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Database: UniProt
Entry: A0A172Q8S9_9STRE
LinkDB: A0A172Q8S9_9STRE
Original site: A0A172Q8S9_9STRE 
ID   A0A172Q8S9_9STRE        Unreviewed;       490 AA.
AC   A0A172Q8S9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
DE            EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
GN   ORFNames=A0O21_07300 {ECO:0000313|EMBL:AND79832.1};
OS   Streptococcus pantholopis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1811193 {ECO:0000313|EMBL:AND79832.1, ECO:0000313|Proteomes:UP000077317};
RN   [1] {ECO:0000313|EMBL:AND79832.1, ECO:0000313|Proteomes:UP000077317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA 26 {ECO:0000313|EMBL:AND79832.1,
RC   ECO:0000313|Proteomes:UP000077317};
RX   PubMed=27226124; DOI=10.1099/ijsem.0.001189;
RA   Bai X., Xiong Y., Lu S., Jin D., Lai X., Yang J., Niu L., Hu S., Meng X.,
RA   Pu J., Ye C., Xu J.;
RT   "Streptococcuspantholopis sp. nov., isolated from faeces of the Tibetan
RT   antelope (Pantholops hodgsonii).";
RL   Int. J. Syst. Evol. Microbiol. 66:3281-3286(2016).
RN   [2] {ECO:0000313|Proteomes:UP000077317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA 26 {ECO:0000313|Proteomes:UP000077317};
RA   Bai X.;
RT   "Streptococcus antelopensis sp. nov., isolated from the feces of the
RT   Tibetan antelope (Pantholops hodgsonii) in Hoh Xil National Nature Reserve,
RT   Qinghai, China.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC       nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC       ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC       {ECO:0000256|RuleBase:RU365100}.
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         ECO:0000256|RuleBase:RU365100};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU365100}.
CC   -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC       cycle. Phosphorylation strongly increases the affinity for substrates
CC       and increases the rate of nicotinate D-ribonucleotide production.
CC       Dephosphorylation regenerates the low-affinity form of the enzyme,
CC       leading to product release. {ECO:0000256|RuleBase:RU365100}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family.
CC       {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU365100}.
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DR   EMBL; CP014699; AND79832.1; -; Genomic_DNA.
DR   RefSeq; WP_067063635.1; NZ_CP014699.1.
DR   AlphaFoldDB; A0A172Q8S9; -.
DR   STRING; 1811193.A0O21_07300; -.
DR   KEGG; spat:A0O21_07300; -.
DR   OrthoDB; 9770610at2; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000077317; Chromosome.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01570; NAPRTase_A; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041525; N/Namide_PRibTrfase.
DR   InterPro; IPR041619; NAPRTase_C.
DR   InterPro; IPR040727; NAPRTase_N.
DR   InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR   InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   NCBIfam; TIGR01513; NAPRTase_put; 1.
DR   PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   Pfam; PF17956; NAPRTase_C; 1.
DR   Pfam; PF17767; NAPRTase_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   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000313|EMBL:AND79832.1};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365100};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|RuleBase:RU365100};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077317};
KW   Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:AND79832.1}.
FT   DOMAIN          9..132
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          154..333
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   DOMAIN          358..467
FT                   /note="Nicotinate phosphoribosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17956"
SQ   SEQUENCE   490 AA;  55200 MW;  1202EA5A0E4B903D CRC64;
     MYTDDSLTLH TDLYQINMMQ VYFEQGIHNK KAVFEAYFRK EPFANGYAVF AGLERLIQYL
     EGLSFTASDI AYLERLGYPQ DFLSYLKNLK LDLSIRSAKE GDLVFANEPI VQVEGSLAQC
     QLVETALLNI INFQTLIATK AARIRSVIED EPLLEFGTRR AQELDAAIWG TRAAVIGGAD
     ATSNVRAGKL FDIPVSGTHA HALVQAYGND YEAFKAYAKT HKDCVFLVDT YDTLKIGVPS
     AIRVAQEMGD KISFKGVRLD SGDLAYLSKE VRKQLDAAGF TDAKIYASND LDENTILNLK
     MQKAKIDVWG VGTKLITAYD QPALGAVYKI VSIEDENGVM QDTIKLSNNA EKVSTPGKKQ
     VWRITSREKG KSEGDYITFA ETDVNHLDEI VMFHPTYTYI SKTIKNFKAV PLLVDIYQQG
     RLVYDLPTLA EIKEYAKKEL DGLWNEYKRV LNPQDYPVDL AQDVWDNKMN LIDRVRQSAY
     DSAEEERKSL
//
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