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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
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. D-erythrose-4-phosphate dehydrogenase (epd)
  2. Erythronate-4-phosphate dehydrogenase (pdxB)
  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 sitei134 – 1341SubstrateUniRule annotation
Binding sitei135 – 1351SubstrateUniRule annotation
Metal bindingi164 – 1641Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi209 – 2091Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi264 – 2641Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei272 – 2721SubstrateUniRule annotation
Binding sitei281 – 2811SubstrateUniRule annotation
Binding sitei290 – 2901SubstrateUniRule 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

BioCyciSDEN318161:GHKQ-2996-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:Sden_2887
OrganismiShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
Taxonomic identifieri318161 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000001982 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 – 3283284-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128260Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi318161.Sden_2887.

Structurei

3D structure databases

ProteinModelPortaliQ12K60.
SMRiQ12K60. Positions 2-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiRAGQGCL.
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.

Q12K60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKRIAITAG EPASIGPDLV ITLAQQAWPA ELVVCANPEL LLARAAKLGL
60 70 80 90 100
PLRLIPYHSE NKPQPQAAGT LTIAPFELAA EVECGVLNEL NSAYVVDTLR
110 120 130 140 150
FAGEKNMSRE FDAVVTGPVH KGIINQAGIA FSGHTEYFAV QANCQDVVMM
160 170 180 190 200
LAAPGLQVAL MTTHIPLAYV AKAITRERLH HIIHILHKEL KSKFGLGSPK
210 220 230 240 250
IYVCGLNPHA GEDGHIGREE LDVMIPALNE LRAQGIQLVG PLPADTLFQP
260 270 280 290 300
KYLQDADVIL AMYHDQGLPV LKSLGFGKSV NITLGLPYIR TSVDHGTALE
310 320
LAGTGLADSG SFTCALNKAI ELASKVSN
Length:328
Mass (Da):35,054
Last modified:August 22, 2006 - v1
Checksum:i6C050F2226CB0A02
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000302 Genomic DNA. Translation: ABE56166.1.
RefSeqiWP_011497315.1. NC_007954.1.
YP_563889.1. NC_007954.1.

Genome annotation databases

EnsemblBacteriaiABE56166; ABE56166; Sden_2887.
KEGGisdn:Sden_2887.
PATRICi23491808. VBISheDen79529_3032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000302 Genomic DNA. Translation: ABE56166.1.
RefSeqiWP_011497315.1. NC_007954.1.
YP_563889.1. NC_007954.1.

3D structure databases

ProteinModelPortaliQ12K60.
SMRiQ12K60. Positions 2-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi318161.Sden_2887.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE56166; ABE56166; Sden_2887.
KEGGisdn:Sden_2887.
PATRICi23491808. VBISheDen79529_3032.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiRAGQGCL.
OrthoDBiEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.
BioCyciSDEN318161:GHKQ-2996-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: OS217 / ATCC BAA-1090 / DSM 15013.

Entry informationi

Entry nameiPDXA_SHEDO
AccessioniPrimary (citable) accession number: Q12K60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: August 22, 2006
Last modified: May 27, 2015
This is version 70 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.