JHAMT_BOMMO
ID JHAMT_BOMMO Reviewed; 278 AA.
AC Q767F1; G9JKK5; H9JLJ0;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Juvenile hormone acid O-methyltransferase {ECO:0000305};
DE EC=2.1.1.325 {ECO:0000269|PubMed:14530389};
DE AltName: Full=Juvenile hormone acid methyltransferase {ECO:0000303|PubMed:14530389};
DE Short=BmJHAMT {ECO:0000303|PubMed:14530389};
GN Name=JHAMT {ECO:0000303|PubMed:14530389}; ORFNames=BGIBMGA010391;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Kinshu X Showa; TISSUE=Corpora allata;
RX PubMed=14530389; DOI=10.1073/pnas.2134232100;
RA Shinoda T., Itoyama K.;
RT "Juvenile hormone acid methyltransferase: a key regulatory enzyme for
RT insect metamorphosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11986-11991(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corpora allata;
RA Raji P.T., Sinto M.S., Omkumar R.V., Bhaskaran G., Muraleedharan D.;
RT "Molecular characterisation of jhamt gene from Bombyx mori.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T;
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
CC -!- FUNCTION: O-methyltransferase that transfers a methyl group from S-
CC adenosyl-L-methionine (SAM) to the carboxyl group of juvenile hormone
CC acids to produce active juvenile hormones in the corpora allata, the
CC last step during juvenile hormone biosynthesis (PubMed:14530389). Also
CC able to methylate farnesoate to methyl farnesoate (PubMed:14530389).
CC {ECO:0000269|PubMed:14530389}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesoate + S-adenosyl-L-methionine = methyl (2E,6E)-
CC farnesoate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43700,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:80535,
CC ChEBI:CHEBI:83276; EC=2.1.1.325;
CC Evidence={ECO:0000269|PubMed:14530389};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=juvenile hormone III carboxylate + S-adenosyl-L-methionine =
CC juvenile hormone III + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43720, ChEBI:CHEBI:27493, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:83274; EC=2.1.1.325;
CC Evidence={ECO:0000269|PubMed:14530389};
CC -!- TISSUE SPECIFICITY: Specifically expressed in the corpora allata (CA).
CC {ECO:0000269|PubMed:14530389}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the third and fourth instar.
CC At the beginning of the last (fifth) instar, the expression decreases
CC rapidly and becomes undetectable by day 4 and until pupation.
CC {ECO:0000269|PubMed:14530389}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AB113578; BAC98835.1; -; mRNA.
DR EMBL; JN851817; AEV45620.1; -; mRNA.
DR RefSeq; NP_001036901.1; NM_001043436.1.
DR AlphaFoldDB; Q767F1; -.
DR SMR; Q767F1; -.
DR STRING; 7091.BGIBMGA010391-TA; -.
DR GeneID; 692445; -.
DR KEGG; bmor:692445; -.
DR CTD; 34977; -.
DR eggNOG; ENOG502S1MZ; Eukaryota.
DR HOGENOM; CLU_037990_5_0_1; -.
DR OrthoDB; 785883at2759; -.
DR BioCyc; MetaCyc:MON-15959; -.
DR BRENDA; 2.1.1.325; 890.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0019010; F:farnesoic acid O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035049; F:juvenile hormone acid methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006718; P:juvenile hormone biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..278
FT /note="Juvenile hormone acid O-methyltransferase"
FT /id="PRO_0000433618"
FT CONFLICT 213
FT /note="K -> R (in Ref. 2; AEV45620)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="D -> G (in Ref. 2; AEV45620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 32546 MW; 1166CA0874305A14 CRC64;
MNNADLYRKS NSLQKRDALR CLEEHANKIK WKKIGDRVID LGCADGSVTD ILKVYMPKNY
GRLVGCDISE EMVKYANKHH GFGRTSFRVL DIEGDLTADL KQGFDHVFSF YTLHWIRDQE
RAFRNIFNLL GDEGDCLLLF LGHTPIFDVY RTLSHTEKWH SWLEHVDRFI SPYHDNEDPE
KEVKKIMERV GFSNIEVQCK TLFYVYDDLD VLKKSVAAIN PFNIPKDILE DFLEDYIDVV
REMRLLDRCN NNVGESVSIK FNYKVISVYA RKLCLSLM