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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
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. no protein annotated in this organism
  3. no protein annotated in this organism
  4. 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA), 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
  5. Pyridoxine 5'-phosphate synthase (pdxJ), 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 sitei141 – 1411SubstrateUniRule annotation
Binding sitei142 – 1421SubstrateUniRule annotation
Metal bindingi176 – 1761Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi221 – 2211Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi276 – 2761Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei284 – 2841SubstrateUniRule annotation
Binding sitei293 – 2931SubstrateUniRule annotation
Binding sitei302 – 3021SubstrateUniRule 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

BioCyciBMEL224914:GCJ0-1306-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:BMEI1266
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000419 Componenti: Chromosome I

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 – 3433434-hydroxythreonine-4-phosphate dehydrogenasePRO_0000188800Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224914.BAWG_0944.

Structurei

3D structure databases

ProteinModelPortaliP65680.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000221592.
KOiK00097.
OMAiINPHSGD.
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.

P65680-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAKPLPPLA VSIGDPSGIG ADVALAAWLK RCELSLPPFF LIADPKQLAA
60 70 80 90 100
RARHLGLAVD FAILSDPREA EAAFGERLPL LALKHSHTES PGKPLTENAA
110 120 130 140 150
GVIEAIERAV ELTLKGEAAA VVTCPIAKKP LYEAGFQHPG HTEFLAELAG
160 170 180 190 200
HHLGKPVTPV MMLAGPQLRA VPVTIHIPLS EVPARLTTTE IVAVSRITAN
210 220 230 240 250
ELRERFGIAS PRLAISGLNP HAGEGGALGK EDDAIILPAI EQLIREGIDA
260 270 280 290 300
RGPLPADTMF HAPARATYDA AICMYHDQAL IPAKALAFDE TVNVTLGLPF
310 320 330 340
IRTSPDHGTA FDIAGKGIAR PDSLVAAMRL AQQLAENAAS RNA
Length:343
Mass (Da):36,193
Last modified:October 11, 2004 - v1
Checksum:iFBF6CA0AB6D28617
GO

Sequence cautioni

The sequence AAL52447.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL52447.1. Different initiation.
PIRiAD3410.
RefSeqiWP_004683429.1. NZ_GG703778.1.

Genome annotation databases

EnsemblBacteriaiAAL52447; AAL52447; BMEI1266.
KEGGibme:BMEI1266.
PATRICi17852859. VBIBruMel92729_1421.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL52447.1. Different initiation.
PIRiAD3410.
RefSeqiWP_004683429.1. NZ_GG703778.1.

3D structure databases

ProteinModelPortaliP65680.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224914.BAWG_0944.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL52447; AAL52447; BMEI1266.
KEGGibme:BMEI1266.
PATRICi17852859. VBIBruMel92729_1421.

Phylogenomic databases

HOGENOMiHOG000221592.
KOiK00097.
OMAiINPHSGD.
OrthoDBiEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.
BioCyciBMEL224914:GCJ0-1306-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 16M / ATCC 23456 / NCTC 10094.

Entry informationi

Entry nameiPDXA_BRUME
AccessioniPrimary (citable) accession number: P65680
Secondary accession number(s): P58712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 22, 2015
This is version 76 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. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.