Skip Header

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

A8FMU4

- PDXA_CAMJ8

UniProt

A8FMU4 - PDXA_CAMJ8

(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:6 (strain 81116 / NCTC 11828)
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

BioCyciCJEJ407148:GHCS-1218-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:C8J_1182
OrganismiCampylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)
Taxonomic identifieri407148 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000002013: 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_1000072540Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi407148.C8J_1182.

Structurei

3D structure databases

ProteinModelPortaliA8FMU4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PdxA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1995.
HOGENOMiHOG000221591.
KOiK00097.
OMAiAIGTEDE.
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.

A8FMU4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKLAISIGD INGIGLEILV RSHEELSKIC TPFYFIHENL LNKASKLLNL
60 70 80 90 100
KLFNAKIVAF KDDKDYEFNF IKKENSLEIY SFCLPLGFKV DENFEIKAGE
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
KETHFKKIGL 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 SLKT
Length:364
Mass (Da):41,315
Last modified:November 13, 2007 - v1
Checksum:iC399C46022E70AF7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000814 Genomic DNA. Translation: ABV52781.1.
RefSeqiYP_001482758.1. NC_009839.1.

Genome annotation databases

EnsemblBacteriaiABV52781; ABV52781; C8J_1182.
GeneIDi5618490.
KEGGicju:C8J_1182.
PATRICi20055998. VBICamJej119085_1192.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000814 Genomic DNA. Translation: ABV52781.1 .
RefSeqi YP_001482758.1. NC_009839.1.

3D structure databases

ProteinModelPortali A8FMU4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 407148.C8J_1182.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV52781 ; ABV52781 ; C8J_1182 .
GeneIDi 5618490.
KEGGi cju:C8J_1182.
PATRICi 20055998. VBICamJej119085_1192.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00244 ; UER00312 .
BioCyci CJEJ407148:GHCS-1218-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. "The complete genome sequence of Campylobacter jejuni strain 81116 (NCTC11828)."
    Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., van Vliet A.H.M.
    J. Bacteriol. 189:8402-8403(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 81116 / NCTC 11828.

Entry informationi

Entry nameiPDXA_CAMJ8
AccessioniPrimary (citable) accession number: A8FMU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: November 13, 2007
Last modified: October 29, 2014
This is version 49 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