ID A0A1C4K8N9_9ACTN Unreviewed; 588 AA.
AC A0A1C4K8N9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00015486};
DE EC=2.4.2.21 {ECO:0000256|ARBA:ARBA00011991};
DE AltName: Full=N(1)-alpha-phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00030686};
DE Flags: Fragment;
GN ORFNames=GA0115251_11324 {ECO:0000313|EMBL:SCD57771.1};
OS Streptomyces sp. TverLS-915.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839763 {ECO:0000313|EMBL:SCD57771.1, ECO:0000313|Proteomes:UP000198957};
RN [1] {ECO:0000313|EMBL:SCD57771.1, ECO:0000313|Proteomes:UP000198957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TverLS-915 {ECO:0000313|EMBL:SCD57771.1,
RC ECO:0000313|Proteomes:UP000198957};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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};
CC -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC ribazole from 5,6-dimethylbenzimidazole: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005049}.
CC -!- SIMILARITY: Belongs to the CobT family.
CC {ECO:0000256|ARBA:ARBA00007110}.
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DR EMBL; FMCE01000122; SCD57771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4K8N9; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000198957; Unassembled WGS sequence.
DR GO; GO:0008939; F:nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity; IEA:UniProtKB-EC.
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};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:SCD57771.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198957};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SCD57771.1}.
FT DOMAIN 31..197
FT /note="Nitroreductase"
FT /evidence="ECO:0000259|Pfam:PF00881"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SCD57771.1"
SQ SEQUENCE 588 AA; 62050 MW; 20A808D27E8B3001 CRC64;
ASAPVPPQAP AGPPAPGYDE AEREAVLRVM RERRDIRNGF RSDPIPHEVL LRVLEAAHTA
PSVGHSQPWD FVVIRSEETR RAMHELAEKQ RDAYAASLPK GRAKQFRELK IEAILDTPVN
IVVTADPTRG GRHTLGRHTQ PQMAPYSSAL AVENLWLAAR AEGLGVGWVS FFDEREMVRA
LGLPEHLEVV AYLCVGYVDE FPDEPELMQA GWSKRRPLSW VVHEETYGRR VLPGAEPADL
LTETVRRIRP LDAKALGEAW ERQKRMTKPP GALGMLEIIS AQLSGLSRTS PPPIPEPAAV
AIFAGDHGVH AQGVTAWPQE VTAQMVANFL GGGAVCNAFA KQVGAEVCVV DVGVAAELPP
TPGLLPRKVR AGTADMTAGP ALSREDVTAA IEVGIETARD LVAAGNKALL TGEMGIANTT
ASAALISVFT GTDPAEVTGR GTGINDEMHA HKIDVIRRAL DLHRPDPADP IGVLAAVGGL
EHAAMAGLLL GGASLRTPVI LDGVSAGAAA LVARAIAPEV LAACIAGHRS AEPGHVAALN
SLGLRPLVDL DLRLGEGTGA LLALPLVQSA ARAMHEVATF DSAGVTEK
//
