ID   PDUO_MYCBO              Reviewed;         193 AA.
AC   P64804; A0A1R3XY13; Q10622; X2BHJ1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=BQ2027_MB1347C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIT99950.1; -; Genomic_DNA.
DR   RefSeq; NP_855001.1; NC_002945.3.
DR   RefSeq; WP_003406839.1; NC_002945.4.
DR   AlphaFoldDB; P64804; -.
DR   SMR; P64804; -.
DR   EnsemblBacteria; SIT99950; SIT99950; BQ2027_MB1347C.
DR   GeneID; 45425287; -.
DR   PATRIC; fig|233413.5.peg.1476; -.
DR   OMA; HQACTVV; -.
DR   UniPathway; UPA00148; UER00233.
DR   Proteomes; UP000001419; 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; Transferase.
FT   CHAIN           1..193
FT                   /note="Corrinoid adenosyltransferase"
FT                   /id="PRO_0000103799"
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         137..142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   193 AA;  20694 MW;  2FB302A9F5A5208B CRC64;
     MAVHLTRIYT RTGDDGTTGL SDMSRVAKTD ARLVAYADCD EANAAIGAAL ALGHPDTQIT
     DVLRQIQNDL FDAGADLSTP IVENPKHPPL RIAQSYIDRL EGWCDAYNAG LPALKSFVLP
     GGSPLSALLH VARTVVRRAE RSAWAAVDAH PEGVSVLPAK YLNRLSDLLF ILSRVANPDG
     DVLWRPGGDR TAS