CBIF_PRIMG
ID CBIF_PRIMG Reviewed; 258 AA.
AC O87696;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Cobalt-precorrin-4 C(11)-methyltransferase;
DE EC=2.1.1.271;
DE AltName: Full=Cobalt-precorrin-3 methylase;
GN Name=cbiF;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9660189; DOI=10.1046/j.1432-1327.1998.2540341.x;
RA Raux E., Schubert H.L., Woodcock S.C., Wilson K.S., Warren M.J.;
RT "Cobalamin (vitamin B12) biosynthesis -- cloning, expression and
RT crystallisation of the Bacillus megaterium S-adenosyl-L-methionine-
RT dependent cobalt-precorrin-4 transmethylase CbiF.";
RL Eur. J. Biochem. 254:341-346(1998).
CC -!- FUNCTION: Catalyzes the methylation of C-11 in cobalt-precorrin-4 to
CC form cobalt-precorrin-5A. {ECO:0000269|PubMed:23922391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-precorrin-4 + S-adenosyl-L-methionine = Co-precorrin-5A +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:26277,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:60061, ChEBI:CHEBI:60062; EC=2.1.1.271;
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 4/10.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AJ000758; CAA04314.1; -; Genomic_DNA.
DR PIR; T44690; T44690.
DR PDB; 1CBF; X-ray; 2.40 A; A=1-242.
DR PDB; 2CBF; X-ray; 3.10 A; A=1-231.
DR PDBsum; 1CBF; -.
DR PDBsum; 2CBF; -.
DR AlphaFoldDB; O87696; -.
DR SMR; O87696; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR BRENDA; 2.1.1.271; 656.
DR UniPathway; UPA00148; UER00226.
DR EvolutionaryTrace; O87696; -.
DR GO; GO:0046026; F:precorrin-4 C11-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; cd11641; Precorrin-4_C11-MT; 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; IPR006362; Cbl_synth_CobM/CibF.
DR InterPro; IPR003043; Uropor_MeTrfase_CS.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR TIGRFAMs; TIGR01465; cobM_cbiF; 1.
DR PROSITE; PS00839; SUMT_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin biosynthesis; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..258
FT /note="Cobalt-precorrin-4 C(11)-methyltransferase"
FT /id="PRO_0000150392"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1CBF"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:1CBF"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1CBF"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:1CBF"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2CBF"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:1CBF"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:1CBF"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1CBF"
SQ SEQUENCE 258 AA; 28452 MW; 59C2E7FF9FAF1D03 CRC64;
MKLYIIGAGP GDPDLITVKG LKLLQQADVV LYADSLVSQD LIAKSKPGAE VLKTAGMHLE
EMVGTMLDRM REGKMVVRVH TGDPAMYGAI MEQMVLLKRE GVDIEIVPGV TSVFAAAAAA
EAELTIPDLT QTVILTRAEG RTPVPEFEKL TDLAKHKCTI ALFLSATLTK KVMKEFINAG
WSEDTPVVVV YKATWPDEKI VRTTVKDLDD AMRTNGIRKQ AMILAGWALD PHIHDKDYRS
KLYDKTFTHG FRKGVKSE
