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Protein

Cyclohexadienyl dehydratase

Gene

pheC

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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)DescriptionActionsGraphical viewLength
Sitei179Important for catalysis1

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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3475.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
ChainiPRO_000003177326 – 268Cyclohexadienyl dehydrataseAdd BLAST243

Proteomic databases

PaxDbiQ01269.

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi208964.PA3475.

Structurei

Secondary structure

1268
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 36Combined sources8
Beta strandi38 – 43Combined sources6
Beta strandi45 – 47Combined sources3
Turni48 – 50Combined sources3
Beta strandi51 – 53Combined sources3
Beta strandi59 – 61Combined sources3
Helixi62 – 73Combined sources12
Beta strandi77 – 82Combined sources6
Turni85 – 87Combined sources3
Helixi88 – 93Combined sources6
Beta strandi98 – 100Combined sources3
Helixi108 – 111Combined sources4
Beta strandi120 – 123Combined sources4
Beta strandi125 – 130Combined sources6
Helixi131 – 137Combined sources7
Helixi140 – 143Combined sources4
Beta strandi149 – 152Combined sources4
Helixi157 – 165Combined sources9
Beta strandi167 – 173Combined sources7
Turni177 – 179Combined sources3
Helixi180 – 185Combined sources6
Beta strandi190 – 195Combined sources6
Helixi196 – 205Combined sources10
Beta strandi209 – 211Combined sources3
Beta strandi221 – 223Combined sources3
Helixi231 – 246Combined sources16
Helixi249 – 257Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ01269.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105F87. Bacteria.
ENOG410XX9W. LUCA.
HOGENOMiHOG000253885.
InParanoidiQ01269.
KOiK01713.
OMAiMQYGEKA.
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)DescriptionActionsGraphical viewLength
Sequence conflicti42A → T in AAC08596 (PubMed:1733946).Curated1
Sequence conflicti115Y → H in AAC08596 (PubMed:1733946).Curated1
Sequence conflicti123 – 124DG → NS in AAC08596 (PubMed:1733946).Curated2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KBRX-ray1.66A26-261[»]
ProteinModelPortaliQ01269.
SMRiQ01269.
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.
OMAiMQYGEKA.
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...

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: November 2, 2016
This is version 112 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.