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Protein

Cyclohexadienyl dehydratase

Gene

pheC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Forms alternative pathway for phenylalanine biosynthesis. Can catalyze two reactions: prephenate dehydratase and arogenate dehydratase. May have a role in chemotaxis or transport.

Catalytic activityi

Prephenate = phenylpyruvate + H2O + CO2.
L-arogenate = L-phenylalanine + H2O + CO2.

Pathwayi: L-phenylalanine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-phenylalanine from L-arogenate.
Proteins known to be involved in this subpathway in this organism are:
  1. Cyclohexadienyl dehydratase (pheC)
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 L-phenylalanine from L-arogenate, the pathway L-phenylalanine biosynthesis and in Amino-acid biosynthesis.

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. Cyclohexadienyl dehydratase (pheC), P-protein (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
Sitei179 – 1791Important for catalysis

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

BioCyciMetaCyc:MONOMER-17135.
BRENDAi4.2.1.91. 5087.
SABIO-RKQ01269.
UniPathwayiUPA00121; UER00344.
UPA00121; UER00345.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclohexadienyl dehydratase
Including the following 2 domains:
Prephenate dehydratase (EC:4.2.1.51)
Arogenate dehydratase (EC:4.2.1.91)
Gene namesi
Name:pheC
Ordered Locus Names:PA3475
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3475.

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 268243Cyclohexadienyl dehydratasePRO_0000031773Add
BLAST

Proteomic databases

PaxDbiQ01269.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi208964.PA3475.

Structurei

Secondary structure

1
268
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 368Combined sources
Beta strandi38 – 436Combined sources
Beta strandi45 – 473Combined sources
Turni48 – 503Combined sources
Beta strandi51 – 533Combined sources
Beta strandi59 – 613Combined sources
Helixi62 – 7312Combined sources
Beta strandi77 – 826Combined sources
Turni85 – 873Combined sources
Helixi88 – 936Combined sources
Beta strandi98 – 1003Combined sources
Helixi108 – 1114Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi125 – 1306Combined sources
Helixi131 – 1377Combined sources
Helixi140 – 1434Combined sources
Beta strandi149 – 1524Combined sources
Helixi157 – 1659Combined sources
Beta strandi167 – 1737Combined sources
Turni177 – 1793Combined sources
Helixi180 – 1856Combined sources
Beta strandi190 – 1956Combined sources
Helixi196 – 20510Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi221 – 2233Combined sources
Helixi231 – 24616Combined sources
Helixi249 – 2579Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KBRX-ray1.66A26-261[»]
ProteinModelPortaliQ01269.
SMRiQ01269. Positions 27-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01269.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105F87. Bacteria.
ENOG410XX9W. LUCA.
HOGENOMiHOG000253885.
InParanoidiQ01269.
KOiK01713.
OMAiDKKADVM.
OrthoDBiEOG6JQH58.
PhylomeDBiQ01269.

Family and domain databases

InterProiIPR018313. SBP_3_CS.
IPR001638. Solute-binding_3/MltF_N.
[Graphical view]
PfamiPF00497. SBP_bac_3. 1 hit.
[Graphical view]
SMARTiSM00062. PBPb. 1 hit.
[Graphical view]
PROSITEiPS01039. SBP_BACTERIAL_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01269-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKSFRHLVQ ALACLALLAS ASLQAQESRL DRILESGVLR VATTGDYKPF
60 70 80 90 100
SYRTEEGGYA GFDVDMAQRL AESLGAKLVV VPTSWPNLMR DFADDRFDIA
110 120 130 140 150
MSGISINLER QRQAYFSIPY LRDGKTPITL CSEEARFQTL EQIDQPGVTA
160 170 180 190 200
IVNPGGTNEK FARANLKKAR ILVHPDNVTI FQQIVDGKAD LMMTDAIEAR
210 220 230 240 250
LQSRLHPELC AVHPQQPFDF AEKAYLLPRD EAFKRYVDQW LHIAEQSGLL
260
RQRMEHWLEY RWPTAHGK
Length:268
Mass (Da):30,448
Last modified:January 11, 2001 - v2
Checksum:i74E7AA47473DDF4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421A → T in AAC08596 (PubMed:1733946).Curated
Sequence conflicti115 – 1151Y → H in AAC08596 (PubMed:1733946).Curated
Sequence conflicti123 – 1242DG → NS in AAC08596 (PubMed:1733946).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054868 Genomic DNA. Translation: AAC08596.1.
AE004091 Genomic DNA. Translation: AAG06863.1.
PIRiB42325.
H83211.
RefSeqiNP_252165.1. NC_002516.2.
WP_003092003.1. NZ_ASJY01000565.1.

Genome annotation databases

EnsemblBacteriaiAAG06863; AAG06863; PA3475.
GeneIDi878976.
KEGGipae:PA3475.
PATRICi19841561. VBIPseAer58763_3638.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054868 Genomic DNA. Translation: AAC08596.1.
AE004091 Genomic DNA. Translation: AAG06863.1.
PIRiB42325.
H83211.
RefSeqiNP_252165.1. NC_002516.2.
WP_003092003.1. NZ_ASJY01000565.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KBRX-ray1.66A26-261[»]
ProteinModelPortaliQ01269.
SMRiQ01269. Positions 27-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3475.

Proteomic databases

PaxDbiQ01269.

Protocols and materials databases

DNASUi878976.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG06863; AAG06863; PA3475.
GeneIDi878976.
KEGGipae:PA3475.
PATRICi19841561. VBIPseAer58763_3638.

Organism-specific databases

PseudoCAPiPA3475.

Phylogenomic databases

eggNOGiENOG4105F87. Bacteria.
ENOG410XX9W. LUCA.
HOGENOMiHOG000253885.
InParanoidiQ01269.
KOiK01713.
OMAiDKKADVM.
OrthoDBiEOG6JQH58.
PhylomeDBiQ01269.

Enzyme and pathway databases

UniPathwayiUPA00121; UER00344.
UPA00121; UER00345.
BioCyciMetaCyc:MONOMER-17135.
BRENDAi4.2.1.91. 5087.
SABIO-RKQ01269.

Miscellaneous databases

EvolutionaryTraceiQ01269.

Family and domain databases

InterProiIPR018313. SBP_3_CS.
IPR001638. Solute-binding_3/MltF_N.
[Graphical view]
PfamiPF00497. SBP_bac_3. 1 hit.
[Graphical view]
SMARTiSM00062. PBPb. 1 hit.
[Graphical view]
PROSITEiPS01039. SBP_BACTERIAL_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cyclohexadienyl dehydratase from Pseudomonas aeruginosa. Molecular cloning of the gene and characterization of the gene product."
    Zhao G., Xia T.H., Fischer R.S., Jensen R.A.
    J. Biol. Chem. 267:2487-2493(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  3. "Cyclohexadienyl dehydratase from Pseudomonas aeruginosa is a periplasmic protein."
    Zhao G., Xia T., Aldrich H., Jensen R.A.
    J. Gen. Microbiol. 139:807-813(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-36, SUBCELLULAR LOCATION.
  4. "Autoinducer-mediated regulation of rhamnolipid biosurfactant synthesis in Pseudomonas aeruginosa."
    Ochsner U.A., Reiser J.
    Proc. Natl. Acad. Sci. U.S.A. 92:6424-6428(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
    Strain: DSM 2659 / PG201.

Entry informationi

Entry nameiPHEC_PSEAE
AccessioniPrimary (citable) accession number: Q01269
Secondary accession number(s): Q9HYD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 11, 2001
Last modified: December 9, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, 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

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.