Skip Header

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

Q984S6

- PDXA_RHILO

UniProt

Q984S6 - PDXA_RHILO

(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

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
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 bindingi174 – 1741Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi219 – 2191Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi274 – 2741Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei282 – 2821SubstrateUniRule annotation
Binding sitei291 – 2911SubstrateUniRule annotation
Binding sitei300 – 3001SubstrateUniRule 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

BioCyciMLOT266835:GJ9L-6244-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:mll7861
OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Taxonomic identifieri266835 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
ProteomesiUP000000552: 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 – 3423424-hydroxythreonine-4-phosphate dehydrogenasePRO_0000188820Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi266835.mll7861.

Structurei

3D structure databases

ProteinModelPortaliQ984S6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
OMAiFHECARK.
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.

Q984S6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKSAMTALAL SVGDPSGIGP EIAIAAFLAR EAVGLPAFYL LADPALIASR
60 70 80 90 100
ASRLGVSVPI VETTPALAAQ VFARALPIVP LAARFIDSPG RPDPANAAGT
110 120 130 140 150
VEAIDRAVAA CLAGDAAAMV TCPIAKKPLY DAGFRFPGHT EYLAHLAARH
160 170 180 190 200
SGVEAMPVMM LAGPDLRTVP VTIHIALAEV PKALTTELIV ATARITAADL
210 220 230 240 250
AGRFGIARPR LAIAGLNPHA GEGGSLGLED EHIVRPAVDI LRAEGIDAFG
260 270 280 290 300
PLAADTLFHA RARAGYDAAL CMYHDQALIP AKTLAFDDAV NVTLGLPFIR
310 320 330 340
TSPDHGTAFD IAGKGIARPD SLIAALKLAR TLADTDKKAA AA
Length:342
Mass (Da):35,166
Last modified:October 1, 2001 - v1
Checksum:i3ED2D2188F1D384C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB54237.1.
RefSeqiNP_108092.1. NC_002678.2.

Genome annotation databases

EnsemblBacteriaiBAB54237; BAB54237; BAB54237.
GeneIDi1230744.
KEGGimlo:mll7861.
PATRICi22486837. VBIMesLot2464_6295.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000012 Genomic DNA. Translation: BAB54237.1 .
RefSeqi NP_108092.1. NC_002678.2.

3D structure databases

ProteinModelPortali Q984S6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266835.mll7861.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB54237 ; BAB54237 ; BAB54237 .
GeneIDi 1230744.
KEGGi mlo:mll7861.
PATRICi 22486837. VBIMesLot2464_6295.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci MLOT266835:GJ9L-6244-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: MAFF303099.

Entry informationi

Entry nameiPDXA_RHILO
AccessioniPrimary (citable) accession number: Q984S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2001
Last modified: November 26, 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.UniRule annotation

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