4OMT2_PAPSO
ID 4OMT2_PAPSO Reviewed; 357 AA.
AC Q7XB10;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase 2 {ECO:0000303|PubMed:12946416};
DE Short=4'-OMT2 {ECO:0000305};
DE Short=Ps4'OMT2 {ECO:0000303|PubMed:12946416};
DE EC=2.1.1.116 {ECO:0000269|PubMed:16034588};
DE AltName: Full=S-adenosyl-L-methionine:3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase {ECO:0000305};
GN Name=4'OMT2 {ECO:0000303|PubMed:12946416};
OS Papaver somniferum (Opium poppy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Papaver.
OX NCBI_TaxID=3469 {ECO:0000312|EMBL:AAP45314.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION BY ELICITOR AND WOUNDING.
RC STRAIN=cv. Marianne;
RX PubMed=12946416; DOI=10.1016/s0031-9422(03)00292-9;
RA Facchini P.J., Park S.U.;
RT "Developmental and inducible accumulation of gene transcripts involved in
RT alkaloid biosynthesis in opium poppy.";
RL Phytochemistry 64:177-186(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16034588; DOI=10.1007/s00425-005-1550-4;
RA Ziegler J., Diaz-Chavez M.L., Kramell R., Ammer C., Kutchan T.M.;
RT "Comparative macroarray analysis of morphine containing Papaver somniferum
RT and eight morphine free Papaver species identifies an O-methyltransferase
RT involved in benzylisoquinoline biosynthesis.";
RL Planta 222:458-471(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Marianne;
RX PubMed=16813579; DOI=10.1111/j.1365-313x.2006.02801.x;
RA Samanani N., Alcantara J., Bourgault R., Zulak K.G., Facchini P.J.;
RT "The role of phloem sieve elements and laticifers in the biosynthesis and
RT accumulation of alkaloids in opium poppy.";
RL Plant J. 47:547-563(2006).
RN [4]
RP FUNCTION.
RX PubMed=22725256; DOI=10.1111/j.1365-313x.2012.05084.x;
RA Desgagne-Penix I., Facchini P.J.;
RT "Systematic silencing of benzylisoquinoline alkaloid biosynthetic genes
RT reveals the major route to papaverine in opium poppy.";
RL Plant J. 72:331-344(2012).
RN [5]
RP FUNCTION.
RX PubMed=23738019; DOI=10.1371/journal.pone.0065622;
RA Pathak S., Lakhwani D., Gupta P., Mishra B.K., Shukla S., Asif M.H.,
RA Trivedi P.K.;
RT "Comparative transcriptome analysis using high papaverine mutant of Papaver
RT somniferum reveals pathway and uncharacterized steps of papaverine
RT biosynthesis.";
RL PLoS ONE 8:E65622-E65622(2013).
CC -!- FUNCTION: Involved in the biosynthesis of benzylisoquinoline alkaloids
CC (PubMed:16034588, PubMed:22725256, PubMed:23738019). Catalyzes the
CC transfer of the methyl group to the 4'-hydroxyl group of 3'-hydroxy-N-
CC methylcoclaurine to form reticuline (PubMed:16034588). Can also use
CC laudanosoline and, with a lower activity, 6-O-methylnorlaudanosoline
CC and norlaudanosoline as substrates (PubMed:16034588). Also involved in
CC the papaverine biosynthesis (PubMed:22725256, PubMed:23738019).
CC {ECO:0000269|PubMed:16034588, ECO:0000269|PubMed:22725256,
CC ECO:0000269|PubMed:23738019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-3'-hydroxy-N-methylcoclaurine + S-adenosyl-L-methionine =
CC (S)-reticuline + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:57873, ChEBI:CHEBI:58010, ChEBI:CHEBI:59789;
CC EC=2.1.1.116; Evidence={ECO:0000269|PubMed:16034588};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=81 uM for 3'-hydroxy-N-methyl-(S)-coclaurine
CC {ECO:0000269|PubMed:16034588};
CC KM=39 uM for laudanosoline {ECO:0000269|PubMed:16034588};
CC KM=31 uM for 6-O-methylnorlaudanosoline
CC {ECO:0000269|PubMed:16034588};
CC KM=37 uM for norlaudanosoline {ECO:0000269|PubMed:16034588};
CC KM=179 uM for S-adenosyl-L-methionine with 6-O-methylnorlaudanosoline
CC as substrate {ECO:0000269|PubMed:16034588};
CC KM=136 uM for S-adenosyl-L-methionine with norlaudanosoline as
CC substrate {ECO:0000269|PubMed:16034588};
CC Vmax=1824 pmol/sec/mg enzyme with 3'-hydroxy-N-methyl-(S)-coclaurine
CC as substrate {ECO:0000269|PubMed:16034588};
CC Vmax=1239 pmol/sec/mg enzyme with laudanosoline as substrate
CC {ECO:0000269|PubMed:16034588};
CC Vmax=588 pmol/sec/mg enzyme with 6-O-methylnorlaudanosoline as
CC substrate {ECO:0000269|PubMed:16034588};
CC Vmax=236 pmol/sec/mg enzyme with norlaudanosoline as substrate
CC {ECO:0000269|PubMed:16034588};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:16034588};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:16034588};
CC -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-
CC reticuline from (S)-norcoclaurine: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16034588}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers
CC (PubMed:12946416). {ECO:0000269|PubMed:12946416}.
CC -!- DEVELOPMENTAL STAGE: Transiently induced from 4 to 7 days after seed
CC imbibition. {ECO:0000269|PubMed:12946416}.
CC -!- INDUCTION: Up-regulated upon fungal elicitor treatment or wounding.
CC {ECO:0000269|PubMed:12946416}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000305}.
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DR EMBL; AY217334; AAP45314.1; -; mRNA.
DR AlphaFoldDB; Q7XB10; -.
DR SMR; Q7XB10; -.
DR BRENDA; 2.1.1.116; 4515.
DR UniPathway; UPA00306; UER00444.
DR PRO; PR:Q7XB10; -.
DR GO; GO:0030784; F:3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR012967; Plant_MeTrfase_dimerisation.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF08100; Dimerisation; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..357
FT /note="3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-
FT methyltransferase 2"
FT /id="PRO_0000433985"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 357 AA; 39691 MW; AA2943C8048BA471 CRC64;
MGSLDAKPAA ATQEVSIKDQ AQLWNIIYGF ADSLVLRCAV EIGIADIIKN NDGAITLAQL
AAKLPITNVS SDYLYRMVRY LVHLNIIEQE TCNGGVEKVY SLKPVGTLLL RDAERSMVPM
ILGMTQKDFM VSWHFMKEGL GNGSTTAFEK GMGMDIWKYL EGNPDQSQLF NEGMAGETRL
LTKTLIEDCR DTFQGLDSLV DIGGGNGTTI KAIYEAFPHI KCTLYDLPHV VANSHDLPNI
EKVPGDMFKS VPSAQAILLK LILHDWTDEE CVNILKKCKE AIPKETGKVI IVDVALEEES
NHELTKTRLI LDIDMLVNTG GRERTADDWE NLLKRAGFRS HKIRPIRAIQ SVIEAFP
