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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Ruegeria sp. (strain TM1040) (Silicibacter sp.)
Status
Reviewed-Annotation score: -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

Miscellaneous

The active site is located at the dimer interface.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 Zn2+, Mg2+ or Co2+.UniRule annotation

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.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
  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 sitei132SubstrateUniRule annotation1
Binding sitei133SubstrateUniRule annotation1
Metal bindingi162Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi207Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi262Divalent metal cation; shared with dimeric partnerUniRule annotation1
Binding sitei270SubstrateUniRule annotation1
Binding sitei279SubstrateUniRule annotation1
Binding sitei288SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPyridoxine biosynthesis
LigandCobalt, Magnesium, Metal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotation (EC:1.1.1.262UniRule annotation)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenaseUniRule annotation
Gene namesi
Name:pdxAUniRule annotation
Ordered Locus Names:TM1040_0945
OrganismiRuegeria sp. (strain TM1040) (Silicibacter sp.)
Taxonomic identifieri292414 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria
Proteomesi
  • UP000000636 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000515191 – 3264-hydroxythreonine-4-phosphate dehydrogenaseAdd BLAST326

Proteomic databases

PRIDEiQ1GI38

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi292414.TM1040_0945

Structurei

3D structure databases

ProteinModelPortaliQ1GI38
SMRiQ1GI38
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEZ Bacteria
COG1995 LUCA
HOGENOMiHOG000221592
KOiK00097
OMAiAPVHKGV
OrthoDBiPOG091H03XD

Family and domain databases

HAMAPiMF_00536 PdxA, 1 hit
InterProiView protein in InterPro
IPR037510 PdxA
IPR005255 PdxA_fam
PANTHERiPTHR30004 PTHR30004, 1 hit
PfamiView protein in Pfam
PF04166 PdxA, 1 hit
TIGRFAMsiTIGR00557 pdxA, 1 hit

Sequencei

Sequence statusi: Complete.

Q1GI38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGAPQVIAL SCGEPAGIGP EIAVAAWDQL RADCPFVWIG DPRHLPSSHP
60 70 80 90 100
WQPVSAPAEA LQVSADALPV WPLEFAGNTT KGEADPQNAS GVIQSIKTGV
110 120 130 140 150
ELVTSGKAAA LCTAPIHKKA LIDGAGFAYP GHTEFLAALG GVDHVVMMLA
160 170 180 190 200
SAALRVVPAT IHIPLSAVPE VLTPDHLRRV ITLTDRGLRD QFGLTAPRIA
210 220 230 240 250
VTGLNPHAGE GGAMGQEEGD WIEALIREMQ TEGYRLTGPH PADTLFHAAA
260 270 280 290 300
RARYDAAIAM YHDQALIPIK TLDFDKGVNV TLGLPFIRTS PDHGTAFDIA
310 320
GKGLANPSSL IEALRLAQTM AKTRQP
Length:326
Mass (Da):34,339
Last modified:June 27, 2006 - v1
Checksum:i85584BAFB9B8E179
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000377 Genomic DNA Translation: ABF63678.1
RefSeqiWP_011538288.1, NC_008044.1

Genome annotation databases

EnsemblBacteriaiABF63678; ABF63678; TM1040_0945
KEGGisit:TM1040_0945

Similar proteinsi

Entry informationi

Entry nameiPDXA_RUEST
AccessioniPrimary (citable) accession number: Q1GI38
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 27, 2006
Last modified: May 23, 2018
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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