ID U1QKW1_9EURY Unreviewed; 352 AA.
AC U1QKW1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=J07HN4v3_03248 {ECO:0000313|EMBL:ERH07603.1};
OS Halonotius sp. J07HN4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halonotius.
OX NCBI_TaxID=1070774 {ECO:0000313|EMBL:ERH07603.1, ECO:0000313|Proteomes:UP000030639};
RN [1] {ECO:0000313|EMBL:ERH07603.1, ECO:0000313|Proteomes:UP000030639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HN4 {ECO:0000313|Proteomes:UP000030639};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
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}.
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DR EMBL; KE356578; ERH07603.1; -; Genomic_DNA.
DR AlphaFoldDB; U1QKW1; -.
DR eggNOG; ENOG502N5NH; Archaea.
DR HOGENOM; CLU_002982_0_0_2; -.
DR UniPathway; UPA00061; UER00516.
DR Proteomes; UP000030639; 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 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};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:ERH07603.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030639};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ERH07603.1}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 352 AA; 35511 MW; CED11E8C486E57CC CRC64;
MTDGESRSAE AAATDVSIPP LDDTAREAAA ERQQQLLKPP GSLGRLEAMA VEIAAMQATP
TPSVDPAVLF TLAADHGVTA EGISAYPASV TAAMVNAVES GDAAINALAA ANDIDTHVVD
MGVDGDIPES VIDHHIADGT ANMASEPAMT AVHARESIAA GRALVADHAA KAGVIGLGDL
GIGNTTASAA ITAALTDTTV AEVTGHGTGI DEATRQHKIE TIEQALAGTD TDDPLDVLRC
VGGFEIGGLV GVTLEAASRR IPVAVDGVIT GAAALVAAEI NERVTAYLLG SHVSTEPGHA
VQLEQLKLEP CIEYEMGLGE GTGAAVAIGT YRAACRSHTE MATFADVGVD SA
//
