ID A0A847LTI5_9SPIR Unreviewed; 122 AA. AC A0A847LTI5; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 03-AUG-2022, entry version 4. 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=GX435_03580 {ECO:0000313|EMBL:NLJ04777.1}; OS Exilispira sp. OC Bacteria; Spirochaetes; Spirochaetales; Exilispira; OC unclassified Exilispira. OX NCBI_TaxID=2699745 {ECO:0000313|EMBL:NLJ04777.1, ECO:0000313|Proteomes:UP000560828}; RN [1] {ECO:0000313|EMBL:NLJ04777.1, ECO:0000313|Proteomes:UP000560828} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS27yjCOA_19 {ECO:0000313|EMBL:NLJ04777.1}; RX PubMed=32123542; RA Campanaro S., Treu L., Rodriguez-R L.M., Kovalovszki A., Ziels R.M., RA Maus I., Zhu X., Kougias P.G., Basile A., Luo G., Schluter A., RA Konstantinidis K.T., Angelidaki I.; RT "New insights from the biogas microbiome by comprehensive genome-resolved RT metagenomics of nearly 1600 species originating from multiple anaerobic RT digesters."; RL Biotechnol. Biofuels 13:25-20(2020). 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:NLJ04777.1}. 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; JAAYUW010000058; NLJ04777.1; -; Genomic_DNA. DR UniPathway; UPA00148; UER00233. DR Proteomes; UP000560828; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008817; F:cob(I)yrinic acid a,c-diamide adenosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule. 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. 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..122 FT /note="Cob_adeno_trans" FT /evidence="ECO:0000259|Pfam:PF01923" SQ SEQUENCE 122 AA; 13523 MW; 5A3A4394E5B93FD0 CRC64; MSIVSKKGDD GWTTLIDGSS VEKSDLQPSG YGTVDELFSF SGVLKSLCKE NNIIIQDKGS AVDVLDKIQQ RLIVLMAELA TPKKMVSTLL KDRIKEEDII FIEELIYDLE NKTGKIDGFV IP //