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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
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 sitei139SubstrateUniRule annotation1
Binding sitei140SubstrateUniRule annotation1
Metal bindingi173Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi218Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi273Divalent metal cation; shared with dimeric partnerUniRule annotation1
Binding sitei281SubstrateUniRule annotation1
Binding sitei290SubstrateUniRule annotation1
Binding sitei299SubstrateUniRule 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:RPA3065
OrganismiRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Taxonomic identifieri258594 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
Proteomesi
  • UP000001426 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000515111 – 3374-hydroxythreonine-4-phosphate dehydrogenaseAdd BLAST337

Proteomic databases

PRIDEiQ3V7R9

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi258594.RPA3065

Structurei

3D structure databases

ProteinModelPortaliQ3V7R9
SMRiQ3V7R9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEZ Bacteria
COG1995 LUCA
HOGENOMiHOG000221592
KOiK00097
OMAiAPVHKGV
OrthoDBiPOG091H03XD
PhylomeDBiQ3V7R9

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.

Q3V7R9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGMAKPLAL TLGEPAGIGP DIALAAWLKR EQHGLPPFYL LGDAGCLSRC
60 70 80 90 100
AKLLGLDVPL AEVKAEDAAA AFATTLPVVS TGQIATATPG QPDATSAPAA
110 120 130 140 150
IASIEHAVAD VRSGRAAAVV TNPIAKSVLY QAGFHHPGHT EFLAELAKRD
160 170 180 190 200
GIVPQPVMML WCPALAVVPV TIHVSLRDAI TQLTTDLIVS TARIVVKDLR
210 220 230 240 250
ERLGIAQPRL ALAGLNPHAG EDGALGQEDR AVVAPAVAIL RREGVDARGP
260 270 280 290 300
LPADTMFHAA ARKTYDCAIC MYHDQALIPI KTIAFDEGVN VTLGLPFIRT
310 320 330
SPDHGTAFDI AGSGQANPSS LIAALKLAAQ MASAKTA
Length:337
Mass (Da):34,927
Last modified:October 11, 2005 - v1
Checksum:i7C7AECA3938A5127
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX572602 Genomic DNA Translation: CAE28506.1
RefSeqiWP_011158611.1, NC_005296.1

Genome annotation databases

EnsemblBacteriaiCAE28506; CAE28506; RPA3065
KEGGirpa:RPA3065

Similar proteinsi

Entry informationi

Entry nameiPDXA_RHOPA
AccessioniPrimary (citable) accession number: Q3V7R9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 11, 2005
Last modified: May 23, 2018
This is version 80 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

Documents

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

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