ID A0A0D8FXZ6_9ACTN Unreviewed; 558 AA.
AC A0A0D8FXZ6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Cobalt-precorrin-3B C(17)-methyltransferase {ECO:0000313|EMBL:KJE78026.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:KJE78026.1};
GN Name=cbiH {ECO:0000313|EMBL:KJE78026.1};
GN ORFNames=FEAC_00150 {ECO:0000313|EMBL:KJE78026.1};
OS Ferrimicrobium acidiphilum DSM 19497.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Ferrimicrobium.
OX NCBI_TaxID=1121877 {ECO:0000313|EMBL:KJE78026.1, ECO:0000313|Proteomes:UP000032336};
RN [1] {ECO:0000313|EMBL:KJE78026.1, ECO:0000313|Proteomes:UP000032336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T23 {ECO:0000313|EMBL:KJE78026.1,
RC ECO:0000313|Proteomes:UP000032336};
RA Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT "Draft genome of the acidophilic iron oxidizer Ferrimicrobium acidiphilum
RT strain T23.";
RL Submitted (JAN-2015) 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:KJE78026.1}.
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DR EMBL; JXUW01000001; KJE78026.1; -; Genomic_DNA.
DR RefSeq; WP_052564982.1; NZ_JXUW01000001.1.
DR AlphaFoldDB; A0A0D8FXZ6; -.
DR STRING; 1121877.FEAC_00150; -.
DR GeneID; 78371380; -.
DR PATRIC; fig|1121877.4.peg.16; -.
DR eggNOG; COG1010; Bacteria.
DR eggNOG; COG2073; Bacteria.
DR OrthoDB; 9804789at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000032336; 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 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KJE78026.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032336};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KJE78026.1}.
FT DOMAIN 41..115
FT /note="Cobalamin synthesis G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11760"
FT DOMAIN 196..310
FT /note="CobE/GbiG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01890"
FT DOMAIN 319..523
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 558 AA; 58859 MW; ADABF59C006289C0 CRC64;
MTSTQFTNGI VLSLATPPYG LAAQLGFREI AFAKFGDLVD ALTHHRAVVI IAAYPIVVRA
LAQTLSTKGD DPAVVAIDES TSFVTVLAGA HHGGEPLARQ VADYLGATPV ITTASSALDT
IALDQTPQLC FGQMNAGIQA RVNRGDGISL VNPTDLVLSD AIMNLVHDGS SPVKLVISDR
LADEQLGDVR GSVKTLTIGV GCSSDATADE VNELINTVVH SAGLDIAAID RIATIDRRLD
HPALRGLHRE LVGYGAAQLD VMTTPSPSTI VHQSVGTHSV AEAAALLASG EGGSLIVNKV
KTARVTVAIA RRRSLRGSLA VVGIGPGSLD LLTPRAFAAL RSAQYVIGFS RYLDLIEPII
ERGQELHRYP IGQEIERVAE SLALAARGNH VALVTSGDPA VYAMAQLVVE RLSPDVAIRV
IPGVTAAYAA SSTAGAIVGH DHAMISLSDL LTPWSIIENR IAAAAEADFV IAFYNPRSKQ
RSWQLEKALA LIGEHRRPTT PVLIASRVER AGARVTVTTL EDLDPESVDM ETIVIVGATT
TALRHGYLYT PRGYQGTP
//
