ID A0A2I0SWU9_9ACTN Unreviewed; 1220 AA.
AC A0A2I0SWU9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=CW362_03550 {ECO:0000313|EMBL:PKT74363.1};
OS Streptomyces populi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2058924 {ECO:0000313|EMBL:PKT74363.1, ECO:0000313|Proteomes:UP000236178};
RN [1] {ECO:0000313|EMBL:PKT74363.1, ECO:0000313|Proteomes:UP000236178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A249 {ECO:0000313|EMBL:PKT74363.1,
RC ECO:0000313|Proteomes:UP000236178};
RA Wang Z.;
RT "Streptomyces populusis sp. nov., a novel endophytic actinobacterium
RT isolated from stems of Populus adenopoda Maxim.";
RL Submitted (DEC-2017) 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:PKT74363.1}.
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DR EMBL; PJOS01000004; PKT74363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0SWU9; -.
DR OrthoDB; 9773807at2; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000236178; 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:UP000236178};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00230}.
FT DOMAIN 662..829
FT /note="Nitroreductase"
FT /evidence="ECO:0000259|Pfam:PF00881"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ SEQUENCE 1220 AA; 124858 MW; 2C8C9655BB565AC7 CRC64;
MTDTGQVPGE GLPENAGMVE QPGVAAPGAY TFLDASENPV EDDDLLLLPG APGAQGAWGN
EVPPPAPMPF TDEPGPHETD GRDTGAIDLG AVRAPSPAPV PQPVPQPVAP RRPLHLGPPT
PDGSSSPVRS LADRGPAGAR PGSMTTPVVP LHQAGPPTVG PEYLDVPQSA EAPPQSAAPW
GTVPAGGEVM AAETAAPGTV VPETGQLPGS AVDAEPVPDP ELPGAAEAEQ APAVVAEHLV
HDSVPAPDAA QAPAPEADAA PLGLQDRTDD PAPEAVPATD GPDAPQFQDA PETPGAPDTA
DAVTGIASGA ETPVPEVVPA QLAEDAGPAV PHAPAEEPVP AEDAAAQAPE QPADQDTDGA
GPAEPVVQEA EPVAPAPEQA VPLVDEASLP GDEQPVGAPV PHPYETPDSA LSALSARSAD
ASQSGQDITP DAAEAQQFTD RPAPAENGAV PAEEAAAHDG TDLPGPGSAE TPQAAPVEAD
APTEAVGRAD GDPHPESGTD PAAGVPGFPG APVVPQADQS LGHFVPVEGT VPTAAHLAPT
PPHGVTVPPA VEEQPPAQEP AQAAVTVAPV PAEETPVAEA EPVAQASVPA PREAEAEPEG
VSVPQPLTAE PEPVAAQQAE DLRTQGADQE EGTAVVEEVR ESTGPAAPGF NDAEREAVLR
VIRERRDIRN GFRDDPIPHD VLLRVLEAAH TAPSVGHSQP WDFVVIRSAE TRRSMHELAQ
RQREAYAKSL PKGRAKQFKE MKIEAILDTP VNVVVTADPT RGGRHTLGRH TQPQMAPYSA
ALAVENFWLA ARAEGLGVGW VSFFDEREMV RALGLPDHLE VVAYLCVGYV DEFPEEPELM
QAGWSKRRPL SWVVHEETYG RRALPGEEPH DLLAETVSNI RPLDAKALGE AWERQKRMTK
PAGALGMLEI ISAQLSGLSR MCPPPIPEPA AVAIFAGDHG VHAQGVTPWP QEVTGQMVAN
FLGGGAVCNA FANQVGAEVC VVDVGVASDL PATPGLLPRK VRAGTADMTT GPAMTREEAV
AALEVGIETA RDLVAAGNKA LLTGEMGIAN TTASAALISV FTGADPAEVT GRGTGINDET
LARKTEVVRR AIEFHQPDPA DPIGVLAAIG GLEHAAMVGL LLGGASLRTP VILDGVSAGA
AALVARAIAP EVLAACIAGH RSAEPGHVAA LNKLGLRPLI DLDLRLGEGT GALLALPVVQ
SAARAMHEVA TFDSAGVTEK
//