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Database: UniProt
Entry: A0A0T6A7V4_9BACT
LinkDB: A0A0T6A7V4_9BACT
Original site: A0A0T6A7V4_9BACT 
ID   A0A0T6A7V4_9BACT        Unreviewed;       385 AA.
AC   A0A0T6A7V4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE            EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN   ORFNames=XU15_C0002G0269 {ECO:0000313|EMBL:KRT71097.1};
OS   candidate division NC10 bacterium CSP1-5.
OC   Bacteria; candidate division NC10.
OX   NCBI_TaxID=1640516 {ECO:0000313|EMBL:KRT71097.1, ECO:0000313|Proteomes:UP000051123};
RN   [1] {ECO:0000313|EMBL:KRT71097.1, ECO:0000313|Proteomes:UP000051123}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSP1-5 {ECO:0000313|EMBL:KRT71097.1};
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:KRT71097.1}.
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DR   EMBL; LDXR01000002; KRT71097.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6A7V4; -.
DR   STRING; 1640516.XU15_C0002G0269; -.
DR   PATRIC; fig|1640516.3.peg.321; -.
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:KRT71097.1};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRT71097.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRT71097.1}.
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"
SQ   SEQUENCE   385 AA;  42472 MW;  5113CA431BE349F3 CRC64;
     MFHTAREDDI KAGRITDVYF LRTLEILDRE KIDAVVEAEV TLKAFPESWT WGILAGIEEV
     AGLLTGLPVD VDAFREGSSF RVGEPILTVR GPYREWGHYE TAILGLLCQA SGIATKAARC
     KRAADGRTVI SFGARRMHPV LAPMIERNAF IGGCDGVAVV KSAELIKEEP VGTMPHTLVL
     ILGDTVKAAK AFDASIDPRV KRVVLIDTLS DEKFEALRVA EALGERLFAV RLDTPSSRRG
     DMLEILREVR WELNYRGFSW VKLFISGGLD EAEIQRLNPL ADAYGVGTAI SNAPVMNFAL
     DLVEIDGRPI AKRGKRSGRK AAYRCRGCRL RWVLPADASP PACPCGDSVE SLLMPLLRNG
     CIVRKLPTTQ EIRSRVLEEL DYLAL
//
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