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A1B0G5

- PDXA_PARDP

UniProt

A1B0G5 - PDXA_PARDP

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Protein
4-hydroxythreonine-4-phosphate dehydrogenase
Gene
pdxA, Pden_0898
Organism
Paracoccus denitrificans (strain Pd 1222)
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 sitei126 – 1261Substrate By similarity
Binding sitei127 – 1271Substrate By similarity
Metal bindingi160 – 1601Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi205 – 2051Divalent metal cation; shared with dimeric partner By similarity
Metal bindingi260 – 2601Divalent metal cation; shared with dimeric partner By similarity
Binding sitei268 – 2681Substrate By similarity
Binding sitei277 – 2771Substrate By similarity
Binding sitei286 – 2861Substrate 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

BioCyciPDEN318586:GCVQ-911-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:Pden_0898
OrganismiParacoccus denitrificans (strain Pd 1222)
Taxonomic identifieri318586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus
ProteomesiUP000000361: Chromosome 1

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 – 3223224-hydroxythreonine-4-phosphate dehydrogenaseUniRule annotation
PRO_1000128256Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi318586.Pden_0898.

Structurei

3D structure databases

ProteinModelPortaliA1B0G5.

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221593.
KOiK00097.
OMAiYSAHRIS.
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.

A1B0G5-1 [UniParc]FASTAAdd to Basket

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MTEARPIILT CGEPAGVGPE LAPKALASGV PFVFLGDPRH LPEGTAWAEV    50
TAPGEPVADG VLAVLRHDFP APARPGQPDP ANAPAVIEVI ARAVDLAMSG 100
AAGGICTLPI NKEALKRGAG FGFPGHTEYL AHLAGDVPVV MMLASTTVQP 150
PCRVVPVTIH IPLSEVPLAL TPLRLEQAIR ITDAAMRRDF GLAQPRLAIA 200
GLNPHAGENG VMGDEEARWM APLIERLRRE GFDLRGPLPA DTMFHPAARA 250
RYDAALCAYH DQALIPIKTL DFAGGVNITL GLPFVRTSPD HGTAFDIAGQ 300
GIADAESVIA ALRMAHEMAA RR 322
Length:322
Mass (Da):33,869
Last modified:January 23, 2007 - v1
Checksum:i60B2EF5329401A54
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000489 Genomic DNA. Translation: ABL69009.1.
RefSeqiWP_011747237.1. NC_008686.1.
YP_914705.1. NC_008686.1.

Genome annotation databases

EnsemblBacteriaiABL69009; ABL69009; Pden_0898.
GeneIDi4578576.
KEGGipde:Pden_0898.
PATRICi22852954. VBIParDen97112_0874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000489 Genomic DNA. Translation: ABL69009.1 .
RefSeqi WP_011747237.1. NC_008686.1.
YP_914705.1. NC_008686.1.

3D structure databases

ProteinModelPortali A1B0G5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 318586.Pden_0898.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL69009 ; ABL69009 ; Pden_0898 .
GeneIDi 4578576.
KEGGi pde:Pden_0898.
PATRICi 22852954. VBIParDen97112_0874.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221593.
KOi K00097.
OMAi YSAHRIS.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci PDEN318586:GCVQ-911-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: Pd 1222.

Entry informationi

Entry nameiPDXA_PARDP
AccessioniPrimary (citable) accession number: A1B0G5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 56 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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