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Database: UniProt
Entry: L1KJS0_9ACTN
LinkDB: L1KJS0_9ACTN
Original site: L1KJS0_9ACTN 
ID   L1KJS0_9ACTN            Unreviewed;       590 AA.
AC   L1KJS0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Precorrin-3B C(17)-methyltransferase {ECO:0000313|EMBL:EKX61071.1};
DE            EC=2.1.1.131 {ECO:0000313|EMBL:EKX61071.1};
GN   Name=cobJ {ECO:0000313|EMBL:EKX61071.1};
GN   ORFNames=STRIP9103_01959 {ECO:0000313|EMBL:EKX61071.1};
OS   Streptomyces ipomoeae 91-03.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX61071.1, ECO:0000313|Proteomes:UP000010411};
RN   [1] {ECO:0000313|EMBL:EKX61071.1, ECO:0000313|Proteomes:UP000010411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91-03 {ECO:0000313|EMBL:EKX61071.1,
RC   ECO:0000313|Proteomes:UP000010411};
RA   Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL   Submitted (NOV-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|ARBA:ARBA00005879}.
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:EKX61071.1}.
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DR   EMBL; AEJC01000621; EKX61071.1; -; Genomic_DNA.
DR   RefSeq; WP_009338045.1; NZ_AEJC01000621.1.
DR   AlphaFoldDB; L1KJS0; -.
DR   PATRIC; fig|698759.3.peg.8246; -.
DR   OrthoDB; 9804789at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000010411; Unassembled WGS sequence.
DR   GO; GO:0030789; F:precorrin-3B C17-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd11646; Precorrin_3B_C17_MT; 1.
DR   Gene3D; 3.40.50.11220; -; 1.
DR   Gene3D; 3.30.420.180; CobE/GbiG C-terminal domain; 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; IPR021744; CbiG_N.
DR   InterPro; IPR006363; Cbl_synth_CobJ/CibH_dom.
DR   InterPro; IPR002750; CobE/GbiG_C.
DR   InterPro; IPR036518; CobE/GbiG_C_sf.
DR   InterPro; IPR038029; GbiG_N_sf.
DR   NCBIfam; TIGR01466; cobJ_cbiH; 1.
DR   PANTHER; PTHR47036; COBALT-FACTOR III C(17)-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR47036:SF1; COBALT-FACTOR III C(17)-METHYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF01890; CbiG_C; 1.
DR   Pfam; PF11760; CbiG_N; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF159672; CbiG N-terminal domain-like; 1.
DR   SUPFAM; SSF159664; CobE/GbiG C-terminal domain-like; 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:EKX61071.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010411};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKX61071.1}.
FT   DOMAIN          36..116
FT                   /note="Cobalamin synthesis G N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11760"
FT   DOMAIN          202..323
FT                   /note="CobE/GbiG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01890"
FT   DOMAIN          331..536
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   REGION          568..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  60982 MW;  6BC45CDB5B5225FC CRC64;
     MIGLISATAA GAVAAQRLAS AWPERTRVYE GPVRDAVRRA FGECEQLVCF LATGATVRVL
     APLLADKATD PGVVCVDEGG RFAVSLIGGH GGGANELARE VGELLGAEPV ITTATDAVGV
     PGLDTLGLPV EGDVAGVSRA VLDGEAVELD LEIGWPLPAL PSNVGHSASQ RSRAPRQAPV
     IRVTDRVLEP AEGQVVLRPP SLVVGVGASK GAPVDEVLAL VEKALHDAGL SPKSLAEIAT
     VDAKADEPGI VEAAERLGVP LVTHSAEELA AVEVPNPSDA PLAAVGTPSV AEAAALVRGG
     ELLVAKRKSE RADGRPAMAT CAVVRRPARG RLAVVGLGPG ARDLLTPRAK AELQGASVLV
     GLDQYVDQIR DLLRPGTRVL ESGLGAEEER ARTAVAQARK GYAVALIGSG DAGVYAMASP
     ALAEASDDID VIGVPGVTAA LAAAAILGAP LGHDHVSISL SDLHTPWEVI ERRVRAAAEA
     DIVVTFYNPR SRGRDWQLPK ALAILAEHRE PTTPVGVVRQ ASRPDESARV TTLAALDPAT
     VDMMTVVTVG NTASRTIAGR MVTPRGYRWQ TDTQTEPRTK TRTKTQEAAG
//
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