ID A0A3C1GFJ4_9BACT Unreviewed; 456 AA. AC A0A3C1GFJ4; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 13-FEB-2019, entry version 2. DE RecName: Full=Adenosylcobinamide-GDP ribazoletransferase {ECO:0000256|HAMAP-Rule:MF_00719, ECO:0000256|SAAS:SAAS00702411}; DE EC=2.7.8.26 {ECO:0000256|HAMAP-Rule:MF_00719, ECO:0000256|SAAS:SAAS00702417}; DE AltName: Full=Cobalamin synthase {ECO:0000256|HAMAP-Rule:MF_00719}; DE AltName: Full=Cobalamin-5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00719}; GN Name=cobS {ECO:0000256|HAMAP-Rule:MF_00719, GN ECO:0000313|EMBL:HAM57340.1}; GN ORFNames=DCQ64_18785 {ECO:0000313|EMBL:HAM57340.1}; OS Candidatus Rokubacteria bacterium. OC Bacteria; Candidatus Rokubacteria. OX NCBI_TaxID=2053607 {ECO:0000313|EMBL:HAM57340.1}; RN [1] {ECO:0000313|EMBL:HAM57340.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA12499 {ECO:0000313|EMBL:HAM57340.1}; 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 RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Joins adenosylcobinamide-GDP and alpha-ribazole to CC generate adenosylcobalamin (Ado-cobalamin). Also synthesizes CC adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and CC alpha-ribazole 5'-phosphate. {ECO:0000256|HAMAP-Rule:MF_00719, CC ECO:0000256|SAAS:SAAS00702400}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate CC = adenosylcob(III)alamin 5'-phosphate + GMP + H(+); CC Xref=Rhea:RHEA:23560, ChEBI:CHEBI:15378, ChEBI:CHEBI:57918, CC ChEBI:CHEBI:58115, ChEBI:CHEBI:60487, ChEBI:CHEBI:60493; CC EC=2.7.8.26; Evidence={ECO:0000256|HAMAP-Rule:MF_00719, CC ECO:0000256|SAAS:SAAS01124952}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosylcob(III)inamide-GDP + alpha-ribazole = CC adenosylcob(III)alamin + GMP + H(+); Xref=Rhea:RHEA:16049, CC ChEBI:CHEBI:10329, ChEBI:CHEBI:15378, ChEBI:CHEBI:18408, CC ChEBI:CHEBI:58115, ChEBI:CHEBI:60487; EC=2.7.8.26; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00719, CC ECO:0000256|SAAS:SAAS01124946}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00719, ECO:0000256|SAAS:SAAS00702435}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7. CC {ECO:0000256|HAMAP-Rule:MF_00719, ECO:0000256|SAAS:SAAS00702428}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00719}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00719}. CC -!- SIMILARITY: Belongs to the CobS family. {ECO:0000256|HAMAP- CC Rule:MF_00719, ECO:0000256|SAAS:SAAS00702395}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00719}. 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:HAM57340.1}. 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; DMMU01000541; HAM57340.1; -; Genomic_DNA. DR UniPathway; UPA00148; UER00238. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR CDD; cd07067; HP_PGM_like; 1. DR Gene3D; 3.40.50.1240; -; 1. DR HAMAP; MF_00719; CobS; 1. DR InterPro; IPR003805; CobS. DR InterPro; IPR013078; His_Pase_superF_clade-1. DR InterPro; IPR029033; His_PPase_superfam. DR PANTHER; PTHR34148; PTHR34148; 1. DR Pfam; PF02654; CobS; 1. DR Pfam; PF00300; His_Phos_1; 1. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF53254; SSF53254; 1. DR TIGRFAMs; TIGR00317; cobS; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00719, KW ECO:0000256|SAAS:SAAS00702407}; KW Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00719, KW ECO:0000256|SAAS:SAAS00702420}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00719, KW ECO:0000256|SAAS:SAAS00702394}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00719, KW ECO:0000256|SAAS:SAAS00702455}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00719, KW ECO:0000256|SAAS:SAAS00702398, ECO:0000313|EMBL:HAM57340.1}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00719, KW ECO:0000256|SAAS:SAAS00702443}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00719, KW ECO:0000256|SAAS:SAAS00702402}. FT TRANSMEM 31 48 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00719}. FT TRANSMEM 105 124 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00719}. FT TRANSMEM 177 209 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00719}. SQ SEQUENCE 456 AA; 47643 MW; 057D3F02C7EBD3E7 CRC64; MASLILAIRF LTIVPVPGRE AAGPGALGRA AWWFPAVGLG LGAGLVLVDR LLTRAFPPLL AALLVVSLWK VATGGIHLDG LADCLDGLGG RDPGHRVAIM RDSRIGVFGA LGLILSFLIG ITALGELPGD VRWRALLLAP VVGRLSPLVA GACFRAATPE AGSGSAFMAS LSRWAPALSV VWAGVVAALL LELPGLLALA VALAGVLLWS GFLSRRLGGL TGDALGAGVE LAELGVLLAL AAAAHVMQDL TPTVIYLVRH GAVVGAESRR FIGHLDVPLS PLGEAQCEAL ARRLATVALA AVYSSDLLRS RRSAEILAAP HGLRTEALPG LREFAMGRWE GLTAEEIRAR DPVAFEEWMA DIGRFQFPEG EHLEQVAVRA WRAFEGIVAA HAGARVAVVS HGGTNRAILC RALGIPLGRI LALGQDYAAL SVLEAAPEGW RLRLLNHCEP LLAPSP //