4OMT1_PAPSO
ID 4OMT1_PAPSO Reviewed; 354 AA.
AC Q7XB11;
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 1 {ECO:0000303|PubMed:12946416};
DE Short=4'-OMT1 {ECO:0000305};
DE Short=Ps4'OMT1 {ECO:0000303|PubMed:12946416};
DE EC=2.1.1.116 {ECO:0000305};
DE AltName: Full=S-adenosyl-L-methionine:3'-hydroxy-N-methylcoclaurine 4'-O-methyltransferase {ECO:0000305};
GN Name=4'OMT1 {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:AAP45313.1};
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [3]
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 Catalyzes the transfer of the methyl group to the 4'-hydroxyl group of
CC 3'-hydroxy-N-methylcoclaurine to form reticuline. Also involved in the
CC papaverine biosynthesis. {ECO:0000269|PubMed:23738019, ECO:0000305}.
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:0000305};
CC -!- PATHWAY: Alkaloid biosynthesis; (S)-reticuline biosynthesis; (S)-
CC reticuline from (S)-norcoclaurine: step 4/4.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers
CC (PubMed:12946416, PubMed:16813579). Restricted to sieve elements of the
CC phloem adjacent or proximal to laticifers (PubMed:16813579).
CC {ECO:0000269|PubMed:12946416, ECO:0000269|PubMed:16813579}.
CC -!- DEVELOPMENTAL STAGE: Transiently induced from 4 to 7 days after seed
CC imbibition. {ECO:0000269|PubMed:12946416, ECO:0000269|PubMed:16813579}.
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; AY217333; AAP45313.1; -; mRNA.
DR AlphaFoldDB; Q7XB11; -.
DR SMR; Q7XB11; -.
DR PRIDE; Q7XB11; -.
DR BioCyc; MetaCyc:MON-18209; -.
DR BRENDA; 2.1.1.116; 4515.
DR UniPathway; UPA00306; UER00444.
DR PRO; PR:Q7XB11; -.
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 2: Evidence at transcript level;
KW Alkaloid metabolism; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..354
FT /note="3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-
FT methyltransferase 1"
FT /id="PRO_0000433984"
FT ACT_SITE 261
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 354 AA; 39402 MW; 9464FC9A537835EB CRC64;
MGSSIDAETH EVDIKDQAQL WNIIYGYADS LVLRCTVEIG IADIIKNNNG SITLSELVSK
LPLSNVNSDN LYRLLRYLVH LNILGQQTCA AGVDRVYSLK PVGTLLLKDS ERSMAPVILG
LSQKDFLFVW NFVKEGLGTG STTAFEKAMG MDMWKYLEVN PNQSQLFDEG QAGETRLLTK
TLLVDCRDTF QGMDSLVDVG GGNGTTIKAI HEAFPHIKCT LYDLPHVIAN SDDHPNILKV
PGDMFMSVPS AQVLLLKCVL HDWTDEHCVN ILKKCKEAIP KETGKVIIVD VALEEESEHE
LTKARLILDI DMLVNTGGRE RTAEDWENLL KRAGFRSHKI RPIRAIQSVI EAFP
