ID A0A0L8L2M3_9ACTN Unreviewed; 701 AA.
AC A0A0L8L2M3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=ADK37_27210 {ECO:0000313|EMBL:KOG32365.1};
OS Streptomyces resistomycificus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67356 {ECO:0000313|EMBL:KOG32365.1, ECO:0000313|Proteomes:UP000037251};
RN [1] {ECO:0000313|Proteomes:UP000037251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2290 {ECO:0000313|Proteomes:UP000037251};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KOG32365.1}.
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DR EMBL; LGUS01000185; KOG32365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8L2M3; -.
DR STRING; 67356.AQJ84_25510; -.
DR PATRIC; fig|67356.5.peg.5827; -.
DR eggNOG; COG0778; Bacteria.
DR eggNOG; COG2038; Bacteria.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000037251; Unassembled WGS sequence.
DR GO; GO:0008939; F:nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02145; BluB; 1.
DR CDD; cd02439; DMB-PRT_CobT; 1.
DR Gene3D; 1.10.1610.10; -; 1.
DR Gene3D; 3.40.50.10210; -; 1.
DR Gene3D; 3.40.109.10; NADH Oxidase; 1.
DR HAMAP; MF_00230; CobT; 1.
DR InterPro; IPR012825; BluB.
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 InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR NCBIfam; TIGR02476; BluB; 1.
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 Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; FMN-dependent nitroreductase-like; 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:UP000037251};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00230}.
FT DOMAIN 144..310
FT /note="Nitroreductase"
FT /evidence="ECO:0000259|Pfam:PF00881"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 669
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ SEQUENCE 701 AA; 74082 MW; 8962043D7404A114 CRC64;
MPEAQARFVA ADAPAGPLPQ PHADQPLGQF VPVEGSVPTT PHLAPAPAQA LTLPPEALEA
PEAAEPVAAV PTPREGDPEL VQHAEDLDTR AADQEDPQDP QNPQDPQDQE EMSTAPVEDV
RQSTGPAAPA YDDAEREAVL KVMRERRDIR NGFRSDPIPH EVLLRVLEAA HTAPSVGHSQ
PWDFVVIRSA ETRGSMHELA MRQRDAYAKS LPKGRAKQFK ELKIEAILDT PVNIVVTADP
TRGGRHTLGR HTQPQMAPYS AALAVENLWL AARAEGLGVG WVSFFDEREM VRALGLPEHL
EVIAYLCVGY VDEFPDEPEL MQAGWSKRRP LSWVVHEETY GRRALPGEEP HDLLGETVAQ
IRPLDAKALG EAWERQKRMT KPAGALGMLE IISAQLSGLS RQCPPPIPEP AAVAIFAGDH
GVHAQGVTPW PQEVTAQMVA NFLGGGAVCN AFAAQVGAEV CVVDVGVAAD LPATPGLLPR
KVRAGTSDMT TGSAMTREEA KQAIEVGIET ARDLVAAGNK ALLTGEMGIA NTTASAALIS
VFTDADPAEV TGRGTGINDE TLARKTEVVR RALELHQPDP ADPIGVLAAI GGFEHAAIVG
LLLGGASLRT PVILDGVSAG AAALVARAIA PEVLAACIAG HRSAEPGHVA ALNKLGLRPL
VDLDLRLGEG TGALLALPLV QSTARAMHEV ATFDSAGVTE K
//
