ID A0A0R2RH42_9FLAO Unreviewed; 186 AA. AC A0A0R2RH42; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 13-SEP-2023, entry version 20. DE RecName: Full=Corrinoid adenosyltransferase {ECO:0000256|RuleBase:RU366026}; DE EC=2.5.1.17 {ECO:0000256|RuleBase:RU366026}; DE AltName: Full=Cob(II)alamin adenosyltransferase {ECO:0000256|RuleBase:RU366026}; DE AltName: Full=Cob(II)yrinic acid a,c-diamide adenosyltransferase {ECO:0000256|RuleBase:RU366026}; DE AltName: Full=Cobinamide/cobalamin adenosyltransferase {ECO:0000256|RuleBase:RU366026}; GN ORFNames=ABR98_03085 {ECO:0000313|EMBL:KRO59386.1}; OS Cryomorphaceae bacterium BACL7 MAG-120910-bin2. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae. OX NCBI_TaxID=1655558 {ECO:0000313|EMBL:KRO59386.1, ECO:0000313|Proteomes:UP000052134}; RN [1] {ECO:0000313|EMBL:KRO59386.1, ECO:0000313|Proteomes:UP000052134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BACL10 MAG-120910-bin2 {ECO:0000313|EMBL:KRO59386.1}; RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J., RA Andersson A.F.; RT "Metagenome-Assembled Genomes uncover a global brackish microbiome."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. 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 Evidence={ECO:0000256|RuleBase:RU366026}; 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 Evidence={ECO:0000256|RuleBase:RU366026}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7. CC {ECO:0000256|RuleBase:RU366026}. CC -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family. CC {ECO:0000256|RuleBase:RU366026}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KRO59386.1}. 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; LIBQ01000004; KRO59386.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0R2RH42; -. DR EnsemblBacteria; KRO59386; KRO59386; ABR98_03085. DR UniPathway; UPA00148; UER00233. DR Proteomes; UP000052134; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008817; F:corrinoid adenosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule. 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; 1. DR Pfam; PF01923; Cob_adeno_trans; 1. DR SUPFAM; SSF89028; Cobalamin adenosyltransferase-like; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU366026}; KW Cobalamin biosynthesis {ECO:0000256|RuleBase:RU366026}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU366026}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366026}. FT DOMAIN 3..170 FT /note="Cobalamin adenosyltransferase-like" FT /evidence="ECO:0000259|Pfam:PF01923" SQ SEQUENCE 186 AA; 20921 MW; 7A422B0B5F5985F3 CRC64; MKIYTKTGDS GQTGLFSGQR VSKFDLRLHA YGTLDELNAH TGLLHDLAPR ELQKELQVIQ RQLFAIGSHL ANDSLEMVER LPPLNPAWTE NLEAAIDRMD AVLPPLRNFV LPGGHPAVSH AHLARTVCRR AERWCAELQL QLASGPLPMP EAVLPFLNRL SDYFFTCSRW LAHELGVQEI AWKPEP //