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Database: UniProt
Entry: J9RKY8_9ACTN
LinkDB: J9RKY8_9ACTN
Original site: J9RKY8_9ACTN 
ID   J9RKY8_9ACTN            Unreviewed;       432 AA.
AC   J9RKY8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Cobalt-precorrin-6B (C5,15)-methyltransferase {ECO:0000313|EMBL:AFR49022.1};
GN   ORFNames=KTR9_2385 {ECO:0000313|EMBL:AFR49022.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR49022.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR49022.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR49022.1,
RC   ECO:0000313|Proteomes:UP000003281};
RX   PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA   Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA   Indest K.J., Eltis L.D.;
RT   "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT   trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL   Appl. Environ. Microbiol. 78:7798-7800(2012).
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879}.
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DR   EMBL; CP002907; AFR49022.1; -; Genomic_DNA.
DR   RefSeq; WP_014926745.1; NC_018581.1.
DR   AlphaFoldDB; J9RKY8; -.
DR   STRING; 337191.KTR9_2385; -.
DR   KEGG; gor:KTR9_2385; -.
DR   PATRIC; fig|337191.3.peg.2703; -.
DR   eggNOG; COG2241; Bacteria.
DR   eggNOG; COG2242; Bacteria.
DR   HOGENOM; CLU_031955_0_0_11; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000003281; Chromosome.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd11644; Precorrin-6Y-MT; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR012818; CbiE.
DR   InterPro; IPR006365; Cbl_synth_CobL.
DR   InterPro; IPR014008; Cbl_synth_MTase_CbiT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR02467; CbiE; 1.
DR   NCBIfam; TIGR02469; CbiT; 1.
DR   PANTHER; PTHR43182; COBALT-PRECORRIN-6B C(15)-METHYLTRANSFERASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR43182:SF1; COBALT-PRECORRIN-7 C(5)-METHYLTRANSFERASE; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036428; CobL; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AFR49022.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFR49022.1}.
FT   DOMAIN          17..210
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   432 AA;  45301 MW;  BC56324E9A413582 CRC64;
     MRSPGAAVTS TVPTSEFVVV GIGADGWPGL GEPARDELRH ARVIYGAARQ LALLDGAAPR
     LGAQLRPWRS PMSEHLAELV ETGGVDDAHP DTVHILASGD PMFHGVGASI VARVGADRVR
     VYPAVSSASL ACARLGWDLA TTRIVSAVRT EPGVVLGEVT DGARVLVLSR DETTPAAVAE
     LLTDAGFGAS AMTVLEQLGG PAEQIATDTA EGWHRRAGDS LNIVAVDCVG PHRTRLPGRA
     DEAYEHDGQI TKSTIRALTV CALEPAGAQI LWDIGAGSGS VAIEWLRADD RGLAVAFERD
     PERADRLRRN AARHGVAHRL SVRGPAPDEL AAAPQPDAVF IGGGLDEEIL ALAWDALADS
     GRLVVNAVTV ENQALVTQRH ADQGGTLRRL SVETVAPLGT MTTWRPALPI VQWSVDKPTT
     GLPDAGLAEA VR
//
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