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A1W0M2

- PDXA_CAMJJ

UniProt

A1W0M2 - PDXA_CAMJJ

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Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)
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 sitei148 – 1481SubstrateUniRule annotation
Binding sitei149 – 1491SubstrateUniRule annotation
Metal bindingi177 – 1771Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi216 – 2161Divalent metal cation; shared with dimeric partnerUniRule annotation
Metal bindingi301 – 3011Divalent metal cation; shared with dimeric partnerUniRule annotation
Binding sitei309 – 3091SubstrateUniRule annotation
Binding sitei318 – 3181SubstrateUniRule annotation
Binding sitei327 – 3271SubstrateUniRule 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

BioCyciCJEJ354242:GC51-1230-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:CJJ81176_1253
OrganismiCampylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)
Taxonomic identifieri354242 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000000646: 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 – 3643644-hydroxythreonine-4-phosphate dehydrogenasePRO_1000051493Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi354242.CJJ81176_1253.

Structurei

3D structure databases

ProteinModelPortaliA1W0M2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221591.
KOiK00097.
OMAiISIKLAM.
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]

Sequencei

Sequence statusi: Complete.

A1W0M2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKLAISIGD INSIGLEILV RSHEELSKIC TPFYFIHESL LNKALKLLNL
60 70 80 90 100
KLFNAKIVAF KDDKDYEFNF IKKENSLEIY SFCLPLGFKV DENFEIQAGE
110 120 130 140 150
IDAKSGLYGF LSFKAASYFV YEKHAHALLT LPIHKKAWED AGLKYKGHTD
160 170 180 190 200
ALRDFFKKNA IMMLGCKELF VGLFSEHIPL AKVSKKITFK NLSIFLKDFY
210 220 230 240 250
KETHFKKMGL LGFNPHAGDY GVIGGEEEKI MEKAIAFVNA FLHSKKDEKF
260 270 280 290 300
FKKALKDENL QKELLLNFKG KGVYLPYPLV ADTAFTKAGL KNCNRLVAMY
310 320 330 340 350
HDLALAPLKA LYFDKSINVS LNLPIIRVSV DHGTAFDKAY KNAKINTKSY
360
FEAAKFAINL NSKA
Length:364
Mass (Da):41,333
Last modified:February 6, 2007 - v1
Checksum:iC763D460320EFD2E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000538 Genomic DNA. Translation: EAQ72898.1.
RefSeqiYP_001000913.1. NC_008787.1.

Genome annotation databases

EnsemblBacteriaiEAQ72898; EAQ72898; CJJ81176_1253.
GeneIDi4682344.
KEGGicjj:CJJ81176_1253.
PATRICi20052483. VBICamJej103413_1253.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000538 Genomic DNA. Translation: EAQ72898.1 .
RefSeqi YP_001000913.1. NC_008787.1.

3D structure databases

ProteinModelPortali A1W0M2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 354242.CJJ81176_1253.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai EAQ72898 ; EAQ72898 ; CJJ81176_1253 .
GeneIDi 4682344.
KEGGi cjj:CJJ81176_1253.
PATRICi 20052483. VBICamJej103413_1253.

Phylogenomic databases

eggNOGi COG1995.
HOGENOMi HOG000221591.
KOi K00097.
OMAi ISIKLAM.
OrthoDBi EOG6GN6ZC.

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci CJEJ354242:GC51-1230-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 ]
ProtoNeti Search...

Publicationsi

  1. Fouts D.E., Nelson K.E., Sebastian Y.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 81-176.

Entry informationi

Entry nameiPDXA_CAMJJ
AccessioniPrimary (citable) accession number: A1W0M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: October 29, 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.UniRule annotation

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