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Database: UniProt
Entry: A0A1K1NIP2_RUMFL
LinkDB: A0A1K1NIP2_RUMFL
Original site: A0A1K1NIP2_RUMFL 
ID   A0A1K1NIP2_RUMFL        Unreviewed;       251 AA.
AC   A0A1K1NIP2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Cobalt-precorrin 4 C11-methyltransferase {ECO:0000313|EMBL:SFW35196.1};
GN   ORFNames=SAMN02910280_2046 {ECO:0000313|EMBL:SFW35196.1};
OS   Ruminococcus flavefaciens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1265 {ECO:0000313|EMBL:SFW35196.1, ECO:0000313|Proteomes:UP000183461};
RN   [1] {ECO:0000313|EMBL:SFW35196.1, ECO:0000313|Proteomes:UP000183461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YL228 {ECO:0000313|EMBL:SFW35196.1,
RC   ECO:0000313|Proteomes:UP000183461};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879}.
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DR   EMBL; FPIP01000004; SFW35196.1; -; Genomic_DNA.
DR   RefSeq; WP_072300297.1; NZ_FPIP01000004.1.
DR   AlphaFoldDB; A0A1K1NIP2; -.
DR   Proteomes; UP000183461; Unassembled WGS sequence.
DR   GO; GO:0046026; F:precorrin-4 C11-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd11641; Precorrin-4_C11-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; IPR006362; Cbl_synth_CobM/CibF.
DR   NCBIfam; TIGR01465; cobM_cbiF; 1.
DR   PANTHER; PTHR45790:SF4; COBALT-PRECORRIN-4 C(11)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:SFW35196.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFW35196.1}.
FT   DOMAIN          1..207
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   251 AA;  26986 MW;  1F7AEA800EDC675D CRC64;
     MVHFVGAGSG AADLITLRGK KLLEEADVVI YAGSLVNPEL LDYTKSGCEI YNSAVMTLDE
     VIDVMEKAEN VGKTTVRLHT GDPCVYGAVR EQMDRLDKLG IDYDVCPGVS SFCGAAAALK
     VEYTLPDVSQ TVILTRMAGR TPVPEKESIE SLAAHHATMV IFLSTGMLEE LSERLINGGY
     STETPAAIVY KATWADEKVC RCTVGSLAET AAKNGITKTA LITVGDFLGD VRSLSKLYSA
     DFETKFRKAS K
//
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