COBV_SINSX
ID COBV_SINSX Reviewed; 262 AA.
AC P29936;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Adenosylcobinamide-GDP ribazoletransferase;
DE EC=2.7.8.26;
DE AltName: Full=Cobalamin synthase;
DE AltName: Full=Cobalamin-5'-phosphate synthase;
GN Name=cobV;
OS Sinorhizobium sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=42445;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=SC510;
RX PubMed=1917841; DOI=10.1128/jb.173.19.6066-6073.1991;
RA Cameron B., Blanche F., Rouyez M.-C., Bisch D., Famechon A., Couder M.,
RA Cauchois L., Thibaut D., Debussche L., Crouzet J.;
RT "Genetic analysis, nucleotide sequence, and products of two Pseudomonas
RT denitrificans cob genes encoding nicotinate-nucleotide:
RT dimethylbenzimidazole phosphoribosyltransferase and cobalamin (5'-
RT phosphate) synthase.";
RL J. Bacteriol. 173:6066-6073(1991).
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:0000269|PubMed:1917841}.
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:0000269|PubMed:1917841};
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:0000269|PubMed:1917841};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1917841};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 uM for alpha-ribazole 5'-phosphate
CC {ECO:0000269|PubMed:1917841};
CC KM=0.9 uM for adenosylcobinamide-GDP {ECO:0000269|PubMed:1917841};
CC KM=7.8 uM for alpha-ribazole {ECO:0000269|PubMed:1917841};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
CC -!- SUBUNIT: Associated with a large complex of proteins.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CobS family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from Pseudomonas
CC denitrificans, but similarity searches show that the sequence is much
CC closer to Sinorhizobium. The entry's taxonomy has been changed.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25787.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M62868; AAA25787.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P29936; -.
DR BioCyc; MetaCyc:MON-144; -.
DR SABIO-RK; P29936; -.
DR UniPathway; UPA00148; UER00238.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cobalamin biosynthesis; Magnesium;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..262
FT /note="Adenosylcobinamide-GDP ribazoletransferase"
FT /id="PRO_0000146888"
FT TRANSMEM 41..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 262 AA; 26842 MW; 2E2E833C94518D5F CRC64;
MGFVGDFCDD VARSIGFLSR IPMPARHFEG YDGRLSRAVR AFPFAGLAIA LPSAAVAMAL
MALQVSSLFA AFVVVAIQAL VTGALHEDGL GDTADGFGGG RDREAALAIM KDSRIGTYAA
VALILSFGLR VSAFASILPL FSPLGAAMAI LGAACLSRAA MVWHWSSLPP ARSSGVAASA
GEPEPAATRF ALAFGLLVAM LLFYLAQVPA LGVIAALVAF LATVKGFARL AMRKIGGQTG
DTIGATQQLT EIAVLGALAL TV