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C0QBU5

- PDXA_DESAH

UniProt

C0QBU5 - PDXA_DESAH

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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: 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 sitei141 – 1411SubstrateUniRule annotation
Binding sitei142 – 1421SubstrateUniRule annotation
Metal bindingi171 – 1711Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi216 – 2161Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi271 – 2711Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei279 – 2791SubstrateUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Binding sitei297 – 2971SubstrateUniRule 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

BioCyciDAUT177437:GHLR-1854-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:HRM2_18550
OrganismiDesulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
Taxonomic identifieri177437 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfobacterium
ProteomesiUP000000442: 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 – 3403404-hydroxythreonine-4-phosphate dehydrogenasePRO_1000211912Add
BLAST

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

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

        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:
EMBL
GenBank
DDBJ
Links Updated
CP001087 Genomic DNA. Translation: ACN14957.1.
RefSeqiWP_015903743.1. NC_012108.1.
YP_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 WP_015903743.1. NC_012108.1.
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: October 29, 2014
This is version 43 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