ID A0A3C1GFJ4_9BACT Unreviewed; 456 AA. AC A0A3C1GFJ4; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 19-JAN-2022, entry version 12. DE RecName: Full=Adenosylcobinamide-GDP ribazoletransferase {ECO:0000256|ARBA:ARBA00015850, ECO:0000256|HAMAP-Rule:MF_00719}; DE EC=2.7.8.26 {ECO:0000256|ARBA:ARBA00013200, ECO:0000256|HAMAP-Rule:MF_00719}; DE AltName: Full=Cobalamin synthase {ECO:0000256|ARBA:ARBA00019722, ECO:0000256|HAMAP-Rule:MF_00719}; DE AltName: Full=Cobalamin-5'-phosphate synthase {ECO:0000256|ARBA:ARBA00016241, 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; unclassified Candidatus Rokubacteria. OX NCBI_TaxID=2053607 {ECO:0000313|EMBL:HAM57340.1, ECO:0000313|Proteomes:UP000259942}; RN [1] {ECO:0000313|EMBL:HAM57340.1, ECO:0000313|Proteomes:UP000259942} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Joins adenosylcobinamide-GDP and alpha-ribazole to generate CC adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin CC 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- CC phosphate. {ECO:0000256|ARBA:ARBA00025228, ECO:0000256|HAMAP- CC Rule:MF_00719}. 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; EC=2.7.8.26; CC Evidence={ECO:0000256|ARBA:ARBA00001017, ECO:0000256|HAMAP- CC Rule:MF_00719}; 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|ARBA:ARBA00000357, ECO:0000256|HAMAP- CC Rule:MF_00719}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_00719}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7. CC {ECO:0000256|ARBA:ARBA00004663, ECO:0000256|HAMAP-Rule:MF_00719}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00719}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00719}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the CobS family. {ECO:0000256|ARBA:ARBA00010561, CC ECO:0000256|HAMAP-Rule:MF_00719}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00719}. 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: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 Proteomes; UP000259942; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051073; F:adenosylcobinamide-GDP ribazoletransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008818; F:cobalamin 5'-phosphate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule. 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|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00719}; KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP- KW Rule:MF_00719}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00719}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00719}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00719}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00719}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00719}. FT TRANSMEM 31..48 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00719" FT TRANSMEM 105..124 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00719" FT TRANSMEM 177..209 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule: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 //