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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei133 – 1331SubstrateUniRule annotation
Binding sitei134 – 1341SubstrateUniRule annotation
Metal bindingi163 – 1631Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi208 – 2081Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi263 – 2631Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei271 – 2711SubstrateUniRule annotation
Binding sitei280 – 2801SubstrateUniRule annotation
Binding sitei289 – 2891SubstrateUniRule annotation

GO - Molecular functioni

  1. 4-hydroxythreonine-4-phosphate dehydrogenase activity Source: UniProtKB-HAMAP
  2. cobalt ion binding Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP
  4. NAD binding Source: InterPro
  5. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. pyridoxal phosphate biosynthetic process Source: UniProtKB-HAMAP
  2. pyridoxine biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciPATL342610:GHGT-3489-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:Patl_3420
OrganismiPseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
Taxonomic identifieri342610 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas
ProteomesiUP000001981: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3263264-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128257Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi342610.Patl_3420.

Structurei

3D structure databases

ProteinModelPortaliQ15QB2.
SMRiQ15QB2. Positions 2-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
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.

Q15QB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIKLAITPG EPAGVGPDLI ITLAQQQWQA MLVVFANAEL MRTRANELNI
60 70 80 90 100
PLTLLPYDAS RTDIQPAGSL YIVDIPLQDE VIAGKLNPTN SQYVLDTLHQ
110 120 130 140 150
ACQMNLNGEF QALVTGPVHK GVINEAGIPF SGHTEFFAQQ SNTPEVVMML
160 170 180 190 200
ATEGLRVTLA TTHIPVTAVS AAITQPKLDN VIRIIDHDLR TKFGIAKPHI
210 220 230 240 250
FVCGLNPHAG EDGHIGREEI DTIIPALNAL RQEGITLTGP LPADTIFNPK
260 270 280 290 300
YLQQADTVLA MYHDQGLPVL KYKGFSQAVN ITLGLPFIRT SVDHGTALDL
310 320
AATGQADVGS FSIAIKEAIS LAKSTQ
Length:326
Mass (Da):35,063
Last modified:July 25, 2006 - v1
Checksum:i65BD0237F78722A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000388 Genomic DNA. Translation: ABG41926.1.
RefSeqiWP_011576155.1. NC_008228.1.
YP_662980.1. NC_008228.1.

Genome annotation databases

EnsemblBacteriaiABG41926; ABG41926; Patl_3420.
GeneIDi4175197.
KEGGipat:Patl_3420.
PATRICi23052164. VBIPseAtl25434_3635.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000388 Genomic DNA. Translation: ABG41926.1.
RefSeqiWP_011576155.1. NC_008228.1.
YP_662980.1. NC_008228.1.

3D structure databases

ProteinModelPortaliQ15QB2.
SMRiQ15QB2. Positions 2-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi342610.Patl_3420.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG41926; ABG41926; Patl_3420.
GeneIDi4175197.
KEGGipat:Patl_3420.
PATRICi23052164. VBIPseAtl25434_3635.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiDTLFQDK.
OrthoDBiEOG6GN6ZC.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.
BioCyciPATL342610:GHGT-3489-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: T6c / ATCC BAA-1087.

Entry informationi

Entry nameiPDXA_PSEA6
AccessioniPrimary (citable) accession number: Q15QB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 25, 2006
Last modified: February 4, 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.