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Database: UniProt
Entry: M9RGW2_9RHOB
LinkDB: M9RGW2_9RHOB
Original site: M9RGW2_9RHOB 
ID   M9RGW2_9RHOB            Unreviewed;       336 AA.
AC   M9RGW2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
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   ECO:0000313|EMBL:AGI70958.1};
GN   ORFNames=OA238_c07390 {ECO:0000313|EMBL:AGI70958.1};
OS   Octadecabacter arcticus 238.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391616 {ECO:0000313|EMBL:AGI70958.1, ECO:0000313|Proteomes:UP000004688};
RN   [1] {ECO:0000313|EMBL:AGI70958.1, ECO:0000313|Proteomes:UP000004688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=238 {ECO:0000313|EMBL:AGI70958.1,
RC   ECO:0000313|Proteomes:UP000004688};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
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}.
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DR   EMBL; CP003742; AGI70958.1; -; Genomic_DNA.
DR   RefSeq; WP_015494186.1; NC_020908.1.
DR   AlphaFoldDB; M9RGW2; -.
DR   STRING; 391616.OA238_c07390; -.
DR   KEGG; oar:OA238_c07390; -.
DR   eggNOG; COG2038; Bacteria.
DR   HOGENOM; CLU_002982_0_1_5; -.
DR   OrthoDB; 9781491at2; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000004688; Chromosome.
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:UP000004688};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00230}.
FT   ACT_SITE        304
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   336 AA;  34048 MW;  4C94E1E391FF17ED CRC64;
     MTAPFATLNE FRAMLEAATG PDMASIAGAK ARNGQLTKPP GALGRLEELA IWYASWRNTD
     RPRIKNPQII VFAGNHGVCA QGVSAFPPEV TAQMVGNFEH GGAAINQLAK TFGATLNVHA
     LELEMPTQDF TSAPAMSEVE VVIALMAGWD AVDPKADLLV TGEMGIGNTT SAAAVAAAVL
     GGSAADWTGR GTGVDDDGLA RKTDAVARGL ALHDTSDPLE ALRCLGGREL AAMAGAIAAA
     RHHRIPVILD GFICCAAAAT LEKAVAGSLD HAVAGHLSAE GAHEKLLVAL GKSPILALDL
     RLGEGSGGAL AIGILQAAVA CHSGMATFAE AGVAAG
//
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