BTUR_ECOLI
ID BTUR_ECOLI Reviewed; 196 AA.
AC P0A9H5; P13040;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
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; Synonyms=cobA; OrderedLocusNames=b1270, JW1262;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2644187; DOI=10.1128/jb.171.1.154-161.1989;
RA Lundrigan M.D., Kadner R.J.;
RT "Altered cobalamin metabolism in Escherichia coli btuR mutants affects btuB
RT gene regulation.";
RL J. Bacteriol. 171:154-161(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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.
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; M21528; AAA23530.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74352.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14807.1; -; Genomic_DNA.
DR PIR; A64875; A64875.
DR RefSeq; NP_415786.1; NC_000913.3.
DR RefSeq; WP_001278906.1; NZ_SSZK01000031.1.
DR AlphaFoldDB; P0A9H5; -.
DR SMR; P0A9H5; -.
DR BioGRID; 4259575; 12.
DR IntAct; P0A9H5; 14.
DR STRING; 511145.b1270; -.
DR jPOST; P0A9H5; -.
DR PaxDb; P0A9H5; -.
DR PRIDE; P0A9H5; -.
DR EnsemblBacteria; AAC74352; AAC74352; b1270.
DR EnsemblBacteria; BAA14807; BAA14807; BAA14807.
DR GeneID; 66674908; -.
DR GeneID; 945839; -.
DR KEGG; ecj:JW1262; -.
DR KEGG; eco:b1270; -.
DR PATRIC; fig|1411691.4.peg.1014; -.
DR EchoBASE; EB0128; -.
DR eggNOG; COG2109; Bacteria.
DR HOGENOM; CLU_088595_0_0_6; -.
DR InParanoid; P0A9H5; -.
DR OMA; HAMGEGF; -.
DR PhylomeDB; P0A9H5; -.
DR BioCyc; EcoCyc:COBALADENOSYLTRANS-MON; -.
DR UniPathway; UPA00148; UER00233.
DR PRO; PR:P0A9H5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; ISS:EcoCyc.
DR GO; GO:0019250; P:aerobic cobalamin biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IMP:EcoCyc.
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; Reference proteome; Transferase.
FT CHAIN 1..196
FT /note="Corrinoid adenosyltransferase"
FT /id="PRO_0000065009"
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
