COBS_THEVB
ID COBS_THEVB Reviewed; 243 AA.
AC Q8DJ91;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Adenosylcobinamide-GDP ribazoletransferase {ECO:0000255|HAMAP-Rule:MF_00719};
DE EC=2.7.8.26 {ECO:0000255|HAMAP-Rule:MF_00719};
DE AltName: Full=Cobalamin synthase {ECO:0000255|HAMAP-Rule:MF_00719};
DE AltName: Full=Cobalamin-5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00719};
GN Name=cobS {ECO:0000255|HAMAP-Rule:MF_00719}; OrderedLocusNames=tll1337;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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:0000255|HAMAP-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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00719};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00719};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
CC {ECO:0000255|HAMAP-Rule:MF_00719}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00719}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00719}.
CC -!- SIMILARITY: Belongs to the CobS family. {ECO:0000255|HAMAP-
CC Rule:MF_00719}.
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; BA000039; BAC08889.1; -; Genomic_DNA.
DR RefSeq; NP_682127.1; NC_004113.1.
DR RefSeq; WP_011057177.1; NC_004113.1.
DR AlphaFoldDB; Q8DJ91; -.
DR STRING; 197221.22295061; -.
DR EnsemblBacteria; BAC08889; BAC08889; BAC08889.
DR KEGG; tel:tll1337; -.
DR PATRIC; fig|197221.4.peg.1405; -.
DR eggNOG; COG0368; Bacteria.
DR OMA; GHTGDTY; -.
DR OrthoDB; 1996371at2; -.
DR UniPathway; UPA00148; UER00238.
DR Proteomes; UP000000440; Chromosome.
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 HAMAP; MF_00719; CobS; 1.
DR InterPro; IPR003805; CobS.
DR PANTHER; PTHR34148; PTHR34148; 1.
DR Pfam; PF02654; CobS; 1.
DR TIGRFAMs; TIGR00317; cobS; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cobalamin biosynthesis; Magnesium;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..243
FT /note="Adenosylcobinamide-GDP ribazoletransferase"
FT /id="PRO_0000146898"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
SQ SEQUENCE 243 AA; 26329 MW; 4EFDD3C65F3AEE64 CRC64;
MKSLWQEWLG AIAFYTCLPI SPRWPIQLAG AAKWCPWVGL VLGGMLWGVQ WLLDFLQVPS
PVASAVLVAL WLALTGGLHL DGAMDTADGL AVRDQQRRLE VMADSRAGAF GVMAAMVILL
LKVTSLSSLE KGSVLVWVLV LGRLAQVWAI ARYPYLKPQG TGQIHKTSGV FPRDFWPSGL
LVLLLSFLLP LPLGQLLFGL LLILLIPAWF QSQLGGHTGD SYGAVVEWTE ALLLVAFTVG
SAS
