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B3Q9S3

- PDXA_RHOPT

UniProt

B3Q9S3 - PDXA_RHOPT

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Rhodopseudomonas palustris (strain TIE-1)
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

Zn2+UniRule annotation, Mg2+UniRule annotation, Co2+UniRule annotationNote: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391SubstrateUniRule annotation
Binding sitei140 – 1401SubstrateUniRule annotation
Metal bindingi173 – 1731Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi218 – 2181Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi273 – 2731Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei281 – 2811SubstrateUniRule annotation
Binding sitei290 – 2901SubstrateUniRule annotation
Binding sitei299 – 2991SubstrateUniRule 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

BioCyciRPAL395960:GHPC-3508-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:Rpal_3475
OrganismiRhodopseudomonas palustris (strain TIE-1)
Taxonomic identifieri395960 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas
ProteomesiUP000001725: 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 – 3373374-hydroxythreonine-4-phosphate dehydrogenasePRO_1000128259Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi395960.Rpal_3475.

Structurei

3D structure databases

ProteinModelPortaliB3Q9S3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

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.

B3Q9S3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTGMAKPLAL TLGEPAGIGP DIALAAWLKR EQHGLPPFYL LGDAGCLSRC
60 70 80 90 100
AKLLGLDVPL AEVKAEDAAA AFATTLPVVS TGQIATATPG QPDATSAPAA
110 120 130 140 150
IASIEHAVAD VRSGRAAAVV TNPIAKSVLY QAGFHHPGHT EFLAELAKRD
160 170 180 190 200
GIVPQPVMML WCPALAVVPV TIHVSLRDAI TQLTTDLIVS TARIVVKDLR
210 220 230 240 250
ERLGIAQPRL ALAGLNPHAG EDGALGQEDR AVVAPAVAIL RREGVDARGP
260 270 280 290 300
LPADTMFHAA ARKTYDCAIC MYHDQALIPI KTIAFDEGVN VTLGLPFIRT
310 320 330
SPDHGTAFDI AGSGQANPSS LIAALKLAAQ MASAKTA
Length:337
Mass (Da):34,927
Last modified:September 2, 2008 - v1
Checksum:i7C7AECA3938A5127
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001096 Genomic DNA. Translation: ACF01976.1.
RefSeqiWP_011158611.1. NC_011004.1.
YP_001992451.1. NC_011004.1.

Genome annotation databases

EnsemblBacteriaiACF01976; ACF01976; Rpal_3475.
GeneIDi6411149.
KEGGirpt:Rpal_3475.
PATRICi23311442. VBIRhoPal88240_3520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001096 Genomic DNA. Translation: ACF01976.1 .
RefSeqi WP_011158611.1. NC_011004.1.
YP_001992451.1. NC_011004.1.

3D structure databases

ProteinModelPortali B3Q9S3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 395960.Rpal_3475.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF01976 ; ACF01976 ; Rpal_3475 .
GeneIDi 6411149.
KEGGi rpt:Rpal_3475.
PATRICi 23311442. VBIRhoPal88240_3520.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci RPAL395960:GHPC-3508-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: TIE-1.

Entry informationi

Entry nameiPDXA_RHOPT
AccessioniPrimary (citable) accession number: B3Q9S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: November 26, 2014
This is version 52 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3