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Q9KUS1

- PDXA_VIBCH

UniProt

Q9KUS1 - PDXA_VIBCH

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene
pdxA, VC_0444
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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 sitei135 – 1351Substrate By similarity
Binding sitei136 – 1361Substrate By similarity
Metal bindingi165 – 1651Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi210 – 2101Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi266 – 2661Divalent metal cation; shared with dimeric partner By similarity
Binding sitei274 – 2741Substrate By similarity
Binding sitei283 – 2831Substrate By similarity
Binding sitei292 – 2921Substrate By similarity

GO - Molecular functioni

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

GO - Biological processi

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

BioCyciVCHO:VC0444-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:VC_0444
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584: Chromosome 1

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 – 3303304-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotationPRO_0000188833Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi243277.VC0444.

Structurei

3D structure databases

ProteinModelPortaliQ9KUS1.
SMRiQ9KUS1. Positions 1-325.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
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.

Q9KUS1-1 [UniParc]FASTAAdd to Basket

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MSSKRIIVTA GEPAGIGPDL VLALSAQDWP HQLVVCADKA LLAQRATQLG    50
IQVKLLDYQR DNPVQAQQAG TLLVEHIPLA EPVVAGQLNP ANGHYVLKTL 100
ERAAKGCMNG EFDAIVTGPV HKGVINRAGV AFSGHTEFFA EQSKTPLVVM 150
MLATEGLRTA LVTTHLPLAE VPQAITCERL EQIVHILHKD LVEKFAIAEP 200
KIYVCGLNPH AGEDGVLGMD EIETITPTLQ RLREQYGMQL VGPLPADTIF 250
SEKYLQQADA VLGMYHDQVL PVLKYKGFGR SVNITLGLPF IRTSVDHGTA 300
LDLAGTGQAD AGSFWTALAY AIELVDKKAQ 330
Length:330
Mass (Da):35,605
Last modified:October 1, 2000 - v1
Checksum:iEDA785D5D5513995
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF93617.1.
PIRiC82323.
RefSeqiNP_230098.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF93617; AAF93617; VC_0444.
GeneIDi2615776.
KEGGivch:VC0444.
PATRICi20079967. VBIVibCho83274_0418.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF93617.1 .
PIRi C82323.
RefSeqi NP_230098.1. NC_002505.1.

3D structure databases

ProteinModelPortali Q9KUS1.
SMRi Q9KUS1. Positions 1-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243277.VC0444.

Protocols and materials databases

DNASUi 2615776.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF93617 ; AAF93617 ; VC_0444 .
GeneIDi 2615776.
KEGGi vch:VC0444.
PATRICi 20079967. VBIVibCho83274_0418.

Phylogenomic databases

eggNOGi COG1995.
KOi K00097.
OMAi DTLFQDK.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci VCHO:VC0444-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 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiPDXA_VIBCH
AccessioniPrimary (citable) accession number: Q9KUS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 81 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, 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

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