JHAMT_DROME
ID JHAMT_DROME Reviewed; 297 AA.
AC Q9VJK8; Q767F0; Q8T900;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Juvenile hormone acid O-methyltransferase {ECO:0000303|PubMed:18549957, ECO:0000305};
DE EC=2.1.1.325 {ECO:0000269|PubMed:18549957};
DE AltName: Full=Juvenile hormone acid methyltransferase {ECO:0000303|PubMed:18549957};
DE Short=DmJHAMT {ECO:0000303|PubMed:18549957};
GN Name=jhamt {ECO:0000312|FlyBase:FBgn0028841};
GN ORFNames=CG17330 {ECO:0000312|FlyBase:FBgn0028841};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18549957; DOI=10.1016/j.ibmb.2008.04.003;
RA Niwa R., Niimi T., Honda N., Yoshiyama M., Itoyama K., Kataoka H.,
RA Shinoda T.;
RT "Juvenile hormone acid O-methyltransferase in Drosophila melanogaster.";
RL Insect Biochem. Mol. Biol. 38:714-720(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-297.
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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:18549957). Also
CC able to methylate farnesoate to methyl farnesoate (PubMed:18549957).
CC {ECO:0000269|PubMed:18549957}.
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:18549957};
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:18549957};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.32 uM for juvenile hormone III acid
CC {ECO:0000269|PubMed:18549957};
CC KM=0.18 uM for farnesoate {ECO:0000269|PubMed:18549957};
CC Note=kcat is 7.7 min(-1) for juvenile hormone III acid. kcat is 10.1
CC min(-1) for farnesoate. kcat is 0.103 min(-1) for laureate acid. kcat
CC is 0.041 min(-1) for palmitate acid. {ECO:0000269|PubMed:18549957};
CC -!- TISSUE SPECIFICITY: Predominantly expressed in corpora allata. Also
CC expressed at low level in testis. {ECO:0000269|PubMed:18549957}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the first instar larvae and
CC then gradually decreases during larval development. Expression
CC increases again in the wandering third larval stage. The lowest amount
CC of expression is observed in the early and mid-pupal stages. After
CC this, expression increases in the late pupal stage in both male and
CC female adults. {ECO:0000269|PubMed:18549957}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL68063.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB113579; BAC98836.1; -; mRNA.
DR EMBL; AE014134; AAF53533.2; -; Genomic_DNA.
DR EMBL; AE014134; AHN54494.1; -; Genomic_DNA.
DR EMBL; AY075194; AAL68063.1; ALT_INIT; mRNA.
DR RefSeq; NP_001285980.1; NM_001299051.1.
DR RefSeq; NP_609793.2; NM_135949.3.
DR AlphaFoldDB; Q9VJK8; -.
DR SMR; Q9VJK8; -.
DR STRING; 7227.FBpp0099678; -.
DR PaxDb; Q9VJK8; -.
DR EnsemblMetazoa; FBtr0080859; FBpp0099678; FBgn0028841.
DR EnsemblMetazoa; FBtr0340233; FBpp0309208; FBgn0028841.
DR GeneID; 34977; -.
DR KEGG; dme:Dmel_CG17330; -.
DR UCSC; CG17330-RA; d. melanogaster.
DR CTD; 34977; -.
DR FlyBase; FBgn0028841; jhamt.
DR VEuPathDB; VectorBase:FBgn0028841; -.
DR eggNOG; ENOG502S1MZ; Eukaryota.
DR HOGENOM; CLU_037990_5_0_1; -.
DR InParanoid; Q9VJK8; -.
DR OMA; HVTSFYC; -.
DR OrthoDB; 785883at2759; -.
DR PhylomeDB; Q9VJK8; -.
DR BRENDA; 2.1.1.325; 1994.
DR BioGRID-ORCS; 34977; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34977; -.
DR PRO; PR:Q9VJK8; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0028841; Expressed in spermathecum and 14 other tissues.
DR Genevisible; Q9VJK8; DM.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0019010; F:farnesoic acid O-methyltransferase activity; IDA:FlyBase.
DR GO; GO:0004395; F:hexaprenyldihydroxybenzoate methyltransferase activity; IBA:GO_Central.
DR GO; GO:0035049; F:juvenile hormone acid methyltransferase activity; IDA:FlyBase.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006718; P:juvenile hormone biosynthetic process; IDA:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08242; Methyltransf_12; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; Transferase.
FT CHAIN 1..297
FT /note="Juvenile hormone acid O-methyltransferase"
FT /id="PRO_0000433619"
FT CONFLICT 166
FT /note="F -> Y (in Ref. 1; BAC98836 and 4; AAL68063)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="N -> S (in Ref. 4; AAL68063)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> N (in Ref. 1; BAC98836 and 4; AAL68063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 34065 MW; 9ACFBB7E0472E010 CRC64;
MNQASLYQHA NQVQRHDAKL ILDEFASTMQ WRSDGEDALL DVGSGSGNVL MDFVKPLLPI
RGQLVGTDIS SQMVHYASKH YQREERTRFQ VLDIGCERLP EELSGRFDHV TSFYCLHWVQ
NLKGALGNIY NLLKPEGGDC LLAFLASNPV YEVYKILKTN DKWSTFMQDV ENFISPLHYS
LSPGEEFSQL LNDVGFVQHN VEIRNEVFVY EGVRTLKDNV KAICPFLERM PADLHEQFLD
DFIDIVISMN LQQGENNEDQ KFLSPYKLVV AYARKTPEFV NNVFLEPTHQ NLVKGIN
