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A8ZUN0

- PDXA_DESOH

UniProt

A8ZUN0 - PDXA_DESOH

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Desulfococcus oleovorans (strain DSM 6200 / Hxd3)
Status
Reviewed - 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

Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391SubstrateUniRule annotation
Binding sitei140 – 1401SubstrateUniRule annotation
Metal bindingi169 – 1691Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi214 – 2141Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi270 – 2701Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei278 – 2781SubstrateUniRule annotation
Binding sitei287 – 2871SubstrateUniRule annotation
Binding sitei296 – 2961SubstrateUniRule 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

BioCyciDOLE96561:GHF3-648-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:Dole_0633
OrganismiDesulfococcus oleovorans (strain DSM 6200 / Hxd3)
Taxonomic identifieri96561 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfococcus
ProteomesiUP000008561: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3383384-hydroxythreonine-4-phosphate dehydrogenasePRO_1000211913Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi96561.Dole_0633.

Structurei

3D structure databases

ProteinModelPortaliA8ZUN0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221593.
KOiK00097.
OMAiAIPMGDP.
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.

A8ZUN0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPRPLIGIT MGDPVGIGPE IILTALAGTS VYEKCRPLVI GDPGVLGQAM
60 70 80 90 100
AVAGYAPVIH MTDTPETGVY RPGTISMFSP APPLSPVTWG EPTPETGGAM
110 120 130 140 150
EAWITTAVDM AMAGAISAMV TCPINKEALK MAGSAFAGHT EMLAMRTGTN
160 170 180 190 200
RYAMMLAGNR LRVVLVTIHT ALQNVPGLLS VDAIADTILL TVESLKQRFG
210 220 230 240 250
MNAPRVAVAG LNPHAGEGGL FGDEEARLIT PAIEAARRKT EAAITGPWPP
260 270 280 290 300
DTVFVKAAAG DFDAVVCMYH DQGLIPFKLL HFEDGVNTTL GLPIIRTSVD
310 320 330
HGTAYDIAGT GRADCRSLTA AIDMAIDQAA CLGKRPAA
Length:338
Mass (Da):35,285
Last modified:January 15, 2008 - v1
Checksum:i2F821914F8A5FDD8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000859 Genomic DNA. Translation: ABW66443.1.
RefSeqiYP_001528520.1. NC_009943.1.

Genome annotation databases

EnsemblBacteriaiABW66443; ABW66443; Dole_0633.
GeneIDi5693462.
KEGGidol:Dole_0633.
PATRICi21691273. VBIDesOle35880_0654.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000859 Genomic DNA. Translation: ABW66443.1 .
RefSeqi YP_001528520.1. NC_009943.1.

3D structure databases

ProteinModelPortali A8ZUN0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 96561.Dole_0633.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABW66443 ; ABW66443 ; Dole_0633 .
GeneIDi 5693462.
KEGGi dol:Dole_0633.
PATRICi 21691273. VBIDesOle35880_0654.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221593.
KOi K00097.
OMAi AIPMGDP.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci DOLE96561:GHF3-648-MONOMER.

Family and domain databases

Gene3Di 3.40.718.10. 1 hit.
HAMAPi MF_00536. PdxA.
InterProi IPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view ]
Pfami PF04166. PdxA. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00557. pdxA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 6200 / Hxd3.

Entry informationi

Entry nameiPDXA_DESOH
AccessioniPrimary (citable) accession number: A8ZUN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: January 15, 2008
Last modified: October 29, 2014
This is version 55 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