ID   CBIG_PRIMG              Reviewed;         374 AA.
AC   O87697;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Cobalt-precorrin-5A hydrolase;
DE            EC=3.7.1.12;
GN   Name=cbiG;
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=16866557; DOI=10.1021/ja062940a;
RA   Kajiwara Y., Santander P.J., Roessner C.A., Perez L.M., Scott A.I.;
RT   "Genetically engineered synthesis and structural characterization of
RT   cobalt-precorrin 5A and -5B, two new intermediates on the anaerobic pathway
RT   to vitamin B12: definition of the roles of the CbiF and CbiG enzymes.";
RL   J. Am. Chem. Soc. 128:9971-9978(2006).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the ring A acetate delta-lactone
CC       of cobalt-precorrin-5A resulting in the loss of the C-20 carbon and its
CC       attached methyl group in the form of acetaldehyde.
CC       {ECO:0000269|PubMed:16866557}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co-precorrin-5A + H2O = acetaldehyde + Co-precorrin-5B + H(+);
CC         Xref=Rhea:RHEA:26281, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:60062, ChEBI:CHEBI:60063; EC=3.7.1.12;
CC         Evidence={ECO:0000269|PubMed:16866557};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC       step 5/10.
CC   -!- SIMILARITY: Belongs to the CbiG family. {ECO:0000305}.
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DR   EMBL; AJ000758; CAA04315.1; -; Genomic_DNA.
DR   PIR; T44691; T44691.
DR   AlphaFoldDB; O87697; -.
DR   SMR; O87697; -.
DR   BRENDA; 3.7.1.12; 656.
DR   UniPathway; UPA00148; UER00561.
DR   GO; GO:0043779; F:cobalt-precorrin-5A acetaldehyde-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.420.180; -; 1.
DR   InterPro; IPR021745; CbiG_mid.
DR   InterPro; IPR021744; CbiG_N.
DR   InterPro; IPR002750; CobE/GbiG_C.
DR   InterPro; IPR036518; CobE/GbiG_C_sf.
DR   InterPro; IPR038029; GbiG_N_sf.
DR   Pfam; PF01890; CbiG_C; 1.
DR   Pfam; PF11761; CbiG_mid; 1.
DR   Pfam; PF11760; CbiG_N; 1.
DR   SUPFAM; SSF159664; SSF159664; 1.
DR   SUPFAM; SSF159672; SSF159672; 1.
PE   1: Evidence at protein level;
KW   Cobalamin biosynthesis; Hydrolase.
FT   CHAIN           1..374
FT                   /note="Cobalt-precorrin-5A hydrolase"
FT                   /id="PRO_0000429641"
SQ   SEQUENCE   374 AA;  41125 MW;  CED8E56B2CC9C4E4 CRC64;
     MIQLEEGKKA PITQRGDYAV VAITKHGVEI ARNLGRIFQQ SDVYYMSKFE KGDEQEQNIQ
     MFSGSVRMLL PSLFESYKGL IIIISLGAVV RMIAPILKDK KTDPAVVVID DKGENVISVL
     SGHIGGANEL TREVAAALRA HPVITTASDV QKTIPVDLFG KRFGWVWESA ENVTPVSASV
     VNEEEIAVVQ ESGEKSWWHY EHPVPANIKT YSSIQTALEA SPHAALVVTH RDLKKEEEAI
     LENGVLYRPK VLAIGMGCNR GTSAAEIETV IEKTLAELQF SMKSVKALCT IELKKDEEGL
     LEVASKYGWE FVYYSPQELN SISIQQPSDT VFKYTGAYGV SEPAAMLYSG ADTLELVKKK
     SGNVTISVAL IPYD