ID   LIS_THAL4               Reviewed;         644 AA.
AC   N6Z5E2;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Linalool isomerase {ECO:0000303|PubMed:26979141};
DE            EC=5.4.4.8 {ECO:0000269|PubMed:26979141};
DE   AltName: Full=Geraniol isomerase {ECO:0000303|PubMed:26979141};
GN   Name=lis {ECO:0000303|PubMed:26979141};
GN   ORFNames=C666_11245 {ECO:0000312|EMBL:ENO87364.1};
OS   Thauera linaloolentis (strain DSM 12138 / CCUG 41526 / CIP 105981 / IAM
OS   15112 / NBRC 102519 / 47Lol).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=1123367;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12138 / CCUG 41526 / CIP 105981 / IAM 15112 / NBRC 102519 /
RC   47Lol;
RA   Liu B., Shapleigh J.P., Frostegard A.H.;
RT   "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=DSM 12138 / CCUG 41526 / CIP 105981 / IAM 15112 / NBRC 102519 /
RC   47Lol;
RX   PubMed=26979141; DOI=10.1186/s12858-016-0062-0;
RA   Marmulla R., Safaric B., Markert S., Schweder T., Harder J.;
RT   "Linalool isomerase, a membrane-anchored enzyme in the anaerobic
RT   monoterpene degradation in Thauera linaloolentis 47Lol.";
RL   BMC Biochem. 17:6-6(2016).
CC   -!- FUNCTION: Involved in linalool degradation. Catalyzes the reversible
CC       isomerization of linalool to geraniol. Does not show stereospecificity
CC       towards linalool isomers and acts equally well on both (R) and (S)-
CC       linalool. Cannot use the monoterpenoids citronellol and nerol as
CC       substrates. {ECO:0000269|PubMed:26979141}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=linalool = (2E)-geraniol; Xref=Rhea:RHEA:54656,
CC         ChEBI:CHEBI:17447, ChEBI:CHEBI:17580; EC=5.4.4.8;
CC         Evidence={ECO:0000269|PubMed:26979141};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54657;
CC         Evidence={ECO:0000269|PubMed:26979141};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=455 uM for geraniol {ECO:0000269|PubMed:26979141};
CC         Vmax=3.42 nmol/sec/mg enzyme for the geraniol isomerization reaction
CC         {ECO:0000269|PubMed:26979141};
CC       pH dependence:
CC         Optimum pH is around 8.0. {ECO:0000269|PubMed:26979141};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius.
CC         {ECO:0000269|PubMed:26979141};
CC   -!- PATHWAY: Terpene metabolism; monoterpene degradation.
CC       {ECO:0000269|PubMed:26979141}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:26979141}; Multi-pass membrane protein
CC       {ECO:0000255}.
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DR   EMBL; AMXE01000039; ENO87364.1; -; Genomic_DNA.
DR   EnsemblBacteria; ENO87364; ENO87364; C666_11245.
DR   KEGG; ag:ENO87364; -.
DR   eggNOG; ENOG502Z8JJ; Bacteria.
DR   BRENDA; 5.4.4.8; 15349.
DR   UniPathway; UPA00137; -.
DR   Proteomes; UP000013232; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR041411; Ldi.
DR   Pfam; PF18566; Ldi; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Isomerase; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..644
FT                   /note="Linalool isomerase"
FT                   /id="PRO_0000455105"
FT   TRANSMEM        30..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..644
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:26979141"
SQ   SEQUENCE   644 AA;  71826 MW;  A74B48D8A5F4CE9C CRC64;
     MESTRMLRQP IQLLQGHKGP VTASRHRRNA VVYALLCLLA LLPVATGQSA AWQAAGLGLF
     MPGAGFLALG GAWALLFPLT VFVFWLAVIA WFWSGMVVAP LTLWLGTAAL AGWLAGEAIW
     PPAVYLAPAA AAATFLFFQY RGAKRRAKDR EHFKFRQSFF AESLAEVHQR AATEPEPGER
     ELTPDQLQGV RYLLELALQP VGQYKGYTII DQFQPAALRY QLNHIGFALG MVQGHYTPNF
     QGYLGQAQRN VIDTYRERKV WGYWVYESMW GHFNFSDFDP ARKDNIMLTG WYGMHVGQYM
     LNAGDTRYSQ PGSLSFRLND KTCYHHDIHS INQSVRENFQ SSDFCLYPCE PNWVYPVCNM
     YGMSSLAVYD TLFERRDTAQ VLPKWLHMLD TEFTDQKGSL VGLRSYWTGL EMPFYTGEAG
     FAFFANIFST DLARKLWAVG RKELSMCLTQ DAEGQTRLTL PKEALAFFDT IDAGNYRPGK
     LFAYVAVQMC AREFGDDELA EAARRSMDQD CGPVVENGVA RYTKGSTLAN IWGVEGRLMR
     TGDFRNSFVK GPPSSVFDGP LLGDARYPEI LVAKAFSRGD DLELVLYPGA GDGPQTLGFE
     RLKPGVRYVV EGAASGEFTA DADGRASLAV TLSGRTALHI KPGH