HTM_MYCA9
ID HTM_MYCA9 Reviewed; 227 AA.
AC B1MCE2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase {ECO:0000305};
DE Short=HQNO methyltransferase {ECO:0000303|PubMed:33064871};
DE Short=HQNO-MTase {ECO:0000303|PubMed:33064871};
DE EC=2.1.1.374 {ECO:0000269|PubMed:33064871};
DE AltName: Full=Heterocyclic toxin methyltransferase {ECO:0000303|PubMed:33064871};
GN Name=htm {ECO:0000303|PubMed:33064871};
GN OrderedLocusNames=MAB_2834c {ECO:0000312|EMBL:CAM62913.1};
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS 13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC 1543;
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC 1543;
RX PubMed=33064871; DOI=10.1111/febs.15595;
RA Sartor P., Bock J., Hennecke U., Thierbach S., Fetzner S.;
RT "Modification of the Pseudomonas aeruginosa toxin 2-heptyl-1-
RT hydroxyquinolin-4(1H)-one and other secondary metabolites by
RT methyltransferases from mycobacteria.";
RL FEBS J. 288:2360-2376(2021).
CC -!- FUNCTION: Involved in cellular response to chemical stress and may
CC contribute to resistance toward antimicrobial natural compounds as well
CC as drugs (Probable). Catalyzes the methylation and detoxification of
CC the P.aeruginosa toxin 2-heptyl-1-hydroxy-4(1H)-quinolinone (HQNO) to
CC 2-heptyl-1-methoxy-4(1H)-quinolinone (HMOQ) (PubMed:33064871). Can also
CC methylate 3-bromo-2-heptyl-1-hydroxy-4(1H)-quinolinone, and shows much
CC lower activity with 1-hydroxyquinolin-4(1H)-one, quercetin, 4-
CC hydroxyquinolin-2(1H)-one (DHQ) and 4-hydroxyisoquinolin-1(2H)-one
CC (PubMed:33064871). {ECO:0000269|PubMed:33064871,
CC ECO:0000305|PubMed:33064871}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-heptyl-1-hydroxy-4(1H)-quinolinone + S-adenosyl-L-methionine
CC = 2-heptyl-1-methoxy-4(1H)-quinolinone + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:65924, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:157768,
CC ChEBI:CHEBI:157769; EC=2.1.1.374;
CC Evidence={ECO:0000269|PubMed:33064871};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65925;
CC Evidence={ECO:0000269|PubMed:33064871};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-bromo-2-heptyl-1-hydroxy-4(1H)-quinolinone + S-adenosyl-L-
CC methionine = 3-bromo-2-heptyl-1-methoxy-4(1H)-quinolinone + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:65928, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:157778,
CC ChEBI:CHEBI:157779; EC=2.1.1.374;
CC Evidence={ECO:0000269|PubMed:33064871};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65929;
CC Evidence={ECO:0000269|PubMed:33064871};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.8 uM for HQNO {ECO:0000269|PubMed:33064871};
CC Note=kcat is 2.0 sec(-1) with HQNO as substrate.
CC {ECO:0000269|PubMed:33064871};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:33064871}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A5TZU0}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; CU458896; CAM62913.1; -; Genomic_DNA.
DR RefSeq; WP_005082352.1; NZ_MLCG01000003.1.
DR AlphaFoldDB; B1MCE2; -.
DR SMR; B1MCE2; -.
DR EnsemblBacteria; CAM62913; CAM62913; MAB_2834c.
DR GeneID; 66968255; -.
DR KEGG; mab:MAB_2834c; -.
DR OMA; DSGCGHA; -.
DR BRENDA; 2.1.1.374; 8960.
DR Proteomes; UP000007137; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..227
FT /note="2-heptyl-1-hydroxyquinolin-4(1H)-one
FT methyltransferase"
FT /id="PRO_0000452328"
SQ SEQUENCE 227 AA; 24731 MW; 3297ABB08580DABD CRC64;
MTENLQDMFE SSYRGEAPEQ LAARPPWSIG QPQPEILKLI EQGKVHGDVL DAGCGEAATA
LYLAERGHTA VGLDAAPTAI QLAKGYAAER GLTNVTFDVA DISNFTGYDG RFGTIIDSTL
FHSMPVELRE GYQQSIVRAA APGANYIVLV FDKAAFPPDI DGPHPVSEPE LREIVSKYWT
VDDISPARLY ANGDGFQDGG AQRFAEFREE SNGWVSMAGW LLQAHRD
