ID   COBO_SINSX              Reviewed;         214 AA.
AC   P29930;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 95.
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   Name=cobO;
OS   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC510;
RX   PubMed=1655697; DOI=10.1128/jb.173.19.6074-6087.1991;
RA   Crouzet J., Levy-Schil S., Cameron B., Cauchois L., Rigault S.,
RA   Rouyez M.-C., Blanche F., Debussche L., Thibaut D.;
RT   "Nucleotide sequence and genetic analysis of a 13.1-kilobase-pair
RT   Pseudomonas denitrificans DNA fragment containing five cob genes and
RT   identification of structural genes encoding Cob(I)alamin
RT   adenosyltransferase, cobyric acid synthase, and bifunctional cobinamide
RT   kinase-cobinamide phosphate guanylyltransferase.";
RL   J. Bacteriol. 173:6074-6087(1991).
RN   [2]
RP   CHARACTERIZATION, AND PROTEIN SEQUENCE OF 2-15.
RX   PubMed=1917862; DOI=10.1128/jb.173.19.6300-6302.1991;
RA   Debussche L., Couder M., Thibaut D., Cameron B., Crouzet J., Blanche F.;
RT   "Purification and partial characterization of Cob(I)alamin
RT   adenosyltransferase from Pseudomonas denitrificans.";
RL   J. Bacteriol. 173:6300-6302(1991).
CC   -!- FUNCTION: Required for both de novo synthesis of the corrin ring for
CC       the assimilation of exogenous corrinoids. Participates in the
CC       adenosylation of a variety of incomplete and complete corrinoids (By
CC       similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from Pseudomonas
CC       denitrificans, but similarity searches show that the sequence is much
CC       closer to Sinorhizobium. The entry's taxonomy has been changed.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M62866; AAA25781.1; -; Genomic_DNA.
DR   AlphaFoldDB; P29930; -.
DR   SMR; P29930; -.
DR   BioCyc; MetaCyc:MON-123; -.
DR   UniPathway; UPA00148; UER00233.
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   CDD; cd00561; CobA_CobO_BtuR; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003724; CblAdoTrfase_CobA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02572; CobA_CobO_BtuR; 1.
DR   PIRSF; PIRSF015617; Adensltrnsf_CobA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00708; cobA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cobalamin biosynthesis; Cytoplasm; Direct protein sequencing;
KW   Manganese; Nucleotide-binding; Porphyrin biosynthesis; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1917862"
FT   CHAIN           2..214
FT                   /note="Corrinoid adenosyltransferase"
FT                   /id="PRO_0000089992"
FT   BINDING         50..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        14
FT                   /note="E -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   214 AA;  24028 MW;  A110C89668990ECC CRC64;
     MSDETTVGGE APAEKDDARH AMKMAKKKAA REKIMATKTD EKGLIIVNTG KGKGKSTAGF
     GMIFRHIAHG MPCAVVQFIK GAMATGEREL IEKHFGDVCQ FYTLGEGFTW ETQDRARDVA
     MAEKAWEKAK ELIRDERNSM VLLDEINIAL RYDYIDVAEV VRFLKEEKPH MTHVVLTGRN
     AKEDLIEVAD LVTEMELIKH PFRSGIKAQQ GVEF