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Q1GI38

- PDXA_RUEST

UniProt

Q1GI38 - PDXA_RUEST

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Protein
4-hydroxythreonine-4-phosphate dehydrogenase
Gene
pdxA, TM1040_0945
Organism
Ruegeria sp. (strain TM1040) (Silicibacter sp.)
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 sitei132 – 1321Substrate By similarity
Binding sitei133 – 1331Substrate By similarity
Metal bindingi162 – 1621Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi207 – 2071Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi262 – 2621Divalent metal cation; shared with dimeric partner By similarity
Binding sitei270 – 2701Substrate By similarity
Binding sitei279 – 2791Substrate By similarity
Binding sitei288 – 2881Substrate 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

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

BioCyciRSP292414:GHCT-962-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:TM1040_0945
OrganismiRuegeria sp. (strain TM1040) (Silicibacter sp.)
Taxonomic identifieri292414 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria
ProteomesiUP000000636: 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 – 3263264-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotation
PRO_1000051519Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi292414.TM1040_0945.

Structurei

3D structure databases

ProteinModelPortaliQ1GI38.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221592.
KOiK00097.
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.

Q1GI38-1 [UniParc]FASTAAdd to Basket

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MTGAPQVIAL SCGEPAGIGP EIAVAAWDQL RADCPFVWIG DPRHLPSSHP    50
WQPVSAPAEA LQVSADALPV WPLEFAGNTT KGEADPQNAS GVIQSIKTGV 100
ELVTSGKAAA LCTAPIHKKA LIDGAGFAYP GHTEFLAALG GVDHVVMMLA 150
SAALRVVPAT IHIPLSAVPE VLTPDHLRRV ITLTDRGLRD QFGLTAPRIA 200
VTGLNPHAGE GGAMGQEEGD WIEALIREMQ TEGYRLTGPH PADTLFHAAA 250
RARYDAAIAM YHDQALIPIK TLDFDKGVNV TLGLPFIRTS PDHGTAFDIA 300
GKGLANPSSL IEALRLAQTM AKTRQP 326
Length:326
Mass (Da):34,339
Last modified:June 27, 2006 - v1
Checksum:i85584BAFB9B8E179
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000377 Genomic DNA. Translation: ABF63678.1.
RefSeqiWP_011538288.1. NC_008044.1.
YP_612940.1. NC_008044.1.

Genome annotation databases

EnsemblBacteriaiABF63678; ABF63678; TM1040_0945.
GeneIDi4077339.
KEGGisit:TM1040_0945.
PATRICi23386010. VBIRueSp69653_1831.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000377 Genomic DNA. Translation: ABF63678.1 .
RefSeqi WP_011538288.1. NC_008044.1.
YP_612940.1. NC_008044.1.

3D structure databases

ProteinModelPortali Q1GI38.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 292414.TM1040_0945.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF63678 ; ABF63678 ; TM1040_0945 .
GeneIDi 4077339.
KEGGi sit:TM1040_0945.
PATRICi 23386010. VBIRueSp69653_1831.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci RSP292414:GHCT-962-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: TM1040.

Entry informationi

Entry nameiPDXA_RUEST
AccessioniPrimary (citable) accession number: Q1GI38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 27, 2006
Last modified: September 3, 2014
This is version 67 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

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