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Q9ZHY3 (PHEA_NEIG1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
P-protein

Including the following 2 domains:

  1. Chorismate mutase
    Short name=CM
    EC=5.4.99.5
  2. Prephenate dehydratase
    Short name=PDT
    EC=4.2.1.51
Gene names
Name:pheA
Ordered Locus Names:NGO1510
OrganismNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Taxonomic identifier242231 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existencePredicted

General annotation (Comments)

Catalytic activity

Chorismate = prephenate.

Prephenate = phenylpyruvate + H2O + CO2.

Pathway

Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.

Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.

Subcellular location

Cytoplasm.

Sequence similarities

Contains 1 ACT domain.

Contains 1 chorismate mutase domain.

Contains 1 prephenate dehydratase domain.

Sequence caution

The sequence AAD05425.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAW90148.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362P-protein
PRO_0000119189

Regions

Domain3 – 9189Chorismate mutase
Domain92 – 269178Prephenate dehydratase
Domain280 – 35677ACT
Region270 – 36293Regulatory (Phe-binding)

Sites

Site2621Essential for prephenate dehydratase activity Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZHY3 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: BEC6582338E84DE2

FASTA36239,354
        10         20         30         40         50         60 
MSQTIDELLI PHRNAIDTID AEILRLLNER AQHAHAIGEL KGTGAVYRPE REVAVLRRIQ 

        70         80         90        100        110        120 
DLNKGPLPDE SVARLFREVM SECLAVERPL TIAYLGPQGT FTQQAAIKHF GHAAHTMACP 

       130        140        150        160        170        180 
TIDDCFKQVE TRQADYLVAP VENSTEGSVG RTLDLLAVTA LQACGEVVLR IHHNLLRKNN 

       190        200        210        220        230        240 
GSTEGIAKVF SHAQALAQCN DWLGRRLPNA ERIAVSSNAE AARLVAESDD GTVAAIAGRT 

       250        260        270        280        290        300 
AAEIYGLDMV AECIEDEPNN TTRFLVMGHH ETGASGSDKT SLAVSAPNRA GAVASLLQPL 

       310        320        330        340        350        360 
TESGISMTKF ESRPSKSVLW EYLFFIDIEG HRRDAQIQTA LERLGERASF VKAIGSYPTA 


VL 

« Hide

References

« Hide 'large scale' references
[1]"Differential roles of homologous recombination pathways in Neisseria gonorrhoeae pilin antigenic variation, DNA transformation and DNA repair."
Mehr I.J., Seifert H.S.
Mol. Microbiol. 30:697-710(1998) [PubMed: 10094619] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of Neisseria gonorrhoeae."
Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H. expand/collapse author list , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700825 / FA 1090.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF047375 Genomic DNA. Translation: AAD05425.1. Different initiation.
AE004969 Genomic DNA. Translation: AAW90148.1. Different initiation.
RefSeqYP_208560.1. NC_002946.2.

3D structure databases

ProteinModelPortalQ9ZHY3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9ZHY3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000002795; EBNEIP00000002636; EBNEIG00000002795.
GeneID3281542.
GenomeReviewsGene locus NGO1510 in contig AE004969_GR.
KEGGngo:NGO1510.
NMPDRfig|242231.4.peg.1527.
PATRIC20336494. VBINeiGon24812_1795.

Phylogenomic databases

eggNOGCOG0077.
GeneTreeEBGT00050000020499.
HOGENOMHBG693866.
PhylomeDBQ9ZHY3.
ProtClustDBCLSK877559.

Enzyme and pathway databases

BioCycNGON242231:NGO1510-MONOMER.

Family and domain databases

InterProIPR002912. ACT-bd.
IPR008242. Chor_mutase/pphenate_deHydtase.
IPR002701. Chorismate_mutase.
IPR020822. Chorismate_mutase_type_II.
IPR010957. G/b/e-P-prot_chorismate_mutase.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
Gene3DG3DSA:1.20.59.10. Chorismate_mutase. 1 hit.
KOK14170.
PfamPF01842. ACT. 1 hit.
PF01817. CM_2. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view]
PIRSFPIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
SMARTSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMSSF48600. Chorismate_mut. 1 hit.
TIGRFAMsTIGR01807. CM_P2. 1 hit.
PROSITEPS51168. CHORISMATE_MUT_2. 1 hit.
PS00857. PREPHENATE_DEHYDR_1. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHEA_NEIG1
AccessionPrimary (citable) accession number: Q9ZHY3
Secondary accession number(s): Q5F6N9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: January 25, 2012
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families