ID L0H3P1_9GAMM Unreviewed; 417 AA.
AC L0H3P1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Precorrin-6y C5,15-methyltransferase (Decarboxylating), CbiE subunit,precorrin-6Y C5,15-methyltransferase (Decarboxylating), CbiT subunit {ECO:0000313|EMBL:AGA92209.1};
GN ORFNames=Thimo_3552 {ECO:0000313|EMBL:AGA92209.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA92209.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA92209.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA92209.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
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DR EMBL; CP003051; AGA92209.1; -; Genomic_DNA.
DR AlphaFoldDB; L0H3P1; -.
DR STRING; 765912.Thimo_3552; -.
DR KEGG; tmb:Thimo_3552; -.
DR PATRIC; fig|765912.4.peg.3481; -.
DR eggNOG; COG2241; Bacteria.
DR eggNOG; COG2242; Bacteria.
DR HOGENOM; CLU_031955_0_0_6; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000010816; 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; cd02440; AdoMet_MTases; 1.
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 4: Predicted;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AGA92209.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010816};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGA92209.1}.
FT DOMAIN 20..204
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 417 AA; 43712 MW; C55391756AC403B2 CRC64;
MRRGELVMKD PQSGRVAPWL SIIGVGEDGV EGLGDAAREL ISAAELVVAG RRHLELAAPL
IRGETRVWAS PLAATLPELL ARRGRPVAVL ASGDPFHFGV GATLARHVAP AEMRVLPQPS
SLSLAAARLG VALQDCAVVS LCGRPLATLR PALQPGARVL VLSADGETPR AVCAALADWG
LGASRVTVLE ALGGPRERRR TCAAETYDLA DVDPLNLLAI EVAAGPGVRV LPHAPGLPDD
WFEHDGQITK REVRALTLSS LRPMAGELLW DIGCGSGSVA IEWLLAHPGT RAIALDADVE
RATRAGRNAE RLGVPHLEVR VGRAPEALAG LPAPAAIFIG GGARDRILID ACWAALPRGG
RLVVNAVALE TQQALVSVWQ DHGGELCRLS LERPGPLGGL HALRPALPII HWAGVKA
//
