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Database: UniProt
Entry: A0A1M6H0P6_9ACTN
LinkDB: A0A1M6H0P6_9ACTN
Original site: A0A1M6H0P6_9ACTN 
ID   A0A1M6H0P6_9ACTN        Unreviewed;       450 AA.
AC   A0A1M6H0P6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN02745244_01850 {ECO:0000313|EMBL:SHJ15694.1};
OS   Tessaracoccus bendigoensis DSM 12906.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Tessaracoccus.
OX   NCBI_TaxID=1123357 {ECO:0000313|EMBL:SHJ15694.1, ECO:0000313|Proteomes:UP000184512};
RN   [1] {ECO:0000313|EMBL:SHJ15694.1, ECO:0000313|Proteomes:UP000184512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12906 {ECO:0000313|EMBL:SHJ15694.1,
RC   ECO:0000313|Proteomes:UP000184512};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQZG01000029; SHJ15694.1; -; Genomic_DNA.
DR   RefSeq; WP_073187410.1; NZ_FQZG01000029.1.
DR   AlphaFoldDB; A0A1M6H0P6; -.
DR   STRING; 1123357.SAMN02745244_01850; -.
DR   OrthoDB; 9770610at2; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000184512; Unassembled WGS sequence.
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; 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:SF8; NICOTINATE PHOSPHORIBOSYLTRANSFERASE PNCB1; 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:SHJ15694.1};
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:UP000184512};
KW   Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:SHJ15694.1}.
FT   DOMAIN          5..128
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
SQ   SEQUENCE   450 AA;  48091 MW;  589B2E395C93EC8F CRC64;
     MTTALLTDHY ELTMVQAALD AGTANRRSLF DLFTRRLPEG RRYGVVAGLG RALDAIDAFR
     FGDAELGFLL ERGIIRENLA DWLSDFRFTG DIWGYPEGEV YFPGSPVLSV EGTFAEACIL
     ETVLLSIYNH DSAIAAAGSR MTAMAGERSC AEMGSRRAGE WAAVAAARAA YITGFASTSN
     LEAGRTYGIP TIGTAAHSFT LLHDTEEEAF SAQIDSLGED TTLLVDTYDV EAAIRKGIEL
     TGGRLGAIRL DSGDLAIMAR QARDLLDDLG ATHTRIMVTS DLDEWQIALL QGAPVDGYGV
     GTSLVTGSGH PTCGFVYKLV ARASSDEPDA ALISVGKRSK GKNTLGGRKF AMRRRGEDGR
     AESEVIGLGA PPANDGNDRD LLIPIVTGGE RVYSATLEDA RRRHIDSLAE LPLAARRISK
     GDPALETLIL DETGTLTTNP YQAAPVVTNI
//
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