ID A0A0R2RH42_9FLAO Unreviewed; 186 AA. AC A0A0R2RH42; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 03-JUL-2019, entry version 10. DE RecName: Full=Corrinoid adenosyltransferase {ECO:0000256|RuleBase:RU366026}; DE EC=2.5.1.17 {ECO:0000256|RuleBase:RU366026}; GN ORFNames=ABR98_03085 {ECO:0000313|EMBL:KRO59386.1}; OS Cryomorphaceae bacterium BACL7 MAG-120910-bin2. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Cryomorphaceae; unclassified 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., RA Pinhassi J., 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- CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:16304, CC ChEBI:CHEBI:18036, ChEBI:CHEBI:18408, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; 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 CC family. {ECO:0000256|RuleBase:RU366026}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00148; UER00233. DR Proteomes; UP000052134; Unassembled WGS sequence. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 1.20.1200.10; -; 1. DR InterPro; IPR016030; CblAdoTrfase-like. DR InterPro; IPR036451; CblAdoTrfase-like_sf. DR InterPro; IPR029499; PduO-typ. DR PANTHER; PTHR12213; PTHR12213; 1. DR Pfam; PF01923; Cob_adeno_trans; 1. DR SUPFAM; SSF89028; SSF89028; 1. DR TIGRFAMs; TIGR00636; PduO_Nterm; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|RuleBase:RU366026}; KW Complete proteome {ECO:0000313|Proteomes:UP000052134}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU366026}; KW Transferase {ECO:0000256|RuleBase:RU366026, KW ECO:0000313|EMBL:KRO59386.1}. FT DOMAIN 3 170 Cob_adeno_trans. {ECO:0000259|Pfam: FT 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 //