ID A0A0T6A6M2_9BACT Unreviewed; 414 AA.
AC A0A0T6A6M2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN ORFNames=XU15_C0003G0120 {ECO:0000313|EMBL:KRT70746.1};
OS candidate division NC10 bacterium CSP1-5.
OC Bacteria; candidate division NC10.
OX NCBI_TaxID=1640516 {ECO:0000313|EMBL:KRT70746.1, ECO:0000313|Proteomes:UP000051123};
RN [1] {ECO:0000313|EMBL:KRT70746.1, ECO:0000313|Proteomes:UP000051123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-5 {ECO:0000313|EMBL:KRT70746.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the NadC/ModD family.
CC {ECO:0000256|ARBA:ARBA00009400}.
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:KRT70746.1}.
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DR EMBL; LDXR01000003; KRT70746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6A6M2; -.
DR STRING; 1640516.XU15_C0003G0120; -.
DR PATRIC; fig|1640516.3.peg.573; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000051123; Unassembled WGS sequence.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01571; NAPRTase_B; 1.
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; IPR035809; NAPRTase_arc-type.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR PANTHER; PTHR43202:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43202; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE; 1.
DR Pfam; PF01729; QRPTase_C; 1.
DR Pfam; PF02749; QRPTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 2.
DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:KRT70746.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRT70746.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRT70746.1}.
FT DOMAIN 34..111
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 113..301
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
FT REGION 387..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 45304 MW; 09BABF59C5348013 CRC64;
MYHCTSYDAI KAGRVTDIYF ARTLEILKAE GLDKPVKAEF IAKNLPEDWT WAVLAGVEEV
AALADGMKVN IRAMDEGTVF RPWEPVLEIE GMYTDFCVYE TAMLGLICQA SGIATMAARC
RLAAGGRSLI SFGARRMHPI LAPLIERNAF IGGCDGVSVG EGAELIGQPP MGTMPHALVL
MYGDTVEATK AFDRVVPADV KRISLIDTFQ DEKFEAIRVA SALGDRLYGV RLDTPGSRRG
DFKRIAQEVR WELDLRGFTH VKIFVSGGIG ERQIRELNPV VDGYGVGTAI SDAPVVDFSM
DIVEIDNVPL AKRGKPSGAK QVYRCQLCHQ DRVTPQAHGS PVCECGGRME RLLNRWIERG
NLVGPLPSAA RIRQRVLDQL RWIGRLDEPQ SPREPAPKGV EERATGAVAG TVAA
//
