ID   CBIET_PRIMG             Reviewed;         398 AA.
AC   O87694;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Cobalamin biosynthesis bifunctional protein CbiET;
DE   Includes:
DE     RecName: Full=Cobalt-precorrin-7 C(5)-methyltransferase;
DE              EC=2.1.1.289;
DE   Includes:
DE     RecName: Full=Cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating);
DE              EC=2.1.1.196;
GN   Name=cbiET;
OS   Priestia megaterium (Bacillus megaterium).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 509 / CCM 1464 / NBRC 12109;
RX   PubMed=9742225; DOI=10.1042/bj3350159;
RA   Raux E., Lanois A., Warren M.J., Rambach A., Thermes C.;
RT   "Cobalamin (vitamin B12) biosynthesis: identification and characterization
RT   of a Bacillus megaterium cobI operon.";
RL   Biochem. J. 335:159-166(1998).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=23922391; DOI=10.1073/pnas.1308098110;
RA   Moore S.J., Lawrence A.D., Biedendieck R., Deery E., Frank S., Howard M.J.,
RA   Rigby S.E., Warren M.J.;
RT   "Elucidation of the anaerobic pathway for the corrin component of cobalamin
RT   (vitamin B12).";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:14906-14911(2013).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the methylation of C-15 in
CC       cobalt-precorrin-6B followed by the decarboxylation of C-12 to form
CC       cobalt-precorrin-7, and then methylates cobalt-precorrin-7 at C-5 to
CC       form cobalt-precorrin-8. {ECO:0000269|PubMed:23922391}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-7 + S-adenosyl-L-methionine = Co-precorrin-8X +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:34591,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:70791, ChEBI:CHEBI:70792; EC=2.1.1.289;
CC         Evidence={ECO:0000269|PubMed:23922391};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 +
CC         CO2 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36067,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:70791, ChEBI:CHEBI:72780; EC=2.1.1.196;
CC         Evidence={ECO:0000269|PubMed:23922391};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 8/10.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the precorrin
CC       methyltransferase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the methyltransferase
CC       superfamily. Bacterial-type CbiT family. {ECO:0000305}.
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DR   EMBL; AJ000758; CAA04312.1; -; Genomic_DNA.
DR   PIR; T44688; T44688.
DR   AlphaFoldDB; O87694; -.
DR   SMR; O87694; -.
DR   UniPathway; UPA00148; UER00229.
DR   GO; GO:0043776; F:cobalt-precorrin-6B C5-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0043777; F:cobalt-precorrin-7 C15-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd11644; Precorrin-6Y-MT; 1.
DR   Gene3D; 3.30.950.10; -; 1.
DR   Gene3D; 3.40.1010.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 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   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036428; CobL; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR02467; CbiE; 1.
DR   TIGRFAMs; TIGR02469; CbiT; 1.
PE   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Methyltransferase; Multifunctional enzyme;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..398
FT                   /note="Cobalamin biosynthesis bifunctional protein CbiET"
FT                   /id="PRO_0000429631"
FT   REGION          1..205
FT                   /note="Cobalt-precorrin-7 C(5)-methyltransferase"
FT   REGION          206..398
FT                   /note="Cobalt-precorrin-6B C(15)-methyltransferase
FT                   (decarboxylating)"
FT   BINDING         227
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         251..255
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  44023 MW;  3244092321A62536 CRC64;
     MAIKIIGIGD DGKLSLLPMY EQWIYESDVL IGGKRHLDFF QDFQGEKVAI EGGLSSLVER
     LKNEEGNAVV LASGDPLFYG IGSYLSTKLD VEIYPYLSSI QLAFSRLKER WQDAYFTSVH
     GRSIKGLAQR IDGYKKVAIL TDEQNSPTAL ANYLLSFGMT EYKMFVAENL GGETERCQLL
     SLEEAANQFF SPLNVVILKQ VEESPVWPLG IEDDEFIQRK PDKGLITKKE IRTLSISALQ
     LKRDSVVWDI GTCTGSVAIE AAKIAREGQI FAVEKNEADL ENCRENLAKF RVDAHTVHGK
     APEGLNEFAD PDAVFIGGTA GGMETILDVC CSRLNSGGRI VLNAVTIENL AEAMKAFKER
     GFETAVTLAQ ISRSKPILHL TRFDALNPIY IITAKRGE