ID A0A1S9ZQG7_9GAMM Unreviewed; 345 AA.
AC A0A1S9ZQG7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=B0180_01860 {ECO:0000313|EMBL:OOR85557.1};
OS Moraxella canis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=90239 {ECO:0000313|EMBL:OOR85557.1, ECO:0000313|Proteomes:UP000190322};
RN [1] {ECO:0000313|EMBL:OOR85557.1, ECO:0000313|Proteomes:UP000190322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 8415A {ECO:0000313|EMBL:OOR85557.1,
RC ECO:0000313|Proteomes:UP000190322};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Moore E.;
RT "Draft genome sequence of Moraxella canis CCUG 8415A type strain.";
RL Submitted (FEB-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|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:OOR85557.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MUXT01000001; OOR85557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9ZQG7; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000190322; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00230}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 251..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00230"
SQ SEQUENCE 345 AA; 36807 MW; B41A073AAB5CE962 CRC64;
MWYLDPTKPI NQHMRTQAQK RQDKLTKPAG SLGEMETVVI QLAGMQGKVC PTADKPYMCT
FAGDHGIASL GVSAYPQTVT RQMLYNFAQG GACISVMARH YGAISRVIDC GTLGGAYEAH
GIDQQPIAPS THNFLERAAM SDDDCQRALV IGKNSVEEAV ALGADIYIAG EMGIGNTTSS
SVLAGLLLGE RADQLTGLGT GIDEATFNFK RAVIDQAIDL YQHNEPLTYL QSVAGFEMAA
MVGAYLRAAQ LGMPVIIGGF ISAVCALCAV RINPGVRDYM LFSHKSAEYG NQLVLDALEA
RPLIDLGLRL GEGTGAMTAF GIIQLACTVH RDMSTFDEAG VSDRS
//
