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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
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

a divalent metal cationUniRule annotationNote: Binds 1 divalent metal cation per subunit.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)
  5. no protein annotated in this organism
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 sitei138 – 1381SubstrateUniRule annotation
Binding sitei139 – 1391SubstrateUniRule annotation
Metal bindingi168 – 1681Divalent 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 sitei292 – 2921SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, NADP

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:FN0226
OrganismiFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Taxonomic identifieri190304 [NCBI]
Taxonomic lineageiBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium
ProteomesiUP000002521 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 – 3323324-hydroxythreonine-4-phosphate dehydrogenasePRO_0000188808Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi190304.FN0226.

Structurei

3D structure databases

ProteinModelPortaliQ8RGR0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221593.
InParanoidiQ8RGR0.
KOiK00097.
OMAiEISVATM.
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.

Q8RGR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTKIAIPMG DPAGVGPEIV VKTAVSKEIL DLCDLVVIGD KKVLEKATKI
60 70 80 90 100
CQVDLKIHTI KNIEEGKYEK GILNVIDLEN VDMNTLEYGQ VQGMCGKAAF
110 120 130 140 150
EYIKKCVELA MEYKVDAIAT TPINKESLRA GNVNYIGHTE ILGDLSNSRD
160 170 180 190 200
PLTMFEVDNM RVFFLTRHMS LRKACDAITK ERVLEYIERC TKALKQLGVT
210 220 230 240 250
GKMAVAGLNP HSGEHGLFGN EEVKEITPAI EEAQKLGYDV VGPIGADSVF
260 270 280 290 300
HQALQGRYVA VLSLYHDQGH IATKTYDFER TIAITLDMPF LRTSVDHGTA
310 320 330
FDIAGKGIVS AISMIEAVKL AAKYAPNFKN IK
Length:332
Mass (Da):36,547
Last modified:June 1, 2002 - v1
Checksum:iA9032E3F6E7081FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009951 Genomic DNA. Translation: AAL94432.1.
RefSeqiNP_603133.1. NC_003454.1.
WP_011016238.1. NC_003454.1.

Genome annotation databases

EnsemblBacteriaiAAL94432; AAL94432; FN0226.
GeneIDi993114.
KEGGifnu:FN0226.
PATRICi21950229. VBIFusNuc122357_0807.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009951 Genomic DNA. Translation: AAL94432.1.
RefSeqiNP_603133.1. NC_003454.1.
WP_011016238.1. NC_003454.1.

3D structure databases

ProteinModelPortaliQ8RGR0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190304.FN0226.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL94432; AAL94432; FN0226.
GeneIDi993114.
KEGGifnu:FN0226.
PATRICi21950229. VBIFusNuc122357_0807.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221593.
InParanoidiQ8RGR0.
KOiK00097.
OMAiEISVATM.
OrthoDBiEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.

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: ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131.

Entry informationi

Entry nameiPDXA_FUSNN
AccessioniPrimary (citable) accession number: Q8RGR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 2002
Last modified: July 22, 2015
This is version 88 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.