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C0QBU5

- PDXA_DESAH

UniProt

C0QBU5 - PDXA_DESAH

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene
pdxA, HRM2_18550
Organism
Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
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) By similarity.UniRule annotation

Catalytic activityi

4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH.UniRule annotation

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Substrate By similarity
Binding sitei142 – 1421Substrate By similarity
Metal bindingi171 – 1711Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi216 – 2161Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi271 – 2711Divalent metal cation; shared with dimeric partner By similarity
Binding sitei279 – 2791Substrate By similarity
Binding sitei288 – 2881Substrate By similarity
Binding sitei297 – 2971Substrate By similarity

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

BioCyciDAUT177437:GHLR-1854-MONOMER.
UniPathwayiUPA00244; UER00312.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenase (EC:1.1.1.262)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase
Gene namesi
Name:pdxA
Ordered Locus Names:HRM2_18550
OrganismiDesulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
Taxonomic identifieri177437 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfobacterium
ProteomesiUP000000442: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 – 3403404-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotationPRO_1000211912Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi177437.HRM2_18550.

Structurei

3D structure databases

ProteinModelPortaliC0QBU5.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221593.
KOiK00097.
OMAiSIDIRTI.
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.

C0QBU5-1 [UniParc]FASTAAdd to Basket

« Hide

MTDNRPVIGI TMGDPVGIGP EIIVSALDDP FVYTVCRPLV LGDEGVMERA    50
IDLKSARMDV HTTDTPAGGK YCHGTMDIVP LSRLDAATLL AGHPTPGTGK 100
AMIDYITTGV DLAMDGKIQA IATCPITKTA MKLAGSKFHG HTELIADRTH 150
TPRVAMMMAG DRLRVVLVTI HIPLCEVSAR LNQAEILATI SLTSETLKTK 200
FGIPEPRIAV AGLNPHGGED GMFGSEELEI IAPAVEQARS KGITVSGPFP 250
PDTLFFNAAN HKFDAVVCMY HDQGLIPFKM IHFSDGVNTT LGLPIIRTSV 300
DHGTAYDIAW RGTADPSSLI AAIKMAALQA TITGANRINR 340
Length:340
Mass (Da):36,215
Last modified:May 5, 2009 - v1
Checksum:iD10C3F53007C3BA4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001087 Genomic DNA. Translation: ACN14957.1.
RefSeqiYP_002603121.1. NC_012108.1.

Genome annotation databases

EnsemblBacteriaiACN14957; ACN14957; HRM2_18550.
GeneIDi7500958.
KEGGidat:HRM2_18550.
PATRICi21683381. VBIDesAut25181_1961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001087 Genomic DNA. Translation: ACN14957.1 .
RefSeqi YP_002603121.1. NC_012108.1.

3D structure databases

ProteinModelPortali C0QBU5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 177437.HRM2_18550.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACN14957 ; ACN14957 ; HRM2_18550 .
GeneIDi 7500958.
KEGGi dat:HRM2_18550.
PATRICi 21683381. VBIDesAut25181_1961.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci DAUT177437:GHLR-1854-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: ATCC 43914 / DSM 3382 / HRM2.

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: May 14, 2014
This is version 41 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 By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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