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.

Q3V7R9

- PDXA_RHOPA

UniProt

Q3V7R9 - PDXA_RHOPA

(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, RPA3065
Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
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 sitei139 – 1391Substrate By similarity
Binding sitei140 – 1401Substrate By similarity
Metal bindingi173 – 1731Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi218 – 2181Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi273 – 2731Divalent metal cation; shared with dimeric partner By similarity
Binding sitei281 – 2811Substrate By similarity
Binding sitei290 – 2901Substrate By similarity
Binding sitei299 – 2991Substrate 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

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:RPA3065
OrganismiRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Taxonomic identifieri258594 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000001426: 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 – 3373374-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotation
PRO_1000051511Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi258594.RPA3065.

Structurei

3D structure databases

ProteinModelPortaliQ3V7R9.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiAIGTEDE.
OrthoDBiEOG6GN6ZC.
PhylomeDBiQ3V7R9.

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.

Q3V7R9-1 [UniParc]FASTAAdd to Basket

« Hide

MTGMAKPLAL TLGEPAGIGP DIALAAWLKR EQHGLPPFYL LGDAGCLSRC    50
AKLLGLDVPL AEVKAEDAAA AFATTLPVVS TGQIATATPG QPDATSAPAA 100
IASIEHAVAD VRSGRAAAVV TNPIAKSVLY QAGFHHPGHT EFLAELAKRD 150
GIVPQPVMML WCPALAVVPV TIHVSLRDAI TQLTTDLIVS TARIVVKDLR 200
ERLGIAQPRL ALAGLNPHAG EDGALGQEDR AVVAPAVAIL RREGVDARGP 250
LPADTMFHAA ARKTYDCAIC MYHDQALIPI KTIAFDEGVN VTLGLPFIRT 300
SPDHGTAFDI AGSGQANPSS LIAALKLAAQ MASAKTA 337
Length:337
Mass (Da):34,927
Last modified:October 11, 2005 - v1
Checksum:i7C7AECA3938A5127
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX572602 Genomic DNA. Translation: CAE28506.1.
RefSeqiNP_948404.1. NC_005296.1.

Genome annotation databases

EnsemblBacteriaiCAE28506; CAE28506; RPA3065.
GeneIDi2690551.
KEGGirpa:RPA3065.
PATRICi23290597. VBIRhoPal84835_3222.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX572602 Genomic DNA. Translation: CAE28506.1 .
RefSeqi NP_948404.1. NC_005296.1.

3D structure databases

ProteinModelPortali Q3V7R9.
ModBasei Search...

Protein-protein interaction databases

STRINGi 258594.RPA3065.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE28506 ; CAE28506 ; RPA3065 .
GeneIDi 2690551.
KEGGi rpa:RPA3065.
PATRICi 23290597. VBIRhoPal84835_3222.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221592.
KOi K00097.
OMAi AIGTEDE.
OrthoDBi EOG6GN6ZC.
PhylomeDBi Q3V7R9.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .

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 BAA-98 / CGA009.

Entry informationi

Entry nameiPDXA_RHOPA
AccessioniPrimary (citable) accession number: Q3V7R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 63 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