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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Shigella boydii serotype 4 (strain Sb227)
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. D-erythrose-4-phosphate dehydrogenase (epd)
  2. Erythronate-4-phosphate dehydrogenase (pdxB)
  3. Phosphoserine aminotransferase (serC)
  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 sitei136SubstrateUniRule annotation1
Binding sitei137SubstrateUniRule annotation1
Metal bindingi166Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi211Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi266Divalent metal cation; shared with dimeric partnerUniRule annotation1
Binding sitei274SubstrateUniRule annotation1
Binding sitei283SubstrateUniRule annotation1
Binding sitei292SubstrateUniRule 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:SBO_0041
OrganismiShigella boydii serotype 4 (strain Sb227)
Taxonomic identifieri300268 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000007067 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000515141 – 3294-hydroxythreonine-4-phosphate dehydrogenaseAdd BLAST329

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ326I1
SMRiQ326I1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000221592
KOiK00097
OMAiAPVHKGV

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.

Q326I1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLTDRAAML
60 70 80 90 100
GLPLTLRPYS PNSPAQPQTA GTLTLLPVAL RESVTAGQLA IENGHYVVET
110 120 130 140 150
LARACDGCLN GEFAALITGP VHKGVINDAG IPFTGHTEFF EERSQAKKVV
160 170 180 190 200
MMLATEELRV ALATTHLPLR DIADAITPAL LHEVIAILHH DLRTKFGIAE
210 220 230 240 250
PRILVCGLNP HAGEGGHMGT EEIDTIIPVL DELRAQGMIL NGPLPADTLF
260 270 280 290 300
QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA
310 320
LELAGRGEAD VGSFITALNL AIKMIVNTQ
Length:329
Mass (Da):35,164
Last modified:December 6, 2005 - v1
Checksum:i82E2A51DABBFC3E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000036 Genomic DNA Translation: ABB64777.1

Genome annotation databases

EnsemblBacteriaiABB64777; ABB64777; SBO_0041
KEGGisbo:SBO_0041

Similar proteinsi

Entry informationi

Entry nameiPDXA_SHIBS
AccessioniPrimary (citable) accession number: Q326I1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: March 28, 2018
This is version 79 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
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Main funding by: National Institutes of Health