ID   SUMT_BACSU              Reviewed;         257 AA.
AC   O34744; Q796I5;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Uroporphyrinogen-III C-methyltransferase;
DE            Short=Urogen III methylase;
DE            EC=2.1.1.107 {ECO:0000250|UniProtKB:P29928};
DE   AltName: Full=S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase;
DE            Short=SUMT;
DE   AltName: Full=Uroporphyrinogen III methylase;
DE            Short=UROM;
GN   Name=sumT; Synonyms=ylnD; OrderedLocusNames=BSU15610;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Foulger D., Errington J.;
RT   "Cloning and sequencing 8 Kbp of DNA from Bacillus subtilis downstream of
RT   the pyr operon.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   INDUCTION.
RC   STRAIN=168 / JH642;
RX   PubMed=11004190; DOI=10.1128/jb.182.20.5885-5892.2000;
RA   Mansilla M.C., Albanesi D., de Mendoza D.;
RT   "Transcriptional control of the sulfur-regulated cysH operon, containing
RT   genes involved in L-cysteine biosynthesis in Bacillus subtilis.";
RL   J. Bacteriol. 182:5885-5892(2000).
CC   -!- FUNCTION: Catalyzes the two successive C-2 and C-7 methylation
CC       reactions involved in the conversion of uroporphyrinogen III to
CC       precorrin-2 via the intermediate formation of precorrin-1. It is a step
CC       in the biosynthesis of both cobalamin (vitamin B12) and siroheme.
CC       {ECO:0000250|UniProtKB:P29928}.
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:0000250|UniProtKB:P29928};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32460;
CC         Evidence={ECO:0000250|UniProtKB:P29928};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       precorrin-2 from uroporphyrinogen III: step 1/1.
CC       {ECO:0000250|UniProtKB:P29928}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC       {ECO:0000250|UniProtKB:P29928}.
CC   -!- INDUCTION: Up-regulated by sulfur starvation and repressed by cysteine.
CC       Also induced by O-acetyl-L-serine (OAS), a direct precursor of
CC       cysteine, maybe via inactivation of a putative transcriptional
CC       repressor of the cysH operon whose activity is controlled by the
CC       intracellular levels of OAS. {ECO:0000269|PubMed:11004190}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ000974; CAA04413.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13435.1; -; Genomic_DNA.
DR   PIR; D69877; D69877.
DR   RefSeq; NP_389444.1; NC_000964.3.
DR   RefSeq; WP_003232095.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O34744; -.
DR   SMR; O34744; -.
DR   STRING; 224308.BSU15610; -.
DR   PaxDb; 224308-BSU15610; -.
DR   EnsemblBacteria; CAB13435; CAB13435; BSU_15610.
DR   GeneID; 936712; -.
DR   KEGG; bsu:BSU15610; -.
DR   PATRIC; fig|224308.179.peg.1701; -.
DR   eggNOG; COG0007; Bacteria.
DR   InParanoid; O34744; -.
DR   OrthoDB; 9815856at2; -.
DR   PhylomeDB; O34744; -.
DR   BioCyc; BSUB:BSU15610-MONOMER; -.
DR   UniPathway; UPA00148; UER00211.
DR   UniPathway; UPA00262; UER00211.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IBA:GO_Central.
DR   CDD; cd11642; SUMT; 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   NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR   PANTHER; PTHR45790:SF3; S-ADENOSYL-L-METHIONINE-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   2: Evidence at transcript level;
KW   Cobalamin biosynthesis; Methyltransferase; Porphyrin biosynthesis;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..257
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT                   /id="PRO_0000378491"
FT   BINDING         11
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         87..89
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         117..118
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
FT   BINDING         170
FT                   /ligand="S-adenosyl-L-homocysteine"
FT                   /ligand_id="ChEBI:CHEBI:57856"
FT                   /evidence="ECO:0000250|UniProtKB:P21631"
SQ   SEQUENCE   257 AA;  28516 MW;  B1D28A495D27DA85 CRC64;
     MGKVYIVGAG PGDPDLLTIK ALKAIEKADV ILYDRLVNKE ILQYAKEQAD LIYCGKLPDF
     HTMKQETINR FLVKYAQKGK MVVRLKGGDP FVFGRGGEEA ECLSENGIPF EIIPGITSGI
     AAAAYAGIPV THRDAGSNVA FVTGHYKKEE DFEEKWKALA TGIDTLVIYM GIKNVQQIER
     KLLENGRDGS TPAAFIHWGT TDKQKSVFCT VDTLSETVIK ENITNPSLIV IGNVVNYHYK
     LEWFESELKK QDLSEAL
//