ID   PDUO_MYCLE              Reviewed;         191 AA.
AC   P53523;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Corrinoid adenosyltransferase;
DE            EC=2.5.1.17;
DE   AltName: Full=Cob(II)alamin adenosyltransferase;
DE   AltName: Full=Cob(II)yrinic acid a,c-diamide adenosyltransferase;
DE   AltName: Full=Cobinamide/cobalamin adenosyltransferase;
GN   OrderedLocusNames=ML1149; ORFNames=u471a;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + 2 cob(II)yrinate a,c diamide + reduced [electron-
CC         transfer flavoprotein] = 2 adenosylcob(III)yrinate a,c-diamide + 3
CC         H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate;
CC         Xref=Rhea:RHEA:11528, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:58503,
CC         ChEBI:CHEBI:58537; EC=2.5.1.17;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + 2 cob(II)alamin + reduced [electron-transfer
CC         flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized
CC         [electron-transfer flavoprotein] + 2 triphosphate;
CC         Xref=Rhea:RHEA:28671, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16304, ChEBI:CHEBI:18036,
CC         ChEBI:CHEBI:18408, ChEBI:CHEBI:30616, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307; EC=2.5.1.17;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U15186; AAA63097.1; -; Genomic_DNA.
DR   EMBL; AL583920; CAC31530.1; -; Genomic_DNA.
DR   PIR; T09970; T09970.
DR   RefSeq; NP_301843.1; NC_002677.1.
DR   RefSeq; WP_010908167.1; NC_002677.1.
DR   AlphaFoldDB; P53523; -.
DR   SMR; P53523; -.
DR   STRING; 272631.ML1149; -.
DR   PRIDE; P53523; -.
DR   EnsemblBacteria; CAC31530; CAC31530; CAC31530.
DR   KEGG; mle:ML1149; -.
DR   PATRIC; fig|272631.5.peg.2072; -.
DR   Leproma; ML1149; -.
DR   eggNOG; COG2096; Bacteria.
DR   HOGENOM; CLU_083486_0_0_11; -.
DR   OMA; HQACTVV; -.
DR   UniPathway; UPA00148; UER00233.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide adenosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1200.10; -; 1.
DR   InterPro; IPR016030; CblAdoTrfase-like.
DR   InterPro; IPR036451; CblAdoTrfase-like_sf.
DR   InterPro; IPR029499; PduO-typ.
DR   PANTHER; PTHR12213; PTHR12213; 1.
DR   Pfam; PF01923; Cob_adeno_trans; 1.
DR   SUPFAM; SSF89028; SSF89028; 1.
DR   TIGRFAMs; TIGR00636; PduO_Nterm; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cobalamin biosynthesis; Cytoplasm; Nucleotide-binding;
KW   Porphyrin biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..191
FT                   /note="Corrinoid adenosyltransferase"
FT                   /id="PRO_0000103800"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         140..145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   191 AA;  20916 MW;  6403BB0AB249F175 CRC64;
     MAIHLTRIYT RTGDNGTTGL SDFSRVAKTD LRLVAYADCD ETNSAIGVAL ALGNPDQKIT
     DVLQQIQNDL FDAGADLSTP MQDSVRNPEY PQLRITQTHI DRLEEWCDTY NTPLPTLNSF
     VLPGGSPLSA LLHVARTVAR RAERSAWAAV EAHPGVVSML PAKYLNRLSD LLFILSRVAN
     TGNDVLWRPG G