ID A0A0X3XKI3_9ACTN Unreviewed; 1283 AA.
AC A0A0X3XKI3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=ADL34_26740 {ECO:0000313|EMBL:KUL70860.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL70860.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL70860.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL70860.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL70860.1}.
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DR EMBL; LLZN01000079; KUL70860.1; -; Genomic_DNA.
DR RefSeq; WP_062739822.1; NZ_LLZN01000079.1.
DR OrthoDB; 9773807at2; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000052945; 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:UP000052945};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00230}.
FT DOMAIN 726..892
FT /note="Nitroreductase"
FT /evidence="ECO:0000259|Pfam:PF00881"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1251
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ SEQUENCE 1283 AA; 131439 MW; 91B9459942A77C16 CRC64;
MTDTGQVPGE GLPESAGMVE QPGVPGAPDA YSYLSETPAE EEDLLLPGSQ GAWGNEVAPP
APEPVVEAVH EPDAHELSGR DSGSVDLTGV RLPGPSAPAP TAPTTPIPPI TPRRPLHLGP
PIPDASASPV RSLADRGAVG MPARQPGHAV PEYAETQAPP QAAAWGAPAP AQVGTEAQAA
ETVVPAAEPV GAAQAVVARV ATEAGAATGV PQAAEAGAVA QVAEGQTPVA QDGTYGAPEP
SPEHAAAVPG QAGAPAPVAH EPQGPHENAA ASAMTGGNAQ DAAEPQAVAA TPQDARPGEP
AQVPAGPEVS EAPEAQQGAE TPVPEAAPVA AEPAEPEAVA PDAVMSEAAA PADARPVAES
APAAAVQEAL AQETPVPEAP AQEIPVPAAP APVAEAPEPA PHDVEAPAGV AAPVAEAAEA
QPQPEPAQTP EPAPEPLAET YAPEPVAEAH TPEPAQALPP QVQPSEDVPA EAPDVSDVPE
QAEPRPAATA VPEQPEPEAL AEAPEPAAQA PAAEEAAVPP SEPGPAEQPA QIPDAVAAQP
EQPLPEAPEA VPAEAVQPLA AAAAPEPVTV EQYAAEQYAA EQYVAEPAGP QLRQAAGPDD
VLAVMPGAVP QEPPPGQPLG QFVPVEGTVP TTPHLAPTPP QPLVLPTEES PAPAAEVPAP
READPGLVQH ADDLDTRVAD EDRADEEARA EEAQDAPAEE EPHRPGGPAA PAYDDAEREA
VLKVMRERRD IRNGFRSDPI PHEVLLRVLE AAHTAPSVGH SQPWDFVVIR SSETRRTVHE
LAMRQREAYA KSLPKGRAKQ FKELKIEAIL DTPVNIVVTA DPTRGGRHTL GRHTQPQMAP
YSAALAVENL WLAARAEGLG VGWVSFFDER EMVRALGLPE HLEVIAYLCV GYVDEFPDEP
ELLQAGWSKR RPLSWVVHEE TYGRRALPGE EPHDLLAETV SQIRPLDAKA LGEAWERQKR
MTKPAGALGM LEIISAQLSG LSRQCPPPIP EPAAVAIFAG DHGVHAQGVT PWPQEVTAQM
VANFLGGGAV CNAFAAQVGA EVCVVDVGVA ADLPATPGLL PRKVRAGTAD MTTGPAMTRE
EAKQAVEVGI ETARDLVAAG NKALLTGEMG IANTTASAAL ISLYTGTDPA EVTGRGTGIN
DETLARKTEV VRRALEFHQP DPADPIGVLA AIGGLEHAAL VGLLLGGASL RTPVILDGVS
AGAAALVARA IAPEVLAACI AGHRSAEPGH VAALNKLGLR PLVDLDLRLG EGTGALLALP
LVQSTARAMH EVATFDSAGV TEK
//
