ID   CBIZ_METMA              Reviewed;         200 AA.
AC   Q8Q0G3;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Adenosylcobinamide amidohydrolase;
DE            Short=AdoCbi hydrolase;
DE            EC=3.5.1.90;
GN   Name=cbiZ; OrderedLocusNames=MM_0173;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=14990804; DOI=10.1073/pnas.0305939101;
RA   Woodson J.D., Escalante-Semerena J.C.;
RT   "CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B12
RT   precursor cobinamide in archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:3591-3596(2004).
CC   -!- FUNCTION: Converts adenosylcobinamide (AdoCbi) to adenosylcobyric acid
CC       (AdoCby), an intermediate of the de novo coenzyme B12 biosynthetic
CC       route. {ECO:0000269|PubMed:14990804}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosylcob(III)inamide + H2O = (R)-1-aminopropan-2-ol +
CC         adenosylcob(III)yrate; Xref=Rhea:RHEA:23504, ChEBI:CHEBI:2480,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:42677, ChEBI:CHEBI:58504; EC=3.5.1.90;
CC   -!- PATHWAY: Cofactor biosynthesis; dicyanocobinamide salvage pathway.
CC   -!- SIMILARITY: Belongs to the CbiZ family. {ECO:0000305}.
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DR   EMBL; AE008384; AAM29869.1; -; Genomic_DNA.
DR   RefSeq; WP_011032127.1; NC_003901.1.
DR   AlphaFoldDB; Q8Q0G3; -.
DR   STRING; 192952.MM_0173; -.
DR   EnsemblBacteria; AAM29869; AAM29869; MM_0173.
DR   GeneID; 44086656; -.
DR   GeneID; 66135107; -.
DR   KEGG; mma:MM_0173; -.
DR   PATRIC; fig|192952.21.peg.207; -.
DR   eggNOG; arCOG01870; Archaea.
DR   HOGENOM; CLU_077662_1_0_2; -.
DR   OMA; SNAPHRG; -.
DR   BioCyc; MetaCyc:MON-14880; -.
DR   BRENDA; 3.5.1.90; 3270.
DR   UniPathway; UPA00297; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0043756; F:adenosylcobinamide hydrolase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR002808; AdoCbi_amidolase.
DR   Pfam; PF01955; CbiZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..200
FT                   /note="Adenosylcobinamide amidohydrolase"
FT                   /id="PRO_0000220407"
SQ   SEQUENCE   200 AA;  21713 MW;  9B2A731CE49AC907 CRC64;
     MQYHIKDQTL IIKGDFEAVS TGLNGGRARV EYIFNKQVPR TFNPPSPEEF IREEARKDGI
     ETASLGLLTA VNMEYLQVIE DDYMTAFITA GVSNCSEFRA KAGTINIILV SKARLSETAL
     FGAIITATEA KGLALLEKGY NFLGTNTDAV IVAYETCSDS GPKSKTNQEI PYAGSSTEFG
     KKITEAVIKG IKAGLELRGE