ID A0A061P5Y3_9BACL Unreviewed; 366 AA.
AC A0A061P5Y3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN ORFNames=JCM19038_4141 {ECO:0000313|EMBL:GAK10252.1};
OS Geomicrobium sp. JCM 19038.
OC Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX NCBI_TaxID=1460635 {ECO:0000313|EMBL:GAK10252.1, ECO:0000313|Proteomes:UP000027014};
RN [1] {ECO:0000313|EMBL:GAK10252.1, ECO:0000313|Proteomes:UP000027014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19038 {ECO:0000313|EMBL:GAK10252.1,
RC ECO:0000313|Proteomes:UP000027014};
RA Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA Hongoh Y., Hattori M., Ohkuma M.;
RT "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL Genome Announc. 2:e00622-14(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide +
CC phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:456216; EC=6.3.4.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001240};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952}.
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:GAK10252.1}.
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DR EMBL; BAXA01000024; GAK10252.1; -; Genomic_DNA.
DR RefSeq; WP_042421022.1; NZ_BAXA01000024.1.
DR AlphaFoldDB; A0A061P5Y3; -.
DR eggNOG; COG1488; Bacteria.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000027014; Unassembled WGS sequence.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.90.1170.20; Quinolinate phosphoribosyl transferase, N-terminal domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR PANTHER; PTHR43202:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43202; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE; 1.
DR Pfam; PF02749; QRPTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 1.
DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:GAK10252.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000027014};
KW Transferase {ECO:0000313|EMBL:GAK10252.1}.
FT DOMAIN 41..115
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
SQ SEQUENCE 366 AA; 41117 MW; 77811A71FBE68A17 CRC64;
MKEIELKLQG KIQRLTNKTF KFDERVGEGW FSAVYFLKTR DIIRKYKPDN IVTMQFFQKK
HAVLCGTDEA IALIQTFADH PEKLEIHSLK DGDRIEPFEP VLTIKGAYHD FGFLEGVIDG
IFSRRTSVAT NVYEVVKAAR TSGVQKPVIF MGDRDDHFTQ QAGDGYAAFI GGSKAQATHA
MNEWWGKSGM GTMPHALIQL FHGDVVAASH AYKEMFPDDQ LMALVDYNND AVTDALRVAR
EFGKELHSVR LDTSNYMVDQ YFCRNPHKMG DFDPTGVNGP LIQALRDALD EEGFKHVNIT
VSGGFTAERI EAYERAGVPV NVYGVGRSLL EKTIGFTGDN VMLDGVHEAK AGRKLRENPR
LERITF
//