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 27-MAR-2024, entry version 99. 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; Actinomycetota; Actinomycetes; Mycobacteriales; 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}. 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; 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 GeneID; 45425287; -. DR PATRIC; fig|233413.5.peg.1476; -. 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:corrinoid 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; Cobalamin adenosyltransferase-like; 1. DR InterPro; IPR016030; CblAdoTrfase-like. DR InterPro; IPR036451; CblAdoTrfase-like_sf. DR InterPro; IPR029499; PduO-typ. DR NCBIfam; TIGR00636; PduO_Nterm; 1. DR PANTHER; PTHR12213; CORRINOID ADENOSYLTRANSFERASE; 1. DR PANTHER; PTHR12213:SF0; CORRINOID ADENOSYLTRANSFERASE MMAB; 1. DR Pfam; PF01923; Cob_adeno_trans; 1. DR SUPFAM; SSF89028; Cobalamin adenosyltransferase-like; 1. PE 3: Inferred from homology; KW ATP-binding; Cobalamin biosynthesis; Cytoplasm; Nucleotide-binding; KW Porphyrin biosynthesis; Reference proteome; 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 //