LDI_CASDE
ID LDI_CASDE Reviewed; 397 AA.
AC E1XUJ2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Linalool dehydratase/isomerase;
DE EC=4.2.1.127 {ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:21950166};
DE EC=5.4.4.4 {ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:21950166};
DE AltName: Full=Geraniol isomerase;
DE AltName: Full=Linalool dehydratase-isomerase {ECO:0000303|PubMed:20663876};
DE AltName: Full=Myrcene hydratase;
DE Flags: Precursor;
GN Name=ldi;
OS Castellaniella defragrans (Alcaligenes defragrans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Castellaniella.
OX NCBI_TaxID=75697;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=DSM 12143 / 65Phen;
RX PubMed=22286981; DOI=10.1128/aem.07226-11;
RA Luddeke F., Wulfing A., Timke M., Germer F., Weber J., Dikfidan A.,
RA Rahnfeld T., Linder D., Meyerdierks A., Harder J.;
RT "Geraniol and geranial dehydrogenases induced in anaerobic monoterpene
RT degradation by Castellaniella defragrans.";
RL Appl. Environ. Microbiol. 78:2128-2136(2012).
RN [2]
RP PROTEIN SEQUENCE OF 27-38, FUNCTION, CATALYTIC ACTIVITY, REVERSIBILITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP SUBCELLULAR LOCATION, PATHWAY, INDUCTION, AND SUBUNIT.
RC STRAIN=DSM 12143 / 65Phen;
RX PubMed=20663876; DOI=10.1074/jbc.m109.084244;
RA Brodkorb D., Gottschall M., Marmulla R., Luddeke F., Harder J.;
RT "Linalool dehydratase-isomerase, a bifunctional enzyme in the anaerobic
RT degradation of monoterpenes.";
RL J. Biol. Chem. 285:30436-30442(2010).
RN [3]
RP CATALYTIC ACTIVITY, AND REACTION STEREOSPECIFICITY.
RC STRAIN=DSM 12143 / 65Phen;
RX PubMed=21950166; DOI=10.1515/znc-2011-7-813;
RA Luddeke F., Harder J.;
RT "Enantiospecific (S)-(+)-linalool formation from beta-myrcene by linalool
RT dehydratase-isomerase.";
RL Z. Naturforsch. C Biosci. 66:409-412(2011).
CC -!- FUNCTION: Anaerobically catalyzes the stereospecific hydration of beta-
CC myrcene to (3S)-linalool and the isomerization of (3S)-linalool to
CC geraniol. Is thus involved in the initial steps of the anaerobic
CC degradation of the monoterpene beta-myrcene. Also catalyzes the reverse
CC reactions, i.e. the isomerization of geraniol to linalool and the
CC dehydration of linalool to myrcene. In this direction, the formation of
CC myrcene from geraniol may be seen as a detoxification process for the
CC monoterpene alcohol. Neither the monoterpenes alpha- and beta-ocimene
CC nor the monoterpenoids citronellol and nerol can be used as substrates.
CC {ECO:0000269|PubMed:20663876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-linalool = beta-myrcene + H2O; Xref=Rhea:RHEA:30711,
CC ChEBI:CHEBI:98, ChEBI:CHEBI:15377, ChEBI:CHEBI:17221; EC=4.2.1.127;
CC Evidence={ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:21950166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geraniol = (S)-linalool; Xref=Rhea:RHEA:30715,
CC ChEBI:CHEBI:98, ChEBI:CHEBI:17447; EC=5.4.4.4;
CC Evidence={ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:21950166};
CC -!- ACTIVITY REGULATION: Is inhibited by molecular oxygen, high salt
CC concentrations (NaCl, KCl, or MgCl(2)), urea, and Ti(III)citrate.
CC Activity is not affected by EDTA. {ECO:0000269|PubMed:20663876}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=750 uM for linalool {ECO:0000269|PubMed:20663876};
CC KM=500 uM for geraniol {ECO:0000269|PubMed:20663876};
CC Vmax=140 nmol/sec/mg enzyme for the linalool dehydration reaction
CC {ECO:0000269|PubMed:20663876};
CC Vmax=410 nmol/sec/mg enzyme for the geraniol isomerization reaction
CC {ECO:0000269|PubMed:20663876};
CC pH dependence:
CC Optimum pH is 9.0 for the linalool dehydratase activity.
CC {ECO:0000269|PubMed:20663876};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius for the linalool
CC dehydratase activity. {ECO:0000269|PubMed:20663876};
CC -!- PATHWAY: Terpene metabolism; monoterpene degradation.
CC {ECO:0000269|PubMed:20663876, ECO:0000269|PubMed:22286981}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20663876}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:20663876}.
CC -!- INDUCTION: By monoterpenes such as limonene and myrcene, but not by
CC acetate. {ECO:0000269|PubMed:20663876}.
CC -!- MISCELLANEOUS: Requires DTT as a reducing agent for activity in vitro.
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DR EMBL; FR669447; CBW30776.1; -; Genomic_DNA.
DR PDB; 5G1U; X-ray; 2.57 A; A/B/C/D/E=27-397.
DR PDB; 5G1V; X-ray; 2.68 A; A/B/C/D/E=27-397.
DR PDB; 5G1W; X-ray; 1.76 A; A/B/C/D/E=27-397.
DR PDB; 5HLR; X-ray; 1.91 A; A/B/C/D/E=27-397.
DR PDB; 5HSS; X-ray; 2.50 A; A/B/C/D/E=27-397.
DR PDB; 5I3T; X-ray; 2.10 A; A/B/C/D/E=1-397.
DR PDB; 7AD2; X-ray; 1.83 A; A/B/C/D/E=27-397.
DR PDBsum; 5G1U; -.
DR PDBsum; 5G1V; -.
DR PDBsum; 5G1W; -.
DR PDBsum; 5HLR; -.
DR PDBsum; 5HSS; -.
DR PDBsum; 5I3T; -.
DR PDBsum; 7AD2; -.
DR AlphaFoldDB; E1XUJ2; -.
DR SMR; E1XUJ2; -.
DR MINT; E1XUJ2; -.
DR BioCyc; MetaCyc:MON-16530; -.
DR BRENDA; 4.2.1.127; 229.
DR BRENDA; 5.4.4.4; 229.
DR UniPathway; UPA00137; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0050486; F:intramolecular transferase activity, transferring hydroxy groups; IDA:UniProtKB.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:UniProtKB.
DR GO; GO:0043694; P:monoterpene catabolic process; IDA:UniProtKB.
DR GO; GO:0016098; P:monoterpenoid metabolic process; IDA:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR InterPro; IPR041411; Ldi.
DR Pfam; PF18566; Ldi; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Lyase; Periplasm;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:20663876"
FT CHAIN 27..397
FT /note="Linalool dehydratase/isomerase"
FT /id="PRO_0000418647"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:5G1W"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5G1W"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:5G1W"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 149..166
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 172..188
FT /evidence="ECO:0007829|PDB:5G1W"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 203..220
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:5G1W"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:5G1W"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:5G1W"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:5G1W"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:5G1W"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:5G1W"
FT TURN 298..301
FT /evidence="ECO:0007829|PDB:5G1W"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:5G1W"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:5G1W"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:5G1W"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 368..377
FT /evidence="ECO:0007829|PDB:5G1W"
FT HELIX 381..385
FT /evidence="ECO:0007829|PDB:5G1W"
SQ SEQUENCE 397 AA; 44454 MW; 63333B1579883BE7 CRC64;
MRFTLKTTAI VSAAALLAGF GPPPRAAELP PGRLATTEDY FAQQAKQAVT PDVMAQLAYM
NYIDFISPFY SRGCSFEAWE LKHTPQRVIK YSIAFYAYGL ASVALIDPKL RALAGHDLDI
AVSKMKCKRV WGDWEEDGFG TDPIEKENIM YKGHLNLMYG LYQLVTGSRR YEAEHAHLTR
IIHDEIAANP FAGIVCEPDN YFVQCNSVAY LSLWVYDRLH GTDYRAATRA WLDFIQKDLI
DPERGAFYLS YHPESGAVKP WISAYTTAWT LAMVHGMDPA FSERYYPRFK QTFVEVYDEG
RKARVRETAG TDDADGGVGL ASAFTLLLAR EMGDQQLFDQ LLNHLEPPAK PSIVSASLRY
EHPGSLLFDE LLFLAKVHAG FGALLRMPPP AAKLAGK
