PHEC_PSEAE
ID PHEC_PSEAE Reviewed; 268 AA.
AC Q01269; Q9HYD3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cyclohexadienyl dehydratase;
DE Includes:
DE RecName: Full=Prephenate dehydratase;
DE EC=4.2.1.51;
DE Includes:
DE RecName: Full=Arogenate dehydratase;
DE EC=4.2.1.91;
DE Flags: Precursor;
GN Name=pheC; OrderedLocusNames=PA3475;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=1733946; DOI=10.1016/s0021-9258(18)45905-4;
RA Zhao G., Xia T.H., Fischer R.S., Jensen R.A.;
RT "Cyclohexadienyl dehydratase from Pseudomonas aeruginosa. Molecular cloning
RT of the gene and characterization of the gene product.";
RL J. Biol. Chem. 267:2487-2493(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP PROTEIN SEQUENCE OF 26-36, AND SUBCELLULAR LOCATION.
RX PubMed=8515238; DOI=10.1099/00221287-139-4-807;
RA Zhao G., Xia T., Aldrich H., Jensen R.A.;
RT "Cyclohexadienyl dehydratase from Pseudomonas aeruginosa is a periplasmic
RT protein.";
RL J. Gen. Microbiol. 139:807-813(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RC STRAIN=DSM 2659 / PG201;
RX PubMed=7604006; DOI=10.1073/pnas.92.14.6424;
RA Ochsner U.A., Reiser J.;
RT "Autoinducer-mediated regulation of rhamnolipid biosurfactant synthesis in
RT Pseudomonas aeruginosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6424-6428(1995).
CC -!- FUNCTION: Forms alternative pathway for phenylalanine biosynthesis. Can
CC catalyze two reactions: prephenate dehydratase and arogenate
CC dehydratase. May have a role in chemotaxis or transport.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-arogenate = CO2 + H2O + L-phenylalanine;
CC Xref=Rhea:RHEA:12536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58095, ChEBI:CHEBI:58180; EC=4.2.1.91;
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC phenylalanine from L-arogenate: step 1/1.
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8515238}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
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DR EMBL; AF054868; AAC08596.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06863.1; -; Genomic_DNA.
DR PIR; B42325; B42325.
DR PIR; H83211; H83211.
DR RefSeq; NP_252165.1; NC_002516.2.
DR RefSeq; WP_003092003.1; NZ_QZGE01000039.1.
DR PDB; 3KBR; X-ray; 1.66 A; A=26-261.
DR PDB; 5HPQ; X-ray; 2.05 A; A=26-268.
DR PDBsum; 3KBR; -.
DR PDBsum; 5HPQ; -.
DR AlphaFoldDB; Q01269; -.
DR SMR; Q01269; -.
DR STRING; 287.DR97_4446; -.
DR PaxDb; Q01269; -.
DR PRIDE; Q01269; -.
DR DNASU; 878976; -.
DR EnsemblBacteria; AAG06863; AAG06863; PA3475.
DR GeneID; 878976; -.
DR KEGG; pae:PA3475; -.
DR PATRIC; fig|208964.12.peg.3638; -.
DR PseudoCAP; PA3475; -.
DR HOGENOM; CLU_019602_9_0_6; -.
DR InParanoid; Q01269; -.
DR OMA; MQYGEKA; -.
DR PhylomeDB; Q01269; -.
DR BioCyc; MetaCyc:MON-17135; -.
DR BioCyc; PAER208964:G1FZ6-3543-MON; -.
DR BRENDA; 4.2.1.91; 5087.
DR SABIO-RK; Q01269; -.
DR UniPathway; UPA00121; UER00344.
DR UniPathway; UPA00121; UER00345.
DR EvolutionaryTrace; Q01269; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0047769; F:arogenate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01069; PBP2_PheC; 1.
DR InterPro; IPR037298; PheC_PBP2.
DR InterPro; IPR018313; SBP_3_CS.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; Lyase; Multifunctional enzyme; Periplasm;
KW Phenylalanine biosynthesis; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:8515238"
FT CHAIN 26..268
FT /note="Cyclohexadienyl dehydratase"
FT /id="PRO_0000031773"
FT SITE 179
FT /note="Important for catalysis"
FT CONFLICT 42
FT /note="A -> T (in Ref. 1; AAC08596)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="Y -> H (in Ref. 1; AAC08596)"
FT /evidence="ECO:0000305"
FT CONFLICT 123..124
FT /note="DG -> NS (in Ref. 1; AAC08596)"
FT /evidence="ECO:0000305"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3KBR"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5HPQ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3KBR"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3KBR"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3KBR"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3KBR"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3KBR"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:3KBR"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5HPQ"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3KBR"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3KBR"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3KBR"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3KBR"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3KBR"
FT HELIX 231..246
FT /evidence="ECO:0007829|PDB:3KBR"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:3KBR"
SQ SEQUENCE 268 AA; 30448 MW; 74E7AA47473DDF4B CRC64;
MPKSFRHLVQ ALACLALLAS ASLQAQESRL DRILESGVLR VATTGDYKPF SYRTEEGGYA
GFDVDMAQRL AESLGAKLVV VPTSWPNLMR DFADDRFDIA MSGISINLER QRQAYFSIPY
LRDGKTPITL CSEEARFQTL EQIDQPGVTA IVNPGGTNEK FARANLKKAR ILVHPDNVTI
FQQIVDGKAD LMMTDAIEAR LQSRLHPELC AVHPQQPFDF AEKAYLLPRD EAFKRYVDQW
LHIAEQSGLL RQRMEHWLEY RWPTAHGK
