CBIG_METJA
ID CBIG_METJA Reviewed; 323 AA.
AC Q58544;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable cobalt-precorrin-5A hydrolase;
DE EC=3.7.1.12;
GN Name=cbiG; OrderedLocusNames=MJ1144;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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. {ECO:0000250}.
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 -!- 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; L77117; AAB99144.1; -; Genomic_DNA.
DR PIR; G64442; G64442.
DR AlphaFoldDB; Q58544; -.
DR SMR; Q58544; -.
DR STRING; 243232.MJ_1144; -.
DR PRIDE; Q58544; -.
DR EnsemblBacteria; AAB99144; AAB99144; MJ_1144.
DR KEGG; mja:MJ_1144; -.
DR eggNOG; arCOG00651; Archaea.
DR HOGENOM; CLU_028397_0_0_2; -.
DR InParanoid; Q58544; -.
DR OMA; GIGCNRG; -.
DR PhylomeDB; Q58544; -.
DR UniPathway; UPA00148; UER00561.
DR Proteomes; UP000000805; Chromosome.
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; 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; PF11760; CbiG_N; 1.
DR SUPFAM; SSF159664; SSF159664; 1.
DR SUPFAM; SSF159672; SSF159672; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Hydrolase; Reference proteome.
FT CHAIN 1..323
FT /note="Probable cobalt-precorrin-5A hydrolase"
FT /id="PRO_0000107187"
SQ SEQUENCE 323 AA; 37500 MW; E6476F3F39DDBCE4 CRC64;
MMIKIVYITK RGKKIAEEIK DVLDYYHYDN KVEPIKDFKI ERNEGGFIFI MATGIVLRKF
LDEIKNDKFK DPFVIICNEN KELIPILSNH LGGGNYFSKL IANNINGRVI FTTATDVNGK
VGIDELSKML FLETPKRKHI LDINKKILEE DVSLTLPKYW KLRNLNGYKI SYHDKYEVVV
DDSIRLKPLK IAVGLGARKG IERYKVYWAV KKALFLRNIP VWRVDAFATI EDKKHERGIL
ETVNKFKKPL IIFKREEINE IYEKIDLEKS EFVYKHLGVY GVSEPASILA VKKLTNKDFD
SIKLILKKFK RNGVTVAIAT ENL