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Database: UniProt
Entry: A0A2I0SWU9_9ACTN
LinkDB: A0A2I0SWU9_9ACTN
Original site: A0A2I0SWU9_9ACTN 
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
//
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