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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Novosphingobium aromaticivorans (Sphingomonas aromaticivorans)
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)
  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
Metal bindingi169 – 1691Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi213 – 2131Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi263 – 2631Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei271 – 2711SubstrateUniRule 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

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
Encoded oniPlasmid pNL10 Publication
OrganismiNovosphingobium aromaticivorans (Sphingomonas aromaticivorans)
Taxonomic identifieri48935 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium

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_0000188830Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliO85987.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

KOiK00097.

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]

Sequencei

Sequence statusi: Complete.

O85987-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTASERVRP VVGTMIGDPA GIGPEVAVRA LADGAVHTDS IPVLVGSAAA
60 70 80 90 100
VERALDFTGT KARLRVMRGF EKPSDDPAII DVIDTGALPD GVLPLGEDTE
110 120 130 140 150
AAGHATAQWL DELDALARDG SFAATIMGPI STGSLKLAKK LDRVISPTPG
160 170 180 190 200
ESYLVLLTGP LRVAHLTDHM SLRQVIDVIS ADLVATAVGQ LHEAMQSWGI
210 220 230 240 250
AQPRIAVAGL NPHAMGDEDR LEIAPGIEAA RARGIDVEGP IAPDSVFRHC
260 270 280 290 300
IEGRYDMVLA MFHDQGHIAV KTWGFSGNSV IIMGPPYLHM SVAHGTAYDI
310 320 330
VGTGKADAAM MLSAMRTCGR LASGRGFEQA
Length:330
Mass (Da):34,579
Last modified:November 1, 1998 - v1
Checksum:i55ABBF8B500CE707
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079317 Genomic DNA. Translation: AAD04003.1.
PIRiT31279.
RefSeqiNP_049207.1. NC_002033.1.
WP_010891025.1. NC_002033.1.

Genome annotation databases

GeneIDi1238515.
KEGGipg:1238515.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079317 Genomic DNA. Translation: AAD04003.1.
PIRiT31279.
RefSeqiNP_049207.1. NC_002033.1.
WP_010891025.1. NC_002033.1.

3D structure databases

ProteinModelPortaliO85987.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1238515.
KEGGipg:1238515.

Phylogenomic databases

KOiK00097.

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]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of a 184 kb catabolic plasmid from Sphingomonas aromaticivorans strain F199."
    Romine M.F., Stillwell L.C., Wong K.-K., Thurston S.J., Sisk E.C., Sensen C.W., Gaasterland T., Saffer J.D., Fredrickson J.K.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 700278 / DSM 12444 / F199.

Entry informationi

Entry nameiPDXA_NOVAR
AccessioniPrimary (citable) accession number: O85987
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: November 1, 1998
Last modified: May 27, 2015
This is version 68 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

Plasmid

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.