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Database: UniProt
Entry: A0A1H3DIG6_9PSEU
LinkDB: A0A1H3DIG6_9PSEU
Original site: A0A1H3DIG6_9PSEU 
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
//
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