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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
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).By similarity

Miscellaneous

The active site is located at the dimer interface.By similarity

Catalytic activityi

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

Cofactori

a divalent metal cationBy similarityNote: Binds 1 divalent metal cation per subunit.By similarity

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.By similarity
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. 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 sitei153SubstrateBy similarity1
Binding sitei154SubstrateBy similarity1
Metal bindingi189Divalent metal cation; shared with dimeric partnerBy similarity1
Metal bindingi238Divalent metal cation; shared with dimeric partnerBy similarity1
Metal bindingi294Divalent metal cation; shared with dimeric partnerBy similarity1
Binding sitei302SubstrateBy similarity1
Binding sitei311SubstrateBy similarity1
Binding sitei320SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPyridoxine biosynthesis
LigandMetal-binding, NAD, NADP

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenaseBy similarity (EC:1.1.1.262By similarity)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenaseBy similarity
Gene namesi
Name:pdxABy similarity
Ordered Locus Names:RB7885
OrganismiRhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Taxonomic identifieri243090 [NCBI]
Taxonomic lineageiBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula
Proteomesi
  • UP000001025 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001888241 – 3514-hydroxythreonine-4-phosphate dehydrogenaseAdd BLAST351

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi243090.RB7885.

Structurei

3D structure databases

ProteinModelPortaliQ7UMZ2.
SMRiQ7UMZ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.Curated

Phylogenomic databases

eggNOGiENOG4105CEZ. Bacteria.
COG1995. LUCA.
HOGENOMiHOG000221591.
InParanoidiQ7UMZ2.
KOiK00097.
OMAiVFMRARH.
OrthoDBiPOG091H03XD.

Family and domain databases

InterProiView protein in InterPro
IPR005255. PdxA.
PANTHERiPTHR30004. PTHR30004. 1 hit.
PfamiView protein in Pfam
PF04166. PdxA. 1 hit.
TIGRFAMsiTIGR00557. pdxA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7UMZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDANQTRPK LAITMGDAAG IGPEISLRVW DSPEVQSQGY PLLFGDAAIY
60 70 80 90 100
HRAAKKLGCD CPGTISLAEF LDMPKQSIPS DAPHGVIVDC GKLTTEELGS
110 120 130 140 150
FTPGKFSAAT GRASYQSVTD AIDAAVSGHV DAIVTGPIQK EAWHQAGIDF
160 170 180 190 200
PGHTELLADR AGRAVQGEPA DVRMMLASDT IACVLETIHI PLADVASQLN
210 220 230 240 250
TESLVRTINL AGETVQRRNQ NRGSLLPPRI AVCGLNPHAG ENGLFSHQEE
260 270 280 290 300
EQIILPAIEA ARQSGWTIEG PLSPDTAFTP AMRERIDIYV CMYHDQGLIP
310 320 330 340 350
LKALSFDDAV NVTLGLPIIR TSVDHGTAMD LAWQGKASIN SMLAAIRWAV

P
Length:351
Mass (Da):37,488
Last modified:October 1, 2003 - v1
Checksum:i6624680A06166B9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294146 Genomic DNA. Translation: CAD75627.1.
RefSeqiNP_868080.1. NC_005027.1.
WP_011121619.1. NC_005027.1.

Genome annotation databases

EnsemblBacteriaiCAD75627; CAD75627; RB7885.
GeneIDi1796393.
KEGGirba:RB7885.
PATRICi23249079. VBIRhoBal59814_3813.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294146 Genomic DNA. Translation: CAD75627.1.
RefSeqiNP_868080.1. NC_005027.1.
WP_011121619.1. NC_005027.1.

3D structure databases

ProteinModelPortaliQ7UMZ2.
SMRiQ7UMZ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243090.RB7885.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD75627; CAD75627; RB7885.
GeneIDi1796393.
KEGGirba:RB7885.
PATRICi23249079. VBIRhoBal59814_3813.

Phylogenomic databases

eggNOGiENOG4105CEZ. Bacteria.
COG1995. LUCA.
HOGENOMiHOG000221591.
InParanoidiQ7UMZ2.
KOiK00097.
OMAiVFMRARH.
OrthoDBiPOG091H03XD.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.

Family and domain databases

InterProiView protein in InterPro
IPR005255. PdxA.
PANTHERiPTHR30004. PTHR30004. 1 hit.
PfamiView protein in Pfam
PF04166. PdxA. 1 hit.
TIGRFAMsiTIGR00557. pdxA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPDXA_RHOBA
AccessioniPrimary (citable) accession number: Q7UMZ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: October 1, 2003
Last modified: May 10, 2017
This is version 87 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

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 one 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.