ERG6_PNEC8
ID ERG6_PNEC8 Reviewed; 377 AA.
AC Q96WX4; A0A0W4ZC26;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Sterol 24-C-methyltransferase;
DE EC=2.1.1.- {ECO:0000269|PubMed:11906033, ECO:0000269|PubMed:12010494};
DE AltName: Full=Delta(24)-sterol C-methyltransferase;
DE AltName: Full=S-adenosyl-L-methionine:sterol C-24 methyl transferase {ECO:0000303|PubMed:12010494};
DE Short=SAM:SMT {ECO:0000303|PubMed:11906033};
GN Name=erg6; ORFNames=T552_03167;
OS Pneumocystis carinii (strain B80) (Rat pneumocystis pneumonia agent)
OS (Pneumocystis carinii f. sp. carinii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis.
OX NCBI_TaxID=1408658;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RX PubMed=11906033; DOI=10.1111/j.1550-7408.2001.tb00491.x;
RA Kaneshiro E.S., Rosenfeld J.A., Basselin M., Bradshaw S., Stringer J.R.,
RA Smulian A.G., Giner J.L.;
RT "Pneumocystis carinii erg6 gene: sequencing and expression of recombinant
RT SAM:sterol methyltransferase in heterologous systems.";
RL J. Eukaryot. Microbiol. 48:144S-146S(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B80;
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=12010494; DOI=10.1046/j.1365-2958.2002.02932.x;
RA Kaneshiro E.S., Rosenfeld J.A., Basselin-Eiweida M., Stringer J.R.,
RA Keely S.P., Smulian A.G., Giner J.L.;
RT "The Pneumocystis carinii drug target S-adenosyl-L-methionine:sterol C-24
RT methyl transferase has a unique substrate preference.";
RL Mol. Microbiol. 44:989-999(2002).
CC -!- FUNCTION: Catalyzes the transfer of 2 methyl groups from 2 S-adenosyl-
CC methionine molecules to the C-24 of lanosterol, producing first
CC eburicol (24-methylenelanosterol) from lanosterol and then
CC pneumocysterol (24Z-ethylidenelanosterol) from eburicol.
CC {ECO:0000269|PubMed:12010494}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lanosterol + S-adenosyl-L-methionine = eburicol + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:52652, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16521, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:70315; Evidence={ECO:0000269|PubMed:11906033,
CC ECO:0000269|PubMed:12010494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eburicol + S-adenosyl-L-methionine = (24Z)-
CC ethylidenelanosterol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55088, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:70315, ChEBI:CHEBI:138589;
CC Evidence={ECO:0000269|PubMed:11906033, ECO:0000269|PubMed:12010494};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.6 uM for lanosterol {ECO:0000269|PubMed:12010494};
CC KM=19.1 uM for 24-methylenelanosterol {ECO:0000269|PubMed:12010494};
CC KM=40.6 uM for zymosterol {ECO:0000269|PubMed:12010494};
CC Vmax=154.7 pmol/min/mg enzyme for lanosterol
CC {ECO:0000269|PubMed:12010494};
CC Vmax=738.3 pmol/min/mg enzyme for 24-methylenelanosterol
CC {ECO:0000269|PubMed:12010494};
CC Vmax=41.9 pmol/min/mg enzyme for zymosterol
CC {ECO:0000269|PubMed:12010494};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:12010494};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:12010494};
CC -!- PATHWAY: Steroid metabolism. {ECO:0000305|PubMed:12010494}.
CC -!- MISCELLANEOUS: Cholesterol is the major sterol found in P.carinii, of
CC which most, if not all, is scavenged from the host. In addition to
CC cholesterol, 41 other sterols have been detected in P.carinii, but
CC ergosterol, the major sterol in higher fungi, is not among them.
CC {ECO:0000305|PubMed:12010494}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Erg6/SMT family. {ECO:0000255|PROSITE-ProRule:PRU01022}.
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DR EMBL; AY032981; AAK54439.1; -; mRNA.
DR EMBL; LFVZ01000015; KTW25893.1; -; Genomic_DNA.
DR RefSeq; XP_018224473.1; XM_018371680.1.
DR AlphaFoldDB; Q96WX4; -.
DR SMR; Q96WX4; -.
DR EnsemblFungi; KTW25893; KTW25893; T552_03167.
DR GeneID; 28937883; -.
DR OrthoDB; 661953at2759; -.
DR BRENDA; 2.1.1.142; 4924.
DR BRENDA; 2.1.1.41; 4924.
DR Proteomes; UP000054454; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR030384; MeTrfase_SMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR013705; Sterol_MeTrfase_C.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF08498; Sterol_MT_C; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51685; SAM_MT_ERG6_SMT; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW S-adenosyl-L-methionine; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..377
FT /note="Sterol 24-C-methyltransferase"
FT /id="PRO_0000124796"
SQ SEQUENCE 377 AA; 43228 MW; 03708EE1EA885DD5 CRC64;
MSFELERIDI EKDREFSEIM HGKDAAKERG LLSSFRKDKE AQKIALDSYF GFWGDKCTSE
KNDIHQQERF KFYATLTRHY YNLVTDFYEY GWSTSFHFCR FAKDESFSQA IARHEHYIAL
HAGIREGETV LDVGCGVGGP ACQISVFTGA NIVGLNNNDY QIQRAKYYSE KKGLSDKLKF
IKGDFMQMPF PENSFDKIYS IEATIHAPSL EGVYSEIYRV LKPGGLYASY EWVMLNKYDE
NDPEHQQIVY GIEIGDSIPK ISKIGEAEAA LIKVGFEIIH SEELSTKNSP LPWYYYLDGD
LRKVRSFRDF ISIARMTTIG KWLISSFIGL MEFIGLLPKG SKKVNDILLV AADSLVKAGK
KEIFTPMQLW VCRKPLV
