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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Sodalis glossinidius (strain morsitans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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

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 Zn(2+), Mg(2+) or Co2+.UniRule annotation

Pathway:ipyridoxine 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. 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361SubstrateUniRule annotation
Binding sitei137 – 1371SubstrateUniRule annotation
Metal bindingi166 – 1661Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi211 – 2111Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi266 – 2661Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei274 – 2741SubstrateUniRule annotation
Binding sitei283 – 2831SubstrateUniRule annotation
Binding sitei292 – 2921SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

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

BioCyciSGLO343509:GJJC-450-MONOMER.
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:SG0425
OrganismiSodalis glossinidius (strain morsitans)
Taxonomic identifieri343509 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSodalis
ProteomesiUP000001932 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3303304-hydroxythreonine-4-phosphate dehydrogenasePRO_1000061034Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi343509.SG0425.

Structurei

3D structure databases

ProteinModelPortaliQ2NVX5.
SMRiQ2NVX5. Positions 1-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
KOiK00097.
OMAiDTLFQDK.
OrthoDBiEOG6GN6ZC.

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.

Q2NVX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSNQRIVIT PGEPAGIGPD LVAALAQQAW PVELVICADP ALLTARAQQL
60 70 80 90 100
GLPLRLHSYR PEQPATPRPA GELTVLAIDT PAPVAAGELN VANSHYVVET
110 120 130 140 150
LARACDSCLN GEFAALLTGP VHKGVINDGG LPFSGHTEYF AQRSGRERVV
160 170 180 190 200
MMLATESLRV ALATTHLPLL AVPGAVTRQS LDEVITILVH DLQQQFGIAQ
210 220 230 240 250
PCIYVCGLNP HAGEGGHMGR EEIEVITPAL DTLRAKGYNL VGPLPADTLF
260 270 280 290 300
QPKYLQQADA VLAMYHDQGL PVLKYQGFGR AVNITLGLPF IRTSVDHGTA
310 320 330
LELAGSGQAE AGSIKTALNI AIDMIKHRNE
Length:330
Mass (Da):35,035
Last modified:February 7, 2006 - v1
Checksum:i940A4955DB83CDF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008232 Genomic DNA. Translation: BAE73700.1.
RefSeqiWP_011410288.1. NC_007712.1.

Genome annotation databases

EnsemblBacteriaiBAE73700; BAE73700; SG0425.
KEGGisgl:SG0425.
PATRICi23647543. VBISodGlo61428_1095.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008232 Genomic DNA. Translation: BAE73700.1.
RefSeqiWP_011410288.1. NC_007712.1.

3D structure databases

ProteinModelPortaliQ2NVX5.
SMRiQ2NVX5. Positions 1-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi343509.SG0425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE73700; BAE73700; SG0425.
KEGGisgl:SG0425.
PATRICi23647543. VBISodGlo61428_1095.

Phylogenomic databases

eggNOGiCOG1995.
KOiK00097.
OMAiDTLFQDK.
OrthoDBiEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.
BioCyciSGLO343509:GJJC-450-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. "Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."
    Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S.
    Genome Res. 16:149-156(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: morsitans.

Entry informationi

Entry nameiPDXA_SODGM
AccessioniPrimary (citable) accession number: Q2NVX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 7, 2006
Last modified: July 22, 2015
This is version 69 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.UniRule annotation

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.