COBT_PSEAB
ID COBT_PSEAB Reviewed; 351 AA.
AC Q02JC0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00230};
DE Short=NN:DBI PRT {ECO:0000255|HAMAP-Rule:MF_00230};
DE EC=2.4.2.21 {ECO:0000255|HAMAP-Rule:MF_00230};
DE AltName: Full=N(1)-alpha-phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00230};
GN Name=cobT {ECO:0000255|HAMAP-Rule:MF_00230}; OrderedLocusNames=PA14_47670;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
CC -!- FUNCTION: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from
CC nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00230};
CC -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC ribazole from 5,6-dimethylbenzimidazole: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00230}.
CC -!- SIMILARITY: Belongs to the CobT family. {ECO:0000255|HAMAP-
CC Rule:MF_00230}.
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DR EMBL; CP000438; ABJ10467.1; -; Genomic_DNA.
DR RefSeq; WP_003082601.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02JC0; -.
DR SMR; Q02JC0; -.
DR EnsemblBacteria; ABJ10467; ABJ10467; PA14_47670.
DR KEGG; pau:PA14_47670; -.
DR HOGENOM; CLU_002982_0_1_6; -.
DR OMA; AWMRKCA; -.
DR BioCyc; PAER208963:G1G74-4005-MON; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0008939; F:nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02439; DMB-PRT_CobT; 1.
DR Gene3D; 1.10.1610.10; -; 1.
DR Gene3D; 3.40.50.10210; -; 1.
DR HAMAP; MF_00230; CobT; 1.
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 Pfam; PF02277; DBI_PRT; 1.
DR SUPFAM; SSF52733; SSF52733; 1.
DR TIGRFAMs; TIGR03160; cobT_DBIPRT; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glycosyltransferase; Transferase.
FT CHAIN 1..351
FT /note="Nicotinate-nucleotide--dimethylbenzimidazole
FT phosphoribosyltransferase"
FT /id="PRO_1000021612"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00230"
SQ SEQUENCE 351 AA; 36526 MW; DDDF387B9F1283AC CRC64;
MSLQWWRDTC READPQMRRR AAERQDRLTK PRGSLGRLEQ VAIDLAALQG RERPSLERLW
VTVFAGDHGV VAEGVSAYPQ AVTGEMLRNF VRGGAAISVL ARELGAGLEV VDLGTAVPLE
ALPGVRHLRL AAGTANFVEA PAMGAEQCLL ALEAGRESVR RAEQAGSQLF IGGEMGIGNT
TAAAAMACAL LDAPVSALVG PGTGLDASGV AHKTAVIERA LALHGAHRAD PFETLRRLGG
LEIAALAGAY LACAQKGMVA LVDGYICSVA ALCAVRLNPA CRDWLLFAHS GAEPGHRHVL
EALAAQPLLD LGLRLGEGSG AALAVPLLRQ ACALHAGMAT FAEAAVSDRP A
