COBS_FUSNN
ID COBS_FUSNN Reviewed; 278 AA.
AC Q8R666;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=FN0912;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(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}.
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DR EMBL; AE009951; AAL95108.1; -; Genomic_DNA.
DR RefSeq; NP_603809.1; NC_003454.1.
DR AlphaFoldDB; Q8R666; -.
DR STRING; 190304.FN0912; -.
DR EnsemblBacteria; AAL95108; AAL95108; FN0912.
DR KEGG; fnu:FN0912; -.
DR PATRIC; fig|190304.8.peg.1475; -.
DR eggNOG; COG0368; Bacteria.
DR HOGENOM; CLU_057426_1_2_0; -.
DR InParanoid; Q8R666; -.
DR OMA; GHTGDTY; -.
DR BioCyc; FNUC190304:G1FZS-1494-MON; -.
DR UniPathway; UPA00148; UER00238.
DR Proteomes; UP000002521; 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; IBA:GO_Central.
DR GO; GO:0008818; F:cobalamin 5'-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IBA:GO_Central.
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..278
FT /note="Adenosylcobinamide-GDP ribazoletransferase"
FT /id="PRO_0000146879"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 185..205
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"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
SQ SEQUENCE 278 AA; 30922 MW; 179B9A78A6F9835E CRC64;
MKGFLLLLSF MTRIPMPKTD YDEEKLGKSM KYFPVVGIIV GFILLFFCII FNFILKNISY
SAVLPLMIIV VILTDLITTG ALHLDGLADT FDGIFSYRSK HKMLEIMKDS RLGSNGALAL
ILYFLLKFIL LFSLTIESRE AAVYAIITYP VVSRFCSVVS CASSPYARGS GMGKTFVDNI
KTCGLIVATV ITLLYTIGML FMPFILFTNY SLPMQFMIRS VLIIVIIVGL LALFAFAFSK
LIERKIGGIT GDTLGALLEI SSLVYIFLFL VIPTFFIG
