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Protein

Prephenate dehydratase

Gene

pheA

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Prephenate = phenylpyruvate + H2O + CO2.

Pathwayi: L-phenylalanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phenylpyruvate from prephenate.
Proteins known to be involved in this subpathway in this organism are:
  1. Prephenate dehydratase (pheA)
This subpathway is part of the pathway L-phenylalanine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phenylpyruvate from prephenate, the pathway L-phenylalanine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei183 – 1831Essential for activityBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Phenylalanine biosynthesis

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-6417-MONOMER.
UniPathwayiUPA00121; UER00345.

Names & Taxonomyi

Protein namesi
Recommended name:
Prephenate dehydratase (EC:4.2.1.51)
Short name:
PDT
Gene namesi
Name:pheA
Ordered Locus Names:MSMEG_6418, MSMEI_6250
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310Prephenate dehydratasePRO_0000382039Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi246196.MSMEG_6418.

Structurei

3D structure databases

ProteinModelPortaliA0R643.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 190188Prephenate dehydratasePROSITE-ProRule annotationAdd
BLAST
Domaini204 – 28178ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ACT domain.PROSITE-ProRule annotation
Contains 1 prephenate dehydratase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CQC. Bacteria.
COG0077. LUCA.
HOGENOMiHOG000018970.
KOiK04518.
OMAiEEWNITR.
OrthoDBiEOG6WHNT1.

Family and domain databases

InterProiIPR002912. ACT_dom.
IPR008242. Chor_mutase/pphenate_deHydtase.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view]
PIRSFiPIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A0R643-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRIAYLGPE GTFTEAALLQ MVAKGMVPGP AEDAGGFTPV RTDSTPGALS
60 70 80 90 100
AVREGRADYA CVPIENSIDG TVLPTLDSLA AGSPLQIYAE LTLDVAFTIV
110 120 130 140 150
VRPGHDGPVR TVAAFPVAAA QVRHWLAANL RDAEVVPAHS NAAAAHDVAE
160 170 180 190 200
GRADAGVSTR LAAERCGLDI MAADVVDEPN ARTRFVLVGL PGTPPPATGA
210 220 230 240 250
DRTAVVLRLV NEPGALVSAM TEFSIRDIDL TRIESRPTRT ELGTYMFFLD
260 270 280 290 300
CAGHIDDDPV AEALKALHRR CVDVRYLGSW PTESAAGAPP PRLDEATTWL
310
EGLRAGSGGA
Length:310
Mass (Da):32,464
Last modified:January 9, 2007 - v1
Checksum:i05E0E37D5F39C0B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK72631.1.
CP001663 Genomic DNA. Translation: AFP42676.1.
RefSeqiWP_003897827.1. NZ_CP009494.1.
YP_890631.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK72631; ABK72631; MSMEG_6418.
AFP42676; AFP42676; MSMEI_6250.
GeneIDi4534511.
KEGGimsb:LJ00_31725.
msg:MSMEI_6250.
msm:MSMEG_6418.
PATRICi18085063. VBIMycSme59918_6244.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK72631.1.
CP001663 Genomic DNA. Translation: AFP42676.1.
RefSeqiWP_003897827.1. NZ_CP009494.1.
YP_890631.1. NC_008596.1.

3D structure databases

ProteinModelPortaliA0R643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_6418.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK72631; ABK72631; MSMEG_6418.
AFP42676; AFP42676; MSMEI_6250.
GeneIDi4534511.
KEGGimsb:LJ00_31725.
msg:MSMEI_6250.
msm:MSMEG_6418.
PATRICi18085063. VBIMycSme59918_6244.

Phylogenomic databases

eggNOGiENOG4105CQC. Bacteria.
COG0077. LUCA.
HOGENOMiHOG000018970.
KOiK04518.
OMAiEEWNITR.
OrthoDBiEOG6WHNT1.

Enzyme and pathway databases

UniPathwayiUPA00121; UER00345.
BioCyciMSME246196:GJ4Y-6417-MONOMER.

Family and domain databases

InterProiIPR002912. ACT_dom.
IPR008242. Chor_mutase/pphenate_deHydtase.
IPR001086. Preph_deHydtase.
IPR018528. Preph_deHydtase_CS.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF00800. PDT. 1 hit.
[Graphical view]
PIRSFiPIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS00858. PREPHENATE_DEHYDR_2. 1 hit.
PS51171. PREPHENATE_DEHYDR_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.

Entry informationi

Entry nameiPHEA_MYCS2
AccessioniPrimary (citable) accession number: A0R643
Secondary accession number(s): I7GFR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: January 9, 2007
Last modified: December 9, 2015
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.