ID A0A2A4KCT4_9ACTN Unreviewed; 1210 AA.
AC A0A2A4KCT4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=CIB93_33890 {ECO:0000313|EMBL:PCG81718.1};
OS Streptomyces sp. WZ.A104.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2023771 {ECO:0000313|EMBL:PCG81718.1, ECO:0000313|Proteomes:UP000217525};
RN [1] {ECO:0000313|EMBL:PCG81718.1, ECO:0000313|Proteomes:UP000217525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZ.A104 {ECO:0000313|EMBL:PCG81718.1,
RC ECO:0000313|Proteomes:UP000217525};
RA Xu L., He S., Yan X.;
RT "Isolation and Genomic Analysis of a Bioactive Actinomycete Associated with
RT Cyanobacterium Lyngbya cf. aestuarii.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000217525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZ.A104 {ECO:0000313|Proteomes:UP000217525};
RA Jiao Y., Han B.;
RL Submitted (SEP-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:PCG81718.1}.
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DR EMBL; NWVL01000102; PCG81718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4KCT4; -.
DR OrthoDB; 9773807at2; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000217525; 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:UP000217525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00230}.
FT DOMAIN 653..819
FT /note="Nitroreductase"
FT /evidence="ECO:0000259|Pfam:PF00881"
FT REGION 1..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..460
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ SEQUENCE 1210 AA; 124181 MW; 4219CA38A2788B1E CRC64;
MTDTGQIPGE GLPENAGMVE QPGIPAPDAY TFLDPSEHTP EDDDLLLMPT SQGAWSDPPA
APAPAPEQTT PAPAPAVAQQ PPAQAPAPEQ PAQQIQPQPQ QYAAQPQPQA PVQGQTAPAP
AEPHGTHESG GRDSGSVDVS AVRIPAPAPA PAPVGAHAAA TASAPVGPAP ARRPLHRGPA
SAEAPSYAGG TQGGGVVRSL ADRGPAGAVR TASPARHAGP PTTGPEYFDV PVEDSSALPG
PQLGEIPPQG GAPWGAPQPS EPAGPAAVAA GATEPAEPTA SARTAGPVAA EPVVEQPVQR
EQPAQVEQPE QLQQPERAAQ PGQIERAEQM EQAEPVAPME SAEPAEPAEP AEPVEPPQQA
IPEETVVPEA AQPEAPVEAV IQPPAEQPSE APAPVAQTPE VPDAGAEAPV EPLAPEPLAV
AAEAAPTHAT APEPQAEAPA SAPDAAPAEP IAPAPASAPD AAPAEPIAEP IAVAEPVTPA
EPVAVADQAP PVAPEPATAP EPAPVVVVAE TPEAAAPAAE PGTQPEARPE PSATDIPAPT
PVQATQAAEP DAEDGTGPEI IETPELTEPD QPAQADEQTD QPAAPEQAEA PQQAEAPQQS
EASQQGEASR SAEEVTELST SPAPAPAPDP APVTAPAPGY DDAEREAVLR VMRERRDIRN
GFRSDPIPHE VLLRVLEAAH TAPSVGHSQP WDFVVIRSAE TRRSMHELAQ SQRDAYAKSL
PKGRAKQFKE LKIEAILDTP VNIVVTADPT RGGRHTLGRH TQPQMAPYSS ALAVENLWLA
ARAEGLGVGW VSFFDEREMV RALGLPEHLE VVAYLCVGYV DEFPEEPELM QAGWSKRRPL
SWVVHEETYG RRALPGEEPH DLLQETISAI RPLDAKALGE AWERQKRMTK PAGALGMLEI
ISAQLSGLSR MCPPPIPEPA AVAIFAGDHG VHAQGVTAWP QEVTAQMVAN FLGGGAVCNA
FAAQVGAEVC VVDVGVATDL PATPGLLPRK VRPGTADFTT GPALTREEVL AAIEVGIETA
RDLVAAGNKA LLTGEMGIAN TTASAALICV YTGIDAAEVT GRGTGINDEM HARKVDVVRR
ALDLHQPDPA DPIGVLAAVG GLEHAAMAGF LLGGASLRTP VILDGVSAGA AALVARAIAP
EALAACIAGH RSAEPGHVAA LNKLGLRPLV DLDLRLGEGT GALLALPIVQ SAARAMHEVA
TFDSAGVTEK
//
