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Database: UniProt
Entry: M3E2R0_9ACTN
LinkDB: M3E2R0_9ACTN
Original site: M3E2R0_9ACTN 
ID   M3E2R0_9ACTN            Unreviewed;       247 AA.
AC   M3E2R0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Precorrin-2 C(20)-methyltransferase {ECO:0000313|EMBL:EMF28162.1};
GN   ORFNames=H114_15352 {ECO:0000313|EMBL:EMF28162.1};
OS   Streptomyces gancidicus BKS 13-15.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces pseudogriseolus group.
OX   NCBI_TaxID=1284664 {ECO:0000313|EMBL:EMF28162.1, ECO:0000313|Proteomes:UP000011732};
RN   [1] {ECO:0000313|EMBL:EMF28162.1, ECO:0000313|Proteomes:UP000011732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BKS 13-15 {ECO:0000313|EMBL:EMF28162.1,
RC   ECO:0000313|Proteomes:UP000011732};
RX   PubMed=23599292;
RA   Kumar S., Kaur N., Singh N.K., Raghava G.P., Mayilraj S.;
RT   "Draft Genome Sequence of Streptomyces gancidicus Strain BKS 13-15.";
RL   Genome Announc. 1:E00150-13(2013).
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879, ECO:0000256|PIRNR:PIRNR036427}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMF28162.1}.
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DR   EMBL; AOHP01000063; EMF28162.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3E2R0; -.
DR   PATRIC; fig|1284664.3.peg.3085; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000011732; Unassembled WGS sequence.
DR   GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:InterPro.
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:EMF28162.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011732};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMF28162.1}.
FT   DOMAIN          8..217
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   247 AA;  25551 MW;  5615620A5BC63E4D CRC64;
     MPDVMSSRLI GVGVGPGDPE LVTVKGVNAL RAADVVVVPV MDTGERGRAE ATVLHYVPAE
     KVVRVVFALN ERTDRARREA AWDAAGERVA GMLREGGTVA FATIGDPNVY STFTYLALTV
     GELVPGVVVE TVPGITAMQD LAARSGAVLT EGTEPLTLVP VTAGAAVLKE ALAGPGTVVA
     YKFGRQAGEV ADALRETGRL DDAVWGSALG LPEESVRPAA EMDGEPLPYL STLIAPPRRG
     GGRGGKL
//
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