ID L7FE25_9ACTN Unreviewed; 245 AA.
AC L7FE25;
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-2 C(20)-methyltransferase {ECO:0000313|EMBL:ELP69618.1};
DE EC=2.1.1.130 {ECO:0000313|EMBL:ELP69618.1};
GN Name=cobI {ECO:0000313|EMBL:ELP69618.1};
GN ORFNames=STRTUCAR8_02694 {ECO:0000313|EMBL:ELP69618.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP69618.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP69618.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP69618.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
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:ELP69618.1}.
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DR EMBL; AEJB01000131; ELP69618.1; -; Genomic_DNA.
DR AlphaFoldDB; L7FE25; -.
DR STRING; 85558.T45_08000; -.
DR PATRIC; fig|698760.3.peg.1687; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000010931; Unassembled WGS sequence.
DR GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:UniProtKB-EC.
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:ELP69618.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELP69618.1}.
FT DOMAIN 6..215
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 245 AA; 25373 MW; ADA8071D36D01F1F CRC64;
MSSINRLVGV GVGPGDPELV TVKGVNALRA ADVIVVPVMD TLERGRAEAT VLHYVPAEKI
VRVVFALNER SDHARREAAW DAAGARVAEL LGAHSVVAFA TIGDPNVYST FTYLAHTIGR
LVPSVVVETV PGITAMQDLA ARSGAVLTEG TEPLTLVPVT AGAAVLKEAL SGPGTVVAYK
FGRQAQEVAE ALRESGRIGD AVWGSALGLE DESIRPAAEL DGAPLPYLST LIAPAPRDGG
RGGKL
//
