ID A0A164BUF9_9SYNE Unreviewed; 629 AA.
AC A0A164BUF9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Cobalt-precorrin-3B C(17)-methyltransferase {ECO:0000313|EMBL:KZR89270.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:KZR89270.1};
GN Name=cbiH {ECO:0000313|EMBL:KZR89270.1};
GN ORFNames=MITS9508_01411 {ECO:0000313|EMBL:KZR89270.1};
OS Synechococcus sp. MIT S9508.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1801629 {ECO:0000313|EMBL:KZR89270.1, ECO:0000313|Proteomes:UP000076799};
RN [1] {ECO:0000313|EMBL:KZR89270.1, ECO:0000313|Proteomes:UP000076799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT S9508 {ECO:0000313|EMBL:KZR89270.1,
RC ECO:0000313|Proteomes:UP000076799};
RA Cubillos-Ruiz A., Berta-Thompson J.W., Becker J.W., Chisholm S.W.;
RT "Evolutionary Radiation of Lanthipeptides in Marine Picocyanobacteria.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
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:KZR89270.1}.
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DR EMBL; LVHU01000006; KZR89270.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164BUF9; -.
DR STRING; 1801629.MITS9508_01411; -.
DR PATRIC; fig|1801629.3.peg.1505; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000076799; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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 4: Predicted;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KZR89270.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZR89270.1}.
FT DOMAIN 77..154
FT /note="Cobalamin synthesis G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11760"
FT DOMAIN 245..370
FT /note="CobE/GbiG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01890"
FT DOMAIN 383..592
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 629 AA; 66511 MW; D672F0E327F836F5 CRC64;
MAPSADSLRP LALNAVDTTF IQLMEAPLAL GLSVSAWPLL QQLQQAGQAD RVGLTPLAAA
ALQTSPSDLL VAPAAEFLSD QWRRGGPTIV IGAMGAVTRL IAPLLSGKQN DPAVVVMDAH
GQNIVPLIGG HAAGAEQLAH ALAAALGGQV VLTGDAASQE RLALDAFGEA WGWVRGGTPE
AWHDLMLSQA SGPSLNVVQQ TGTDLWRSST AGQHFGVTAD SEHGIALAIG PRSDGAPCRW
HPATLWIGIG CERLSCLALI QRAVDRSLQS AGLAKESVAG ISSIEAKGDE PALLEFCEHQ
NWPLRLFGAA ALADVAVPTP SEVVKAEMGT ASVAEASAVL ASGDGAKLLH SKRIFHAEGG
EQGAVTVAIA EAAHPLAANK GELHLVGSGP GSLQLLTADA RTALSRCVLW VGYGLYLDLL
EPLRRCDQVR LDGQLTRERD RCWQALDLAR QGARVALISS GDSGIYGMAG LALELWMDLP
ETERPRFQVH PGLSALQLAA ARAGAPLMHD FCTISLSDRL TPWQVIERRI EAAASGDFVV
AIYNPRSRDR NWQLTRAREI LLCARPETTP VVMARQLGRS DEQVSLHSLG KLRPEDVDML
TVLVIGNSSS RVQDGRMVTP RGYPGATLN
//
