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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Xanthomonas campestris pv. campestris (strain B100)
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: 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. 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 sitei132 – 1321SubstrateUniRule annotation
Metal bindingi160 – 1601Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi205 – 2051Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi260 – 2601Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei268 – 2681SubstrateUniRule annotation
Binding sitei277 – 2771SubstrateUniRule annotation
Binding sitei286 – 2861SubstrateUniRule 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

BioCyciXCAM509169:GHW4-3642-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:xcc-b100_3559
OrganismiXanthomonas campestris pv. campestris (strain B100)
Taxonomic identifieri509169 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000001188 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 – 3223224-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128265Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB0RUI2.
SMRiB0RUI2. Positions 1-321.
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.

B0RUI2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPSLALVPG EPAGIGPELC IRLAQQPRSD AHLIVYADPD TLHSAAKALC
60 70 80 90 100
LSVRLLDPDQ PARLPGDLPL HPIRQAAPTR FGTPDPANAA AVIAGLLGAA
110 120 130 140 150
GDCLSGKLQG IVTGPVHKAV INAGGIAYTG TTELLAAQAG CPVVMMLANS
160 170 180 190 200
IVRVALVTTH LPLRAVPEAI TAEALARCLR ITATAMQRDF GLEHPRIAVL
210 220 230 240 250
GLNPHAGEDG LLGREELDVI IPVLDQLRSE GMQLIGPLPA DTAFLPQKLT
260 270 280 290 300
DFDAVVAMYH DQGLPVLKYS GFEQAVNITL GLPYPRVAVD HGTALELAGR
310 320
GVADPSSLLA ATALCARLAA RS
Length:322
Mass (Da):33,447
Last modified:April 8, 2008 - v1
Checksum:i307A6B1CD2B5EE3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920689 Genomic DNA. Translation: CAP52924.1.
RefSeqiWP_012439174.1. NC_010688.1.
YP_001904964.1. NC_010688.1.

Genome annotation databases

EnsemblBacteriaiCAP52924; CAP52924; xcc-b100_3559.
KEGGixca:xccb100_3559.
PATRICi24087060. VBIXanCam108527_3591.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920689 Genomic DNA. Translation: CAP52924.1.
RefSeqiWP_012439174.1. NC_010688.1.
YP_001904964.1. NC_010688.1.

3D structure databases

ProteinModelPortaliB0RUI2.
SMRiB0RUI2. Positions 1-321.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAP52924; CAP52924; xcc-b100_3559.
KEGGixca:xccb100_3559.
PATRICi24087060. VBIXanCam108527_3591.

Phylogenomic databases

eggNOGiCOG1995.
KOiK00097.
OMAiDTLFQDK.
OrthoDBiEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.
BioCyciXCAM509169:GHW4-3642-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. "The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
    Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
    J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B100.

Entry informationi

Entry nameiPDXA_XANCB
AccessioniPrimary (citable) accession number: B0RUI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: June 24, 2015
This is version 60 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

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.