSRV TSHVALAEVP GLLSQERVGE AIRLIDDALR
210 220 230 240 250
RSGLARPRIG VCGLNPHNGD NGSFGREELD IIAPAVQKAR EQGIAADGPY
260 270 280 290 300
PADTIFLKVQ GDARAFDAVV TMYHDQGQIA IKLMGFSRGV TVQGGLPIPI
310 320 330
ATPAHGTAFD IAGQGRADVG ATRQAFEIAC RMGRHKA
Length:337
Mass (Da):36,321
Last modified:March 1, 2001 - v1
Checksum:i7F53FD3707265B13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG05600.1.
PIRiC83370.
RefSeqiNP_250902.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG05600; AAG05600; PA2212.
GeneIDi881915.
KEGGipae:PA2212.
PATRICi19838872. VBIPseAer58763_2316.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG05600.1.
PIRiC83370.
RefSeqiNP_250902.1. NC_002516.2.

3D structure databases

ProteinModelPortaliQ9I1Q5.
SMRiQ9I1Q5. Positions 6-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA2212.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG05600; AAG05600; PA2212.
GeneIDi881915.
KEGGipae:PA2212.
PATRICi19838872. VBIPseAer58763_2316.

Organism-specific databases

PseudoCAPiPA2212.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221593.
InParanoidiQ9I1Q5.
KOiK00097.
OMAiCGREEID.
OrthoDBiEOG6GN6ZC.
PhylomeDBiQ9I1Q5.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.

Family and domain databases

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

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiPDXA2_PSEAE
AccessioniPrimary (citable) accession number: Q9I1Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 88 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.