SubmitCancel

Skip Header

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

Q9I5U4

- PDXA1_PSEAE

UniProt

Q9I5U4 - PDXA1_PSEAE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
4-hydroxythreonine-4-phosphate dehydrogenase 1
Gene
pdxA1, PA0593
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.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 divalent metal cation per subunit. Can probably use ions such as zinc, magnesium or cobalt.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei135 – 1351Substrate By similarity
Binding sitei136 – 1361Substrate By 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 – 2731Substrate By similarity
Binding sitei282 – 2821Substrate By similarity
Binding sitei291 – 2911Substrate By similarity

GO - Molecular functioni

  1. 4-hydroxythreonine-4-phosphate dehydrogenase activity Source: UniProtKB-HAMAP
  2. NAD binding Source: InterPro
  3. cobalt ion binding Source: UniProtKB-HAMAP
  4. magnesium ion binding Source: UniProtKB-HAMAP
  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 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 – 3283284-hydroxythreonine-4-phosphate dehydrogenase 1UniRule annotation
PRO_0000188815Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA0593.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YXOX-ray2.01A/B1-328[»]
ProteinModelPortaliQ9I5U4.
SMRiQ9I5U4. Positions 1-328.

Miscellaneous databases

EvolutionaryTraceiQ9I5U4.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
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

MSLRFALTPG EPAGIGPDLC LLLARSAQPH PLIAIASRTL LQERAGQLGL    50
AIDLKDVSPA AWPERPAKAG QLYVWDTPLA APVRPGQLDR ANAAYVLETL 100
TRAGQGCLDG HFAGMITAPV HKGVINEAGI PFSGHTEFLA DLTHTAQVVM 150
MLATRGLRVA LATTHLPLRE VADAISDERL TRVARILHAD LRDKFGIAHP 200
RILVCGLNPH AGEGGHLGRE EIEVIEPCLE RLRGEGLDLI GPLPADTLFT 250
PKHLEHCDAV LAMYHDQGLP VLKYKGFGAA VNVTLGLPII RTSVDHGTAL 300
DLAGSGRIDS GSLQVALETA YQMAASRC 328
Length:328
Mass (Da):34,923
Last modified:March 1, 2001 - v1
Checksum:i2C666738F21D7B8C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG03982.1 .
PIRi A83572.
RefSeqi NP_249284.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
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: July 9, 2014
This is version 89 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

Similar proteinsi