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Q2N8X0

- PDXA_ERYLH

UniProt

Q2N8X0 - PDXA_ERYLH

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene
pdxA, ELI_08895
Organism
Erythrobacter litoralis (strain HTCC2594)
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 sitei140 – 1401Substrate By similarity
Metal bindingi171 – 1711Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi216 – 2161Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi271 – 2711Divalent metal cation; shared with dimeric partner By similarity
Binding sitei279 – 2791Substrate By similarity
Binding sitei288 – 2881Substrate By similarity
Binding sitei297 – 2971Substrate By similarity

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

BioCyciELIT314225:GHLE-1812-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:ELI_08895
OrganismiErythrobacter litoralis (strain HTCC2594)
Taxonomic identifieri314225 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesErythrobacteraceaeErythrobacter
ProteomesiUP000008808: 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 – 3363364-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotationPRO_1000051500Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi314225.ELI_08895.

Structurei

3D structure databases

ProteinModelPortaliQ2N8X0.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

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.

Q2N8X0-1 [UniParc]FASTAAdd to Basket

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MGEPQRPLAV SLGDPAGIGP EIIVHAWRMR DSANLAPFAV AGGANVLRSA    50
TEALGVPCPI QEIDDIAEAN SAFLEALPVI KGLDGAYLPG APDPIGAKLA 100
LKSLEMATRL ATAGHASGVV TAPIAKGLLE QVGFTHPGQT EFLAAACGLP 150
EDASVMMLAG PSLRAVPLTV HCPLAEVPGL LSIGLIVERG RIVASALQRD 200
FGIERPRLAV TGLNPHAGED GKFGNEEQDV IAPAIAELLA DGITATGPHP 250
ADALFSPHSR AGFDAALCMY HDQALIPVKA LDFDQGVNVT LGLPIVRTSP 300
DHGTAFDIAG RGTAHPGAMV FALLMAGECA ARRADA 336
Length:336
Mass (Da):34,465
Last modified:February 7, 2006 - v1
Checksum:i213B605C1BF17B80
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000157 Genomic DNA. Translation: ABC63871.1.
RefSeqiWP_011414701.1. NC_007722.1.
YP_458668.1. NC_007722.1.

Genome annotation databases

EnsemblBacteriaiABC63871; ABC63871; ELI_08895.
GeneIDi3870181.
KEGGieli:ELI_08895.
PATRICi21860684. VBIEryLit102657_1765.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000157 Genomic DNA. Translation: ABC63871.1 .
RefSeqi WP_011414701.1. NC_007722.1.
YP_458668.1. NC_007722.1.

3D structure databases

ProteinModelPortali Q2N8X0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 314225.ELI_08895.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC63871 ; ABC63871 ; ELI_08895 .
GeneIDi 3870181.
KEGGi eli:ELI_08895.
PATRICi 21860684. VBIEryLit102657_1765.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci ELIT314225:GHLE-1812-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. "Complete genome sequence of Erythrobacter litoralis HTCC2594."
    Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
    J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HTCC2594.

Entry informationi

Entry nameiPDXA_ERYLH
AccessioniPrimary (citable) accession number: Q2N8X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 7, 2006
Last modified: September 3, 2014
This is version 58 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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