ID A0A2M8IU55_9RHOB Unreviewed; 236 AA.
AC A0A2M8IU55;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00015486};
DE EC=2.4.2.21 {ECO:0000256|ARBA:ARBA00011991};
DE AltName: Full=N(1)-alpha-phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00030686};
GN ORFNames=CVM52_24280 {ECO:0000313|EMBL:PJE34047.1};
OS Pseudooceanicola lipolyticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=2029104 {ECO:0000313|EMBL:PJE34047.1, ECO:0000313|Proteomes:UP000231553};
RN [1] {ECO:0000313|EMBL:PJE34047.1, ECO:0000313|Proteomes:UP000231553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=157 {ECO:0000313|EMBL:PJE34047.1,
RC ECO:0000313|Proteomes:UP000231553};
RX PubMed=29219804; DOI=10.1099/ijsem.0.002521;
RA Huang M.-M., Guo L.-L., Wu Y.-H., Lai Q.-L., Shao Z.-Z., Wang C.-S., Wu M.,
RA Xu X.-W.;
RT "Pseudooceanicola lipolyticus sp. nov., a marine alphaproteobacterium,
RT reclassification of Oceanicola flagellatus as Pseudooceanicola flagellatus
RT comb. nov. and emended description of the genus Pseudooceanicola.";
RL Int. J. Syst. Evol. Microbiol. 68:409-415(2018).
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};
CC -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC ribazole from 5,6-dimethylbenzimidazole: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005049}.
CC -!- SIMILARITY: Belongs to the CobT family.
CC {ECO:0000256|ARBA:ARBA00007110}.
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:PJE34047.1}.
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DR EMBL; PGTB01000250; PJE34047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8IU55; -.
DR OrthoDB; 9781491at2; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000231553; Unassembled WGS sequence.
DR GO; GO:0008939; F:nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1610.10; -; 1.
DR Gene3D; 3.40.50.10210; -; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003200; Nict_dMeBzImd_PRibTrfase.
DR InterPro; IPR023195; Nict_dMeBzImd_PRibTrfase_N.
DR InterPro; IPR036087; Nict_dMeBzImd_PRibTrfase_sf.
DR InterPro; IPR029903; RmlD-like-bd.
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; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52733; Nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase (CobT); 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000231553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 139..232
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 236 AA; 25028 MW; EF1709486C7F3A45 CRC64;
MRSDLTDLSH LRRLLAQAPG PDTAALEGAT ARNGQLTKPP GALGRLEELA IWYAGWRGDP
RPRIAAPQVI VFAGNHGVAA QGVSAFPPEV TEQMVLNFRA GGAAINQLAE AAGAKMDVHA
LDLDQPTADF TQTPAMSEAA CLAALRGLMA DPARTGTYHF AGAPDVSWAG FARAIFEQAG
VDCAVEDIPT EAYPTPAARP KNSRLDCRSF EAAFGLARPD WRAGLREILA ELGEMR
//