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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
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 Zn2+, Mg2+ or Co2+.UniRule annotation

Pathwayi: 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. no protein annotated in this organism
  2. no protein annotated in this organism
  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)DescriptionActionsGraphical viewLength
Binding sitei141SubstrateUniRule annotation1
Binding sitei142SubstrateUniRule annotation1
Metal bindingi171Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi216Divalent metal cation; shared with dimeric partnerUniRule annotation1
Metal bindingi271Divalent metal cation; shared with dimeric partnerUniRule annotation1
Binding sitei279SubstrateUniRule annotation1
Binding sitei288SubstrateUniRule annotation1
Binding sitei297SubstrateUniRule annotation1

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
Ordered Locus Names:HRM2_18550
OrganismiDesulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
Taxonomic identifieri177437 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfobacterium
Proteomesi
  • UP000000442 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002119121 – 3404-hydroxythreonine-4-phosphate dehydrogenaseAdd BLAST340

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi177437.HRM2_18550.

Structurei

3D structure databases

ProteinModelPortaliC0QBU5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEZ. Bacteria.
COG1995. LUCA.
HOGENOMiHOG000221593.
KOiK00097.
OMAiCELADDK.
OrthoDBiPOG091H03XD.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
HAMAPiMF_00536. PdxA. 1 hit.
InterProiIPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view]
PfamiPF04166. PdxA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00557. pdxA. 1 hit.

Sequencei

Sequence statusi: Complete.

C0QBU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDNRPVIGI TMGDPVGIGP EIIVSALDDP FVYTVCRPLV LGDEGVMERA
60 70 80 90 100
IDLKSARMDV HTTDTPAGGK YCHGTMDIVP LSRLDAATLL AGHPTPGTGK
110 120 130 140 150
AMIDYITTGV DLAMDGKIQA IATCPITKTA MKLAGSKFHG HTELIADRTH
160 170 180 190 200
TPRVAMMMAG DRLRVVLVTI HIPLCEVSAR LNQAEILATI SLTSETLKTK
210 220 230 240 250
FGIPEPRIAV AGLNPHGGED GMFGSEELEI IAPAVEQARS KGITVSGPFP
260 270 280 290 300
PDTLFFNAAN HKFDAVVCMY HDQGLIPFKM IHFSDGVNTT LGLPIIRTSV
310 320 330 340
DHGTAYDIAW RGTADPSSLI AAIKMAALQA TITGANRINR
Length:340
Mass (Da):36,215
Last modified:May 5, 2009 - v1
Checksum:iD10C3F53007C3BA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001087 Genomic DNA. Translation: ACN14957.1.
RefSeqiWP_015903743.1. NC_012108.1.

Genome annotation databases

EnsemblBacteriaiACN14957; ACN14957; HRM2_18550.
KEGGidat:HRM2_18550.
PATRICi21683381. VBIDesAut25181_1961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001087 Genomic DNA. Translation: ACN14957.1.
RefSeqiWP_015903743.1. NC_012108.1.

3D structure databases

ProteinModelPortaliC0QBU5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi177437.HRM2_18550.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACN14957; ACN14957; HRM2_18550.
KEGGidat:HRM2_18550.
PATRICi21683381. VBIDesAut25181_1961.

Phylogenomic databases

eggNOGiENOG4105CEZ. Bacteria.
COG1995. LUCA.
HOGENOMiHOG000221593.
KOiK00097.
OMAiCELADDK.
OrthoDBiPOG091H03XD.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00312.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
HAMAPiMF_00536. PdxA. 1 hit.
InterProiIPR024084. IsoPropMal-DH-like_dom.
IPR005255. PdxA.
[Graphical view]
PfamiPF04166. PdxA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00557. pdxA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPDXA_DESAH
AccessioniPrimary (citable) accession number: C0QBU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 5, 2009
Last modified: November 2, 2016
This is version 51 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

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 one 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.