ID   SESA_SINX2              Reviewed;         452 AA.
AC   A0A1J1EM40;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=Sesamin methylene transferase {ECO:0000305};
DE            EC=2.1.5.1 {ECO:0000269|PubMed:27444012};
DE   AltName: Full=Sesamin-metabolizing enzyme {ECO:0000303|PubMed:27444012};
DE   AltName: Full=THF-dependent sesamin/sesamin-monocatechol methylenetransferase {ECO:0000303|PubMed:27444012};
GN   Name=sesA {ECO:0000303|PubMed:27444012};
OS   Sinomonas sp. (strain No.22).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Sinomonas;
OC   unclassified Sinomonas.
OX   NCBI_TaxID=1762963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, AND
RP   MUTAGENESIS OF ASP-95; GLU-189 AND TYR-221.
RC   STRAIN=No.22;
RX   PubMed=27444012; DOI=10.1073/pnas.1605050113;
RA   Kumano T., Fujiki E., Hashimoto Y., Kobayashi M.;
RT   "Discovery of a sesamin-metabolizing microorganism and a new enzyme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9087-9092(2016).
CC   -!- FUNCTION: Converts sesamin into sesamin mono- and di-catechol.
CC       Catalyzes a ring cleavage to transfer the methylene group to
CC       tetrahydrofolate (THF). Also active with (+)-episesamin, (-)-asarinin,
CC       sesaminol, (+)-sesamolin and piperine. {ECO:0000269|PubMed:27444012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(+)-sesamin + (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) =
CC         (+)-sesamin monocatechol + (6R)-5,10-methylenetetrahydrofolyl-(gamma-
CC         L-Glu)(n); Xref=Rhea:RHEA:41011, Rhea:RHEA-COMP:13257, Rhea:RHEA-
CC         COMP:14738, ChEBI:CHEBI:66470, ChEBI:CHEBI:136542,
CC         ChEBI:CHEBI:136572, ChEBI:CHEBI:141005; EC=2.1.5.1;
CC         Evidence={ECO:0000269|PubMed:27444012};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(+)-sesamin monocatechol + (6S)-5,6,7,8-tetrahydrofolyl-
CC         (gamma-L-Glu)(n) = (+)-sesamin dicatechol + (6R)-5,10-
CC         methylenetetrahydrofolyl-(gamma-L-Glu)(n); Xref=Rhea:RHEA:52376,
CC         Rhea:RHEA-COMP:13257, Rhea:RHEA-COMP:14738, ChEBI:CHEBI:136542,
CC         ChEBI:CHEBI:136543, ChEBI:CHEBI:136572, ChEBI:CHEBI:141005;
CC         EC=2.1.5.1; Evidence={ECO:0000269|PubMed:27444012};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.032 mM for sesamin {ECO:0000269|PubMed:27444012};
CC         Vmax=9.3 umol/min/mg enzyme with sesamin as substrate
CC         {ECO:0000269|PubMed:27444012};
CC         Note=kcat is 7.9 sec(-1) with sesamin as substrate.
CC         {ECO:0000269|PubMed:27444012};
CC       pH dependence:
CC         Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:27444012};
CC       Temperature dependence:
CC         Optimum temperature is below 40 degrees Celsius.
CC         {ECO:0000269|PubMed:27444012};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:27444012}.
CC   -!- INDUCTION: Expression is induced in the presence of sesamin.
CC       {ECO:0000269|PubMed:27444012}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
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DR   EMBL; LC101493; BAW03116.1; -; Genomic_DNA.
DR   SMR; A0A1J1EM40; -.
DR   KEGG; ag:BAW03116; -.
DR   BRENDA; 2.1.5.1; 15672.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1360.120; -; 1.
DR   InterPro; IPR028896; GCST/YgfZ/DmdA.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR43757; PTHR43757; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:27444012"
FT   CHAIN           2..452
FT                   /note="Sesamin methylene transferase"
FT                   /id="PRO_0000453263"
FT   MUTAGEN         95
FT                   /note="D->A: 60% decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:27444012"
FT   MUTAGEN         189
FT                   /note="E->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:27444012"
FT   MUTAGEN         221
FT                   /note="Y->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:27444012"
SQ   SEQUENCE   452 AA;  50386 MW;  B0684C1A1056EE5C CRC64;
     MTAEQAINEG AFSLAASFGF VPLEYRGYEA EVLASKETAY IGTALNGAMS PIYDVTGPDA
     LEFLRSVCIN SFRGFQVGQI RHAVLCNDKG QILTDGVVAR IDEDTYRTYW LAPALEYRLI
     NSGLDVKGED QSSNEFFFQL AGPRSLEVLE AAAHEDLHDI AFGRHRMSTI AGIPVRILRL
     GMAGGLAYEV HGAAADTETA YRAIWEAGQP FGLVKQGLNA YLMQHTEAGF PNINLHYPLP
     WYEDPDMAAF FDTRPTQNFY NKYRFFYGSV GPDAEARFVT PYQIGLGKMV DFNHDFIGKE
     ALQREAEADH WAAVTLVWNE DDVADVVASK YRGRDVEPYD KIDDRPFDIY HNLGQPGFAY
     HADWVLADGE RIGTSTGRIN SVYYRRMISL GFIDKRHAAE GTELTVLWGR PGTPQKEIRV
     TVGRYPYFDL EKNNAIDVAS IPRPALDVSA GA