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Q9I5U4

- PDXA1_PSEAE

UniProt

Q9I5U4 - PDXA1_PSEAE

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase 1

Gene

pdxA1

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - 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 Zn(2+), Mg(2+) or Co(2+).1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei135 – 1351SubstrateBy similarity
Binding sitei136 – 1361SubstrateBy similarity
Metal bindingi165 – 1651Divalent metal cation; shared with dimeric partner
Metal bindingi210 – 2101Divalent metal cation; shared with dimeric partner
Metal bindingi265 – 2651Divalent metal cation; shared with dimeric partner
Binding sitei273 – 2731SubstrateBy similarity
Binding sitei282 – 2821SubstrateBy similarity
Binding sitei291 – 2911SubstrateBy similarity

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 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 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA0593.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3283284-hydroxythreonine-4-phosphate dehydrogenase 1PRO_0000188815Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA0593.

Structurei

Secondary structure

1
328
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Helixi16 – 238Combined sources
Beta strandi32 – 365Combined sources
Helixi38 – 4811Combined sources
Beta strandi53 – 564Combined sources
Beta strandi71 – 766Combined sources
Helixi90 – 923Combined sources
Helixi93 – 10816Combined sources
Beta strandi113 – 1175Combined sources
Helixi122 – 1276Combined sources
Helixi135 – 1428Combined sources
Beta strandi149 – 1546Combined sources
Beta strandi157 – 1637Combined sources
Helixi168 – 1703Combined sources
Helixi171 – 1744Combined sources
Helixi177 – 19317Combined sources
Beta strandi201 – 2055Combined sources
Helixi209 – 2124Combined sources
Turni213 – 2175Combined sources
Helixi220 – 2234Combined sources
Helixi225 – 2339Combined sources
Turni234 – 2363Combined sources
Beta strandi238 – 2436Combined sources
Helixi245 – 2484Combined sources
Helixi251 – 2544Combined sources
Beta strandi258 – 2647Combined sources
Helixi265 – 27612Combined sources
Beta strandi281 – 2899Combined sources
Beta strandi291 – 2944Combined sources
Helixi300 – 3023Combined sources
Turni303 – 3053Combined sources
Helixi311 – 32616Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9I5U4.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.Curated

Phylogenomic databases

eggNOGiCOG1995.
InParanoidiQ9I5U4.
KOiK00097.
OMAiWPERPAK.
OrthoDBiEOG6GN6ZC.
PhylomeDBiQ9I5U4.

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]
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.

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 .
PIRi A83572.
RefSeqi NP_249284.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YXO X-ray 2.01 A/B 1-328 [» ]
ProteinModelPortali Q9I5U4.
SMRi Q9I5U4. Positions 1-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA0593.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG03982 ; AAG03982 ; PA0593 .
GeneIDi 880733.
KEGGi pae:PA0593.
PATRICi 19835458. VBIPseAer58763_0629.

Organism-specific databases

PseudoCAPi PA0593.

Phylogenomic databases

eggNOGi COG1995.
InParanoidi Q9I5U4.
KOi K00097.
OMAi WPERPAK.
OrthoDBi EOG6GN6ZC.
PhylomeDBi Q9I5U4.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .

Miscellaneous databases

EvolutionaryTracei Q9I5U4.

Family and domain databases

Gene3Di 3.40.718.10. 1 hit.
HAMAPi MF_00536. PdxA.
InterProi IPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view ]
Pfami PF04166. PdxA. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00557. pdxA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. "Crystal structure of pyridoxal phosphate biosynthetic protein pdxA PA0593."
    Midwest center for structural genomics (MCSG)
    Submitted (APR-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, COFACTOR, SUBUNIT.

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 26, 2014
This is version 92 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

External Data

Dasty 3