SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q88A45

- PDXA_PSESM

UniProt

Q88A45 - PDXA_PSESM

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
4-hydroxythreonine-4-phosphate dehydrogenase
Gene
pdxA, PSPTO_0552
Organism
Pseudomonas syringae pv. tomato (strain DC3000)
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. NAD binding Source: InterPro
  3. cobalt ion binding Source: UniProtKB-HAMAP
  4. magnesium ion binding Source: UniProtKB-HAMAP
  5. zinc ion binding Source: UniProtKB-HAMAP
Complete GO annotation...

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

BioCyciPSYR223283:GJIX-550-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:PSPTO_0552
OrganismiPseudomonas syringae pv. tomato (strain DC3000)
Taxonomic identifieri223283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002515: 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 annotation
PRO_0000188818Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi223283.PSPTO_0552.

Structurei

3D structure databases

ProteinModelPortaliQ88A45.
SMRiQ88A45. Positions 5-327.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiEQNSAYV.
OrthoDBiEOG6GN6ZC.
PhylomeDBiQ88A45.

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.

Q88A45-1 [UniParc]FASTAAdd to Basket

« Hide

MKPKRFALTP GEPAGIGPDL CLLLATQPQP YPLIAITSRD LLTQRAAQLG    50
VAVSLLDVTP ETLPDQPAPA GSLYVWHTPL AAPVETGVLN KANAAFVLQT 100
LTRAGQGCLD GLFSGMITAP VHKGVINDGG IAFSGHTEFL AELTHTEQVV 150
MMLATGDLRV ALVTTHLPLR EVADAITADR LERVTRILHA DLVNKFGIAH 200
PRILVCGLNP HAGESGHLGR EEIDIIEPTL ERLRSEGLDL RGPLPADTLF 250
TPKYLEHCDA VLAMYHDQGL PVLKYKGFGA AVNVTLGLPI IRTSVDHGTA 300
LDLAGSANID TGSLRVALQT AYQMAETHS 329
Length:329
Mass (Da):35,042
Last modified:June 1, 2003 - v1
Checksum:i4568463F9792EED9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016853 Genomic DNA. Translation: AAO54094.1.
RefSeqiNP_790399.1. NC_004578.1.

Genome annotation databases

EnsemblBacteriaiAAO54094; AAO54094; PSPTO_0552.
GeneIDi1182162.
KEGGipst:PSPTO_0552.
PATRICi19992270. VBIPseSyr93040_0562.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016853 Genomic DNA. Translation: AAO54094.1 .
RefSeqi NP_790399.1. NC_004578.1.

3D structure databases

ProteinModelPortali Q88A45.
SMRi Q88A45. Positions 5-327.
ModBasei Search...

Protein-protein interaction databases

STRINGi 223283.PSPTO_0552.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO54094 ; AAO54094 ; PSPTO_0552 .
GeneIDi 1182162.
KEGGi pst:PSPTO_0552.
PATRICi 19992270. VBIPseSyr93040_0562.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221592.
KOi K00097.
OMAi EQNSAYV.
OrthoDBi EOG6GN6ZC.
PhylomeDBi Q88A45.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci PSYR223283:GJIX-550-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: DC3000.

Entry informationi

Entry nameiPDXA_PSESM
AccessioniPrimary (citable) accession number: Q88A45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 80 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

Similar proteinsi