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Database: UniProt
Entry: P36150
LinkDB: P36150
Original site: P36150 
ID   SUMT_YEAST              Reviewed;         593 AA.
AC   P36150; D6VXD0;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000303|PubMed:10051442};
DE            Short=Urogen III methylase {ECO:0000303|PubMed:10051442};
DE            EC=2.1.1.107 {ECO:0000269|PubMed:10051442};
DE   AltName: Full=SUMT;
DE   AltName: Full=Uroporphyrinogen III methylase;
DE            Short=UROM;
GN   Name=MET1 {ECO:0000303|PubMed:10051442}; Synonyms=MET20;
GN   OrderedLocusNames=YKR069W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=9003798; DOI=10.1016/s0014-5793(96)01423-8;
RA   Hansen J., Muldbjerg M., Cherest H., Surdin-Kerjan Y.;
RT   "Siroheme biosynthesis in Saccharomyces cerevisiae requires the products of
RT   both the MET1 and MET8 genes.";
RL   FEBS Lett. 401:20-24(1997).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10051442; DOI=10.1042/bj3380701;
RA   Raux E., McVeigh T., Peters S.E., Leustek T., Warren M.J.;
RT   "The role of Saccharomyces cerevisiae Met1p and Met8p in sirohaem and
RT   cobalamin biosynthesis.";
RL   Biochem. J. 338:701-708(1999).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Siroheme synthase involved in methionine biosynthesis.
CC       {ECO:0000269|PubMed:10051442, ECO:0000269|PubMed:9003798}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) +
CC         precorrin-2 + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32459,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58827, ChEBI:CHEBI:59789; EC=2.1.1.107;
CC         Evidence={ECO:0000269|PubMed:10051442};
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; Z28294; CAA82148.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09220.1; -; Genomic_DNA.
DR   PIR; S38145; S38145.
DR   RefSeq; NP_012995.3; NM_001179859.3.
DR   AlphaFoldDB; P36150; -.
DR   SMR; P36150; -.
DR   BioGRID; 34200; 42.
DR   DIP; DIP-4843N; -.
DR   IntAct; P36150; 2.
DR   MINT; P36150; -.
DR   STRING; 4932.YKR069W; -.
DR   iPTMnet; P36150; -.
DR   MaxQB; P36150; -.
DR   PaxDb; 4932-YKR069W; -.
DR   PeptideAtlas; P36150; -.
DR   EnsemblFungi; YKR069W_mRNA; YKR069W; YKR069W.
DR   GeneID; 853943; -.
DR   KEGG; sce:YKR069W; -.
DR   AGR; SGD:S000001777; -.
DR   SGD; S000001777; MET1.
DR   VEuPathDB; FungiDB:YKR069W; -.
DR   eggNOG; KOG1527; Eukaryota.
DR   HOGENOM; CLU_011276_2_2_1; -.
DR   InParanoid; P36150; -.
DR   OMA; TPCAIVE; -.
DR   OrthoDB; 296644at2759; -.
DR   BioCyc; MetaCyc:G3O-32035-MONOMER; -.
DR   BioCyc; YEAST:G3O-32035-MONOMER; -.
DR   BioGRID-ORCS; 853943; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P36150; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36150; Protein.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IDA:SGD.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IMP:SGD.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR   CDD; cd11642; SUMT; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR006366; CobA/CysG_C.
DR   InterPro; IPR012066; Met1_fungi.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR45790:SF6; UROPORPHYRINOGEN-III C-METHYLTRANSFERASE; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036555; SUMT_yeast; 1.
DR   SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Methionine biosynthesis; Methyltransferase;
KW   Porphyrin biosynthesis; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..593
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT                   /id="PRO_0000150387"
FT   REGION          278..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  66125 MW;  7C704866B08C0C6D CRC64;
     MVRDLVTLPS SLPLITAGFA TDQVHLLIGT GSTDSVSVCK NRIHSILNAG GNPIVVNPSS
     PSHTKQLQLE FGKFAKFEIV EREFRLSDLT TLGRVLVCKV VDRVFVDLPI TQSRLCEEIF
     WQCQKLRIPI NTFHKPEFST FNMIPTWVDP KGSGLQISVT TNGNGYILAN RIKRDIISHL
     PPNISEVVIN MGYLKDRIIN EDHKALLEEK YYQTDMSLPG FGYGLDEDGW ESHKFNKLIR
     EFEMTSREQR LKRTRWLSQI MEYYPMNKLS DIKLEDFETS SSPNKKTKQE TVTEGVVPPT
     DENIENGTKQ LQLSEVKKEE GPKKLGKISL VGSGPGSVSM LTIGALQEIK SADIILADKL
     VPQAILDLIP PKTETFIAKK FPGNAERAQQ ELLAKGLESL DNGLKVVRLK QGDPYIFGRG
     GEEFNFFKDH GYIPVVLPGI SSSLACTVLA QIPATQRDIA DQVLICTGTG RKGALPIIPE
     FVESRTTVFL MALHRANVLI TGLLKHGWDG DVPAAIVERG SCPDQRVTRT LLKWVPEVVE
     EIGSRPPGVL VVGKAVNALV EKDLINFDES RKFVIDEGFR EFEVDVDSLF KLY
//
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