Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9PN58

- PDXA_CAMJE

UniProt

Q9PN58 - PDXA_CAMJE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

4-hydroxythreonine-4-phosphate dehydrogenase

Gene

pdxA

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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

Zn2+UniRule annotation, Mg2+UniRule annotation, Co2+UniRule annotationNote: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).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

BioCyciCJEJ192222:GJTS-1211-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:Cj1239
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000000799: 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_0000188802Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ9PN58. 2 interactions.
STRINGi192222.Cj1239.

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Turni11 – 144Combined sources
Helixi15 – 2612Combined sources
Turni27 – 293Combined sources
Beta strandi30 – 356Combined sources
Helixi38 – 4811Combined sources
Beta strandi54 – 629Combined sources
Beta strandi67 – 737Combined sources
Beta strandi75 – 8410Combined sources
Helixi103 – 12119Combined sources
Beta strandi124 – 1307Combined sources
Helixi135 – 1406Combined sources
Helixi148 – 1569Combined sources
Beta strandi161 – 1666Combined sources
Beta strandi169 – 1757Combined sources
Helixi180 – 1823Combined sources
Helixi183 – 1864Combined sources
Helixi189 – 20315Combined sources
Beta strandi206 – 2116Combined sources
Helixi215 – 2184Combined sources
Turni219 – 2224Combined sources
Helixi226 – 24419Combined sources
Helixi248 – 2547Combined sources
Helixi258 – 2669Combined sources
Helixi281 – 2844Combined sources
Helixi287 – 2926Combined sources
Beta strandi295 – 3006Combined sources
Helixi301 – 31111Combined sources
Turni313 – 3153Combined sources
Beta strandi317 – 3259Combined sources
Beta strandi327 – 3293Combined sources
Helixi348 – 35912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TSNX-ray2.63A/B/C/D1-364[»]
ProteinModelPortaliQ9PN58.
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.

Q9PN58-1 [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 ADTAFTKTGL KNCNRLVAMY
310 320 330 340 350
HDLALAPLKA LYFDKSINVS LNLPIIRVSV DHGTAFDKAY KNAKINTKSY
360
FEAAKFAINL HSKA
Length:364
Mass (Da):41,387
Last modified:October 1, 2000 - v1
Checksum:iDDD26465821FFC3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35354.1.
PIRiA81331.
RefSeqiYP_002344630.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL35354; CAL35354; Cj1239.
GeneIDi905530.
KEGGicje:Cj1239.
PATRICi20059438. VBICamJej33762_1221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35354.1 .
PIRi A81331.
RefSeqi YP_002344630.1. NC_002163.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3TSN X-ray 2.63 A/B/C/D 1-364 [» ]
ProteinModelPortali Q9PN58.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9PN58. 2 interactions.
STRINGi 192222.Cj1239.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL35354 ; CAL35354 ; Cj1239 .
GeneIDi 905530.
KEGGi cje:Cj1239.
PATRICi 20059438. VBICamJej33762_1221.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci CJEJ192222:GJTS-1211-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 11168.

Entry informationi

Entry nameiPDXA_CAMJE
AccessioniPrimary (citable) accession number: Q9PN58
Secondary accession number(s): Q0P917
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 88 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3