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Q32K42

- PDXA_SHIDS

UniProt

Q32K42 - PDXA_SHIDS

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene
pdxA, SDY_0077
Organism
Shigella dysenteriae serotype 1 (strain Sd197)
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 sitei136 – 1361Substrate By similarity
Binding sitei137 – 1371Substrate By similarity
Metal bindingi166 – 1661Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi211 – 2111Divalent 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. 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

BioCyciSDYS300267:GJEW-77-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:SDY_0077
OrganismiShigella dysenteriae serotype 1 (strain Sd197)
Taxonomic identifieri300267 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000002716: 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 – 3293294-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotationPRO_1000051515Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi300267.SDY_0077.

Structurei

3D structure databases

ProteinModelPortaliQ32K42.
SMRiQ32K42. Positions 1-329.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
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.

Q32K42-1 [UniParc]FASTAAdd to Basket

« Hide

MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA TLLTDRAAML    50
GLPLTLRPYS PNSPAQPQTA GILTLLPVAL RESVTAGQLA VENGHYVVET 100
LARACDGCLN GEFAALITGP VHKGVINDAG IPFTGHTEFF EERSRAKKVV 150
MMLATEELRV ALATTHLPLR DIADAITPAL LHEVIAILHH DLRTKFGIAE 200
PRILVCGLNP HAGEGGHMGT EEIGTIIPVL DELRAQGMKL SGPLPADTLF 250
QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA 300
LELAGRGEAD VGSFITALNL AIKMIVNTQ 329
Length:329
Mass (Da):35,120
Last modified:December 6, 2005 - v1
Checksum:iEFCC745DF04FA294
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000034 Genomic DNA. Translation: ABB60315.1.
RefSeqiYP_401804.1. NC_007606.1.

Genome annotation databases

EnsemblBacteriaiABB60315; ABB60315; SDY_0077.
GeneIDi3798957.
KEGGisdy:SDY_0077.
PATRICi18689171. VBIShiDys99784_0087.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000034 Genomic DNA. Translation: ABB60315.1 .
RefSeqi YP_401804.1. NC_007606.1.

3D structure databases

ProteinModelPortali Q32K42.
SMRi Q32K42. Positions 1-329.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300267.SDY_0077.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB60315 ; ABB60315 ; SDY_0077 .
GeneIDi 3798957.
KEGGi sdy:SDY_0077.
PATRICi 18689171. VBIShiDys99784_0087.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221592.
KOi K00097.
OMAi DTLFQDK.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci SDYS300267:GJEW-77-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: Sd197.

Entry informationi

Entry nameiPDXA_SHIDS
AccessioniPrimary (citable) accession number: Q32K42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 59 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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