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Q89NF3

- PDXA1_BRADU

UniProt

Q89NF3 - PDXA1_BRADU

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase 1

Gene

pdxA1

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
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

Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei138 – 1381SubstrateUniRule annotation
Binding sitei139 – 1391SubstrateUniRule annotation
Metal bindingi168 – 1681Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi212 – 2121Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi267 – 2671Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei275 – 2751SubstrateUniRule annotation
Binding sitei295 – 2951SubstrateUniRule annotation
Binding sitei304 – 3041SubstrateUniRule 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

BioCyciBJAP224911:GJEJ-3911-MONOMER.
UniPathwayiUPA00244; UER00312.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenase 1UniRule annotation (EC:1.1.1.262UniRule annotation)
Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase 1UniRule annotation
Gene namesi
Name:pdxA1UniRule annotation
Ordered Locus Names:blr3887
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
ProteomesiUP000002526: 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 – 3453454-hydroxythreonine-4-phosphate dehydrogenase 1PRO_0000188798Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224911.blr3887.

Structurei

3D structure databases

ProteinModelPortaliQ89NF3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221593.
InParanoidiQ89NF3.
KOiK00097.
OrthoDBiEOG6GN6ZC.
PhylomeDBiQ89NF3.

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.

Q89NF3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSRHLAITM GDPAGIGPEI IVKACLGLKG RIATGDLRLL IIGSGAALDG
60 70 80 90 100
AKAALGTDVA IPQVSADDRE WPNLCYLQAD AEGDPIKPGV LSADGGRFAY
110 120 130 140 150
KAIEQGVRLT QAGRTAAIVT APLNKEALNK AGYHFPGHTE MLAHLTGVRG
160 170 180 190 200
SVMLLAHGNM RVSHVSTHVA LEDVPKRLTP ERLRMVIDLT NDALRRLGIA
210 220 230 240 250
KPKIAVAALN PHAGEGGLFG RQDIDVSAPT IAKAVADGLD VIGPVPGDTI
260 270 280 290 300
FVKLRAGQFD AAVAMYHDQG HIPVKLLGFQ VDPATGRWQE LSGVNITLGL
310 320 330 340
PIIRTSVDHG TAFDIAGKGI ANEHSLIEAI DYAERLAAGA SASKS
Length:345
Mass (Da):36,065
Last modified:June 1, 2003 - v1
Checksum:iC67EB244DD7470A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000040 Genomic DNA. Translation: BAC49152.1.
RefSeqiNP_770527.1. NC_004463.1.

Genome annotation databases

EnsemblBacteriaiBAC49152; BAC49152; BAC49152.
GeneIDi1053741.
KEGGibja:blr3887.
PATRICi21191273. VBIBraJap65052_3894.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000040 Genomic DNA. Translation: BAC49152.1 .
RefSeqi NP_770527.1. NC_004463.1.

3D structure databases

ProteinModelPortali Q89NF3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224911.blr3887.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC49152 ; BAC49152 ; BAC49152 .
GeneIDi 1053741.
KEGGi bja:blr3887.
PATRICi 21191273. VBIBraJap65052_3894.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221593.
InParanoidi Q89NF3.
KOi K00097.
OrthoDBi EOG6GN6ZC.
PhylomeDBi Q89NF3.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci BJAP224911:GJEJ-3911-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: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Entry informationi

Entry nameiPDXA1_BRADU
AccessioniPrimary (citable) accession number: Q89NF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 79 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