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Database: UniProt
Entry: I0GRM5_SELRL
LinkDB: I0GRM5_SELRL
Original site: I0GRM5_SELRL 
ID   I0GRM5_SELRL            Unreviewed;       233 AA.
AC   I0GRM5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Putative precorrin-2 C(20)-methyltransferase {ECO:0000313|EMBL:BAL83412.1};
DE            EC=2.1.1.130 {ECO:0000313|EMBL:BAL83412.1};
GN   Name=cbiL {ECO:0000313|EMBL:BAL83412.1};
GN   OrderedLocusNames=SELR_17040 {ECO:0000313|EMBL:BAL83412.1};
OS   Selenomonas ruminantium subsp. lactilytica (strain NBRC 103574 / TAM6421).
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=927704 {ECO:0000313|EMBL:BAL83412.1, ECO:0000313|Proteomes:UP000007887};
RN   [1] {ECO:0000313|EMBL:BAL83412.1, ECO:0000313|Proteomes:UP000007887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103574 / TAM6421 {ECO:0000313|Proteomes:UP000007887};
RA   Oguchi A., Ankai A., Kaneko J., Yamada-Narita S., Fukui S., Takahashi M.,
RA   Onodera T., Kojima S., Fushimi T., Abe N., Kamio Y., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome sequence of Selenomonas ruminantium subsp. lactilytica
RT   TAM6421.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|PIRNR:PIRNR036427}.
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DR   EMBL; AP012292; BAL83412.1; -; Genomic_DNA.
DR   RefSeq; WP_014424845.1; NC_017068.1.
DR   AlphaFoldDB; I0GRM5; -.
DR   KEGG; sri:SELR_17040; -.
DR   PATRIC; fig|927704.6.peg.1765; -.
DR   eggNOG; COG2243; Bacteria.
DR   HOGENOM; CLU_076014_2_1_9; -.
DR   OrthoDB; 9804789at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000007887; Chromosome.
DR   GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd11645; Precorrin_2_C20_MT; 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; IPR012382; CobI/CbiL.
DR   InterPro; IPR006364; CobI/CbiL/CobIJ_dom.
DR   NCBIfam; TIGR01467; cobI_cbiL; 1.
DR   PANTHER; PTHR43467; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43467:SF2; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036427; Precrrn-2_mtase; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:BAL83412.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAL83412.1}.
FT   DOMAIN          5..211
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   233 AA;  25521 MW;  A37C4D435A077DA6 CRC64;
     MSGIFYGIGV GPGDPELLTV KAIKAIEQVD VLIAPKTEKK DGSVALSVAK PYLKKDVEIV
     YQVFPMVKGF AENSTDAWEA NKQEILELLN AGKNVAFLTI GDPMFYSTYI YVFRLLENAG
     VEIKTIPGIP AFAAIGSQLG YPIVEGDDVL SIIPATASPE KVEKAMQAAD NVVLMKVYKN
     FEEVADMLDQ NEMAEQAVLV SRAGLDDEKI IYDVVAHKKD KLNYLSTILT RKN
//
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