ID S6HGU9_9GAMM Unreviewed; 350 AA.
AC S6HGU9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00015486, ECO:0000256|HAMAP-Rule:MF_00230};
DE Short=NN:DBI PRT {ECO:0000256|HAMAP-Rule:MF_00230};
DE EC=2.4.2.21 {ECO:0000256|ARBA:ARBA00011991, ECO:0000256|HAMAP-Rule:MF_00230};
DE AltName: Full=N(1)-alpha-phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00030686, ECO:0000256|HAMAP-Rule:MF_00230};
GN Name=cobT {ECO:0000256|HAMAP-Rule:MF_00230};
GN ORFNames=OFPII_08870 {ECO:0000313|EMBL:EPJ47919.1};
OS Osedax symbiont Rs1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ47919.1, ECO:0000313|Proteomes:UP000014822};
RN [1] {ECO:0000313|EMBL:EPJ47919.1, ECO:0000313|Proteomes:UP000014822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from
CC nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
CC {ECO:0000256|HAMAP-Rule:MF_00230}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide =
CC alpha-ribazole 5'-phosphate + H(+) + nicotinate;
CC Xref=Rhea:RHEA:11196, ChEBI:CHEBI:15378, ChEBI:CHEBI:15890,
CC ChEBI:CHEBI:32544, ChEBI:CHEBI:57502, ChEBI:CHEBI:57918; EC=2.4.2.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001058, ECO:0000256|HAMAP-
CC Rule:MF_00230};
CC -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC ribazole from 5,6-dimethylbenzimidazole: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005049, ECO:0000256|HAMAP-Rule:MF_00230}.
CC -!- SIMILARITY: Belongs to the CobT family. {ECO:0000256|ARBA:ARBA00007110,
CC ECO:0000256|HAMAP-Rule:MF_00230}.
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:EPJ47919.1}.
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DR EMBL; ASZJ01000049; EPJ47919.1; -; Genomic_DNA.
DR AlphaFoldDB; S6HGU9; -.
DR PATRIC; fig|1330036.3.peg.839; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000014822; Unassembled WGS sequence.
DR GO; GO:0008939; F:nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02439; DMB-PRT_CobT; 1.
DR Gene3D; 1.10.1610.10; -; 1.
DR Gene3D; 3.40.50.10210; -; 1.
DR HAMAP; MF_00230; CobT; 1.
DR InterPro; IPR003200; Nict_dMeBzImd_PRibTrfase.
DR InterPro; IPR017846; Nict_dMeBzImd_PRibTrfase_bact.
DR InterPro; IPR023195; Nict_dMeBzImd_PRibTrfase_N.
DR InterPro; IPR036087; Nict_dMeBzImd_PRibTrfase_sf.
DR NCBIfam; TIGR03160; cobT_DBIPRT; 1.
DR PANTHER; PTHR43463; NICOTINATE-NUCLEOTIDE--DIMETHYLBENZIMIDAZOLE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43463:SF1; NICOTINATE-NUCLEOTIDE--DIMETHYLBENZIMIDAZOLE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF02277; DBI_PRT; 1.
DR SUPFAM; SSF52733; Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT); 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00230};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00230}; Reference proteome {ECO:0000313|Proteomes:UP000014822};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00230}.
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ SEQUENCE 350 AA; 36278 MW; D06578596C326B90 CRC64;
MNNWIFSKVK KLDQSARNAA IARQSQLTKP LGALGKLETI AIELAAMQGS MPSINTPYIC
VFAADHGIAA SGVSAFPQEV TAQMVANFAS GGAAISVLAK SLLAPFDIVN LGTVSVTDYP
GVNNEFIGPG TANMLHQDAM TKLQCAQALE IGRNYLLHAK KCGCDMFIGG DMGIGNTTSA
TVLAAALIGA PAISLTGAGT GLDAEGIKHK VDIIEQVLAK HFDDQLTAEK LLQKVGGFEI
AALVGSYIAA AQIGMPVLVD GFICTAAAMV AVAISPESRA WMIFSHGSAE PGHKLMLEHL
QASPVLDLGM RLGEGSGAAV CVPILQIACK LHNQMATFAE AAVAGKLDEH
//