ID   BTUR_ECOL6              Reviewed;         196 AA.
AC   P0A9H6; P13040;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=btuR; OrderedLocusNames=c1735;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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   -!- 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}.
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; AE014075; AAN80201.1; -; Genomic_DNA.
DR   RefSeq; WP_001278906.1; NC_004431.1.
DR   AlphaFoldDB; P0A9H6; -.
DR   SMR; P0A9H6; -.
DR   STRING; 199310.c1735; -.
DR   EnsemblBacteria; AAN80201; AAN80201; c1735.
DR   GeneID; 66674908; -.
DR   KEGG; ecc:c1735; -.
DR   eggNOG; COG2109; Bacteria.
DR   HOGENOM; CLU_088595_0_0_6; -.
DR   OMA; HAMGEGF; -.
DR   BioCyc; ECOL199310:C1735-MON; -.
DR   UniPathway; UPA00148; UER00233.
DR   Proteomes; UP000001410; 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   CDD; cd00561; CobA_CobO_BtuR; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003724; CblAdoTrfase_CobA.
DR   InterPro; IPR025826; Co_AT_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12557; Co_AT_N; 1.
DR   Pfam; PF02572; CobA_CobO_BtuR; 1.
DR   PIRSF; PIRSF015617; Adensltrnsf_CobA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00708; cobA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cobalamin biosynthesis; Cytoplasm; Nucleotide-binding;
KW   Porphyrin biosynthesis; Transferase.
FT   CHAIN           1..196
FT                   /note="Corrinoid adenosyltransferase"
FT                   /id="PRO_0000065008"
FT   BINDING         36..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   196 AA;  21999 MW;  4EE2FDD9C74FE8AE CRC64;
     MSDERYQQRQ QRVKEKVDAR VAQAQDERGI IIVFTGNGKG KTTAAFGTAT RAVGHGKKVG
     VVQFIKGTWP NGERNLLEPH GVEFQVMATG FTWDTQNRES DTAACREVWQ HAKRMLADSS
     LDMVLLDELT YMVAYDYLPL EEVVQALNER PHQQTVIITG RGCHRDILEL ADTVSELRPV
     KHAFDAGVKA QIGIDY