ID A0A094CZ93_9PEZI Unreviewed; 779 AA.
AC A0A094CZ93;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Sterol 24-C-methyltransferase {ECO:0000256|RuleBase:RU362025};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362025};
DE AltName: Full=Delta(24)-sterol C-methyltransferase {ECO:0000256|RuleBase:RU362025};
GN ORFNames=V496_08305 {ECO:0000313|EMBL:KFY52640.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY52640.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY52640.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of methyl groups from S-adenosyl-
CC methionine to the C-24 of sterols. {ECO:0000256|RuleBase:RU362025}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- PATHWAY: Steroid metabolism. {ECO:0000256|RuleBase:RU362025}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Erg6/SMT family. {ECO:0000256|PROSITE-ProRule:PRU01022,
CC ECO:0000256|RuleBase:RU362025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY52640.1}.
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DR EMBL; JPJY01001589; KFY52640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094CZ93; -.
DR STRING; 1420909.A0A094CZ93; -.
DR HOGENOM; CLU_020136_0_0_1; -.
DR OrthoDB; 275921at2759; -.
DR Proteomes; UP000029302; Unassembled WGS sequence.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0003838; F:sterol 24-C-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR030384; MeTrfase_SMT.
DR InterPro; IPR027110; PDHB.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR013705; Sterol_MeTrfase_C.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR11624; DEHYDROGENASE RELATED; 1.
DR PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF08498; Sterol_MT_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51685; SAM_MT_ERG6_SMT; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU362025};
KW Lipid metabolism {ECO:0000256|RuleBase:RU362025};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01022}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01022};
KW Steroid biosynthesis {ECO:0000256|RuleBase:RU362025};
KW Steroid metabolism {ECO:0000256|RuleBase:RU362025};
KW Sterol biosynthesis {ECO:0000256|RuleBase:RU362025};
KW Sterol metabolism {ECO:0000256|RuleBase:RU362025};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01022}.
FT DOMAIN 80..375
FT /note="SAM-dependent methyltransferase Erg6/SMT-type"
FT /evidence="ECO:0000259|PROSITE:PS51685"
SQ SEQUENCE 779 AA; 86260 MW; 33F679ADF073AE5D CRC64;
MASTLETENH VRDQEFAKAM HGKSGAEQNH FMAWMKKDKG AQKEAVDEYF KHWDNKAAKD
ETEAVREARR AEYATLTKHY YNLATDLYEN GWGQSFHFCR FAYGEPFNQA IARHEHYLAH
HIGIKQGMKV LDVGCGVGGP AREIAKFTGA HITGLNNNDY QIERATAYAK KEGLSDQLKF
VKGDFMQMGF PEETFDAVYA IEATVHAQSL EGVYHEIFKT LKPGGVFGVY EWLMTENYDA
TNVRHREIRL GIEQGNGISN MVKISEGLRA IQAAGFVLEL HEDLAQRDDP SPWYYPIAGD
FKYMGSIWDF PTIARMTKLG RGIVHKFVWG LECLRIAPPG TNKSADNLAL AADMLVEGAK
LDLFTPIVLL SSQQSFQNLA RIAVQSLNDS KFRGEADLTI AFRPHNDSST TLKPSIPSLR
TAPVARRAFR RSDLPRVVAA QWRGYASGGV KEMTVREALN EALAEELEQN PKVFVLGEEV
AQYNGAYKVT KGLLDRFGDQ RIIDSPITES GFTGLTVGAA LAGLHPVCEF MTFNFAMQAI
DQIINSAAKT HYMSGGIQPC NITFRGPNGF AAGVAAQHSQ DYSAWYGSIP GLKVVTPWSA
EDAKGLLKAA IRDPNPVVVL ENELLYGQSF PMSEEAQRSD FVIPFGKAKV ERQGKDLTII
TLSRCVGQSL VAAENLKKKY GVEVEVVNLR SIKPLDVAAI VKSVKKTGRL LAVESGFPSF
GVGSEILALT MEYAFDYLEA PAQRITGAEV PTPYAKELED MSFPNEDLIE AFAKKMLKL
//
