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Database: UniProt
Entry: A0A365GYC5_9ACTN
LinkDB: A0A365GYC5_9ACTN
Original site: A0A365GYC5_9ACTN 
ID   A0A365GYC5_9ACTN        Unreviewed;       364 AA.
AC   A0A365GYC5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
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:RAY11827.1};
GN   ORFNames=DPM19_28020 {ECO:0000313|EMBL:RAY11827.1};
OS   Actinomadura craniellae.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=2231787 {ECO:0000313|EMBL:RAY11827.1, ECO:0000313|Proteomes:UP000251891};
RN   [1] {ECO:0000313|EMBL:RAY11827.1, ECO:0000313|Proteomes:UP000251891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW63021 {ECO:0000313|EMBL:RAY11827.1,
RC   ECO:0000313|Proteomes:UP000251891};
RA   Li L., Xu Q.H., Lin H.W., Lu Y.H.;
RT   "Actinomadura craniellae sp. nov. isolated from marine sponge Craniella
RT   sp.";
RL   Submitted (JUN-2018) 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|ARBA:ARBA00002197, 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:RAY11827.1}.
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DR   EMBL; QLYX01000016; RAY11827.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365GYC5; -.
DR   OrthoDB; 9773807at2; -.
DR   UniPathway; UPA00061; UER00516.
DR   Proteomes; UP000251891; 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:UP000251891};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00230}.
FT   ACT_SITE        325
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ   SEQUENCE   364 AA;  36519 MW;  1049467CEEA1C81D CRC64;
     MSSDPMSDLI ERTVAAVPRP DEAAMRDARA HQDRLTKPRG ALGALEDVSV RLAGLAGTCP
     PPLPAPAAVA IFAADHGVHA QGVSPWPQEV TAQMVANFAV GGAVANAFAR QVGAEVVVVD
     VGVAADLPAA PGLLDRKVAR GTADLSQGPA MTAEQVRRAV AAGIEVAGGL ADAGHRCLIT
     GDMGIANTTA SAALIAAFTG LPAERVTGRG TGIDDTVHAR KIEVVRTALA RHGLPGGDPL
     DVLAAVGGLE HAALAGFILG AAARRVPVLL DGVIAGAAAL AAAALCPDVV AACVAGHRSV
     EPGHAATVEH LGLRPLVDLE LRLGEGTGAL LALPLVQSSV RVLHEVATFD SAGVSDKESR
     SAID
//
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