ID   SUMT_METBF              Reviewed;         255 AA.
AC   Q46BL0;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase;
DE            Short=Mba_SUMT;
DE            Short=SUMT;
DE            EC=2.1.1.107;
DE   AltName: Full=Uroporphyrinogen-III C-methyltransferase;
GN   OrderedLocusNames=Mbar_A1791;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=21197080; DOI=10.1155/2010/175050;
RA   Storbeck S., Rolfes S., Raux-Deery E., Warren M.J., Jahn D., Layer G.;
RT   "A novel pathway for the biosynthesis of heme in Archaea: genome-based
RT   bioinformatic predictions and experimental evidence.";
RL   Archaea 2010:175050-175050(2010).
CC   -!- FUNCTION: Involved in the archaeal biosynthesis of heme. Catalyzes the
CC       methylation of carbons 2 and 7 of uroporphyrinogen-III (UROGEN) to
CC       yield precorrin-2. It does not catalyze the overmethylation of
CC       precorrin-2 to trimethylpyrrocorphin. {ECO:0000269|PubMed:21197080}.
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:21197080};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21197080}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000099; AAZ70732.1; -; Genomic_DNA.
DR   RefSeq; WP_011306778.1; NC_007355.1.
DR   AlphaFoldDB; Q46BL0; -.
DR   SMR; Q46BL0; -.
DR   STRING; 269797.Mbar_A1791; -.
DR   EnsemblBacteria; AAZ70732; AAZ70732; Mbar_A1791.
DR   GeneID; 3625153; -.
DR   KEGG; mba:Mbar_A1791; -.
DR   eggNOG; arCOG00644; Archaea.
DR   HOGENOM; CLU_011276_7_0_2; -.
DR   OMA; TRPEQEE; -.
DR   OrthoDB; 67633at2157; -.
DR   UniPathway; UPA00262; UER00211.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IDA:UniProtKB.
DR   CDD; cd11642; SUMT; 1.
DR   Gene3D; 3.30.950.10; -; 1.
DR   Gene3D; 3.40.1010.10; -; 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; IPR003043; Uropor_MeTrfase_CS.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Porphyrin biosynthesis; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..255
FT                   /note="S-adenosyl-L-methionine-dependent uroporphyrinogen
FT                   III methyltransferase"
FT                   /id="PRO_0000428885"
FT   BINDING         15
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         91..93
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         121..122
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         175
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         232
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
SQ   SEQUENCE   255 AA;  27232 MW;  4BE8687DB3876D40 CRC64;
     MSGNYGKVYL VGSGPGDPEL LTLKARRLID SAEVIVYDQL PGKAILDSMP ASAEKINVGK
     YAGSHTMTQA EINEVLVQKA KEGKMVVRLK GGDPYVFGRG GEEAEVLVAE EIEFEVVPGI
     TSAIAVPAYA GIPVTHREST SMVTFITGHE DPTKEESGLD WETLAKFGGT IVILMGVKML
     GRNAEELMKH GKAPDTPVAV IERGTRADQR VTVGTLANIA SLAEERKVKA PAITVVGDVV
     HLHDILGEQR TGVDF