ID A0A3D2XQM5_9FIRM Unreviewed; 126 AA. AC A0A3D2XQM5; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 07-OCT-2020, entry version 9. DE RecName: Full=Adenosylcobinamide kinase {ECO:0000256|ARBA:ARBA00014853}; DE EC=2.7.1.156 {ECO:0000256|ARBA:ARBA00012016}; DE EC=2.7.7.62 {ECO:0000256|ARBA:ARBA00012523}; DE AltName: Full=Adenosylcobinamide-phosphate guanylyltransferase {ECO:0000256|ARBA:ARBA00020787}; GN ORFNames=DHW25_04670 {ECO:0000313|EMBL:HCL09177.1}; OS Blautia sp. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae; Blautia; OC unclassified Blautia. OX NCBI_TaxID=1955243 {ECO:0000313|EMBL:HCL09177.1, ECO:0000313|Proteomes:UP000262112}; RN [1] {ECO:0000313|EMBL:HCL09177.1, ECO:0000313|Proteomes:UP000262112} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA9114 {ECO:0000313|EMBL:HCL09177.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide CC and addition of GMP to adenosylcobinamide phosphate. CC {ECO:0000256|ARBA:ARBA00003889}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosylcob(III)inamide + ATP = adenosylcob(III)inamide CC phosphate + ADP + H(+); Xref=Rhea:RHEA:15769, ChEBI:CHEBI:2480, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58502, CC ChEBI:CHEBI:456216; EC=2.7.1.156; CC Evidence={ECO:0000256|ARBA:ARBA00000312}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosylcob(III)inamide + GTP = adenosylcob(III)inamide CC phosphate + GDP + H(+); Xref=Rhea:RHEA:15765, ChEBI:CHEBI:2480, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, CC ChEBI:CHEBI:58502; EC=2.7.1.156; CC Evidence={ECO:0000256|ARBA:ARBA00001522}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosylcob(III)inamide phosphate + GTP + H(+) = CC adenosylcob(III)inamide-GDP + diphosphate; Xref=Rhea:RHEA:22712, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:58502, ChEBI:CHEBI:60487; EC=2.7.7.62; CC Evidence={ECO:0000256|ARBA:ARBA00000711}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 6/7. CC {ECO:0000256|ARBA:ARBA00004692}. CC -!- SIMILARITY: Belongs to the CobU/CobP family. CC {ECO:0000256|ARBA:ARBA00007490}. 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:HCL09177.1}. 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; DPVL01000023; HCL09177.1; -; Genomic_DNA. DR UniPathway; UPA00148; UER00237. DR Proteomes; UP000262112; Unassembled WGS sequence. DR GO; GO:0043752; F:adenosylcobinamide kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008820; F:cobinamide phosphate guanylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR003203; Cobinamide_kinase/P_G-Trfase. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR34848; PTHR34848; 1. DR Pfam; PF02283; CobU; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:HCL09177.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. SQ SEQUENCE 126 AA; 13778 MW; EA740FE24AD54C8D CRC64; MEMIIGGAFQ GKSDYAKEKH PEICWKNGGK LEEYQLMKAE GVLDFQEFIR KELKAGHDVA GLAEKLAEGN PDIVVVSQEV GYGVVPMDAF DRKYREAVGR VCTGLASKSK KVTRVVCGIG TVIKDA //