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Database: UniProt
Entry: L0A2W5_DEIPD
LinkDB: L0A2W5_DEIPD
Original site: L0A2W5_DEIPD 
ID   L0A2W5_DEIPD            Unreviewed;       277 AA.
AC   L0A2W5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Precorrin-2 C20-methyltransferase {ECO:0000313|EMBL:AFZ67789.1};
GN   OrderedLocusNames=Deipe_2309 {ECO:0000313|EMBL:AFZ67789.1};
OS   Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS   KR-200).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ67789.1, ECO:0000313|Proteomes:UP000010467};
RN   [1] {ECO:0000313|Proteomes:UP000010467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC   {ECO:0000313|Proteomes:UP000010467};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT   19664.";
RL   Submitted (MAR-2012) 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; CP003382; AFZ67789.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0A2W5; -.
DR   STRING; 937777.Deipe_2309; -.
DR   KEGG; dpd:Deipe_2309; -.
DR   PATRIC; fig|937777.3.peg.2311; -.
DR   eggNOG; COG2243; Bacteria.
DR   HOGENOM; CLU_076014_2_1_0; -.
DR   OrthoDB; 9804789at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000010467; Chromosome.
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; 2.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AFZ67789.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010467};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFZ67789.1}.
FT   DOMAIN          10..223
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   277 AA;  29586 MW;  9E6C8197A4234B21 CRC64;
     MGGGRLKPGT FYGVGVGPGP QGLLPVAALE ALRTVNVIFT PRSSVSGDSV ARHCLRGLGL
     PEERFREVEF FMNTDPAQLA RQYAQLAREI AHELRAGRDV AYLTIGDTFT YSTYGYTLAA
     LREELPEAPR ITFPGVTSYA AAAAALEFPL GEGKERTLIL PCPDDMAQLR REIETHDVVI
     LMKIAQRFGA VRTLLHDLGI AQHCVLAARL GLPGEALHHD LSGDLSGDLT APSNLAQATD
     LTQATGERLG YLSTLLIRKA PPRNSSSAGT ARAGGQA
//
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