CBIH_PRIMG
ID CBIH_PRIMG Reviewed; 540 AA.
AC O87689;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Cobalt-factor III methyltransferase;
DE EC=2.1.1.272;
DE AltName: Full=Cobalt-precorrin-3 methylase;
GN Name=cbiH60;
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, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF CYS-402 AND
RP CYS-443.
RC STRAIN=DSM 509 / CCM 1464 / NBRC 12109;
RX PubMed=23155054; DOI=10.1074/jbc.m112.422535;
RA Moore S.J., Biedendieck R., Lawrence A.D., Deery E., Howard M.J.,
RA Rigby S.E., Warren M.J.;
RT "Characterization of the enzyme CbiH60 involved in anaerobic ring
RT contraction of the cobalamin (vitamin B12) biosynthetic pathway.";
RL J. Biol. Chem. 288:297-305(2013).
CC -!- FUNCTION: Methyltransferase that catalyzes the reduction, ring
CC contraction and methylation of C-17 in cobalt-factor III to form
CC cobalt-precorrin-4. Is also able to convert cobalt-precorrin-3 to
CC cobalt-precorrin-4. {ECO:0000269|PubMed:23155054}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + Co(II)-factor III + S-adenosyl-L-methionine = A + Co-
CC precorrin-4 + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:36155,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:60061, ChEBI:CHEBI:73299;
CC EC=2.1.1.272; Evidence={ECO:0000269|PubMed:23155054};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:23155054};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:23155054};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC -!- SIMILARITY: In the N-terminal section; belongs to the precorrin
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AJ000758; CAA04307.1; -; Genomic_DNA.
DR PIR; T44683; T44683.
DR AlphaFoldDB; O87689; -.
DR SMR; O87689; -.
DR PRIDE; O87689; -.
DR BioCyc; MetaCyc:MON-17924; -.
DR BRENDA; 2.1.1.272; 656.
DR UniPathway; UPA00148; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase 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; cd11646; Precorrin_3B_C17_MT; 1.
DR Gene3D; 3.30.413.10; -; 1.
DR Gene3D; 3.30.950.10; -; 1.
DR Gene3D; 3.40.1010.10; -; 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; IPR006363; Cbl_synth_CobJ/CibH_dom.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR01466; cobJ_cbiH; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cobalamin biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..540
FT /note="Cobalt-factor III methyltransferase"
FT /id="PRO_0000430346"
FT BINDING 402
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 405
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 439
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 443
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT MUTAGEN 402
FT /note="C->A: No iron-sulfur cluster formed. Low activity
FT with cobalt-factor III as substrate. Normal activity with
FT Co-precorrin 3."
FT /evidence="ECO:0000269|PubMed:23155054"
FT MUTAGEN 443
FT /note="C->A: No iron-sulfur cluster formed. Low activity
FT with cobalt-factor III as substrate. Normal activity with
FT Co-precorrin 3."
FT /evidence="ECO:0000269|PubMed:23155054"
SQ SEQUENCE 540 AA; 59510 MW; 090C6C1B15E0C9E1 CRC64;
MKGKLLVIGF GPGSFEHITQ RAREAIQESD MIIGYKTYVE LIQGLLTNQQ IISTGMTEEV
SRAQEAVKQA EAGKTVAVIS SGDAGVYGMA GLVYEVLIEK GWKKETGVEL EVIPGISAIN
SCASLLGAPV MHDACTISLS DHLTPWELIE KRIEAAAQAD FVVAFYNPKS GRRTRQIVEA
QRILLKYRSP DTPVGLVKSA YRDREEVVMT NLKDMLNHEI GMLTTVVVGN SSTFFYDDLM
ITPRGYQRKY TLNQTEQPLR PHQRLRKEAE PWALDQEEAV KQSASAIEAV QNTREETAAS
RALAEEALQA ILGESTSAVV HQPIESIFEV AVSPGLANKK FTPVQMTTLA EVVGEKGTME
YTPDHQIKLQ IPTAHPDMII EKLQAASFLL SPVGDVFTIK ACDFCDGEKS DAIPHTEELQ
KRLGGMDMPK ELKLGINGCG MACYGAVQED IGIVYRKGAF DLFLGAKTVG RNAHSGQIVA
EGIAPDDIVE IVENIIHEYK EKGHPNERFH KFFKRVKNVY GFDYQDITPK IKVEPAPCGD
