ID A0A1H3DIG6_9PSEU Unreviewed; 435 AA.
AC A0A1H3DIG6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05421504_103406 {ECO:0000313|EMBL:SDX66205.1};
OS Amycolatopsis xylanica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=589385 {ECO:0000313|EMBL:SDX66205.1, ECO:0000313|Proteomes:UP000199515};
RN [1] {ECO:0000313|EMBL:SDX66205.1, ECO:0000313|Proteomes:UP000199515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 202699 {ECO:0000313|EMBL:SDX66205.1,
RC ECO:0000313|Proteomes:UP000199515};
RA de Groot N.N.;
RL Submitted (OCT-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; FNON01000003; SDX66205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3DIG6; -.
DR STRING; 589385.SAMN05421504_103406; -.
DR OrthoDB; 9770610at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000199515; Unassembled WGS sequence.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
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 InterPro; IPR002638; Quinolinate_PRibosylTrfase_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 Pfam; PF01729; QRPTase_C; 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:SDX66205.1};
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:UP000199515};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:SDX66205.1}.
FT DOMAIN 15..139
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 144..313
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
SQ SEQUENCE 435 AA; 46205 MW; 7DF198AC2CD42FD2 CRC64;
MASENGTEAV TSTALLTDHY ELTMLSSALA DGTADRPCVF EVFARRLPDG RRYGVVAGTA
RVLDAIADFK FTDAEIGQLE STAVVDAETL EWLANYSFGG DIEGYPEGEL YFPNSPILTV
TGGFAEAVVL ETLVLSILNH DSAIASAAAR MSSAAHGRPI IEMGGRRTHE WAAVAAARAS
YLAGFATTSN LEAGRRYGIP TRGTVAHAFM LLHASEEEAF RAQIAKMGPD TTLLVDTYDI
STGIDTAVRV AGKELGAIRI DSGDVGVLAR QAREQLDSLG ARDTRIVVSG DLDEHAIAAL
RAEPVDAYGV GTSVVTGSGA PTAGMVYKLV EVDGRPVAKR SAQKISRGGR KAAIRRHKST
GTAVEEVIYT VDGPVPDSDE YDRALQIPLV RAGQTVDDLP TLDDARARLR RALVSLPWEG
LKLSHGEPAI PTLFL
//