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Database: UniProt
Entry: A0A1H1LHB6_9CORY
LinkDB: A0A1H1LHB6_9CORY
Original site: A0A1H1LHB6_9CORY 
ID   A0A1H1LHB6_9CORY        Unreviewed;       479 AA.
AC   A0A1H1LHB6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=SAMN04488539_0214 {ECO:0000313|EMBL:SDR73923.1};
OS   Corynebacterium timonense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=441500 {ECO:0000313|EMBL:SDR73923.1, ECO:0000313|Proteomes:UP000182237};
RN   [1] {ECO:0000313|EMBL:SDR73923.1, ECO:0000313|Proteomes:UP000182237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45434 {ECO:0000313|EMBL:SDR73923.1,
RC   ECO:0000313|Proteomes:UP000182237};
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; LT629765; SDR73923.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1LHB6; -.
DR   STRING; 1203190.GCA_000312345_00556; -.
DR   eggNOG; COG1488; Bacteria.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000182237; Chromosome i.
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   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; 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; PF04095; NAPRTase; 1.
DR   Pfam; PF17767; NAPRTase_N; 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:SDR73923.1};
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:UP000182237};
KW   Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:SDR73923.1}.
FT   DOMAIN          49..169
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          190..377
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
SQ   SEQUENCE   479 AA;  51111 MW;  E803BA34473B7CB2 CRC64;
     MSTLPTGTLR PQHGIYAPIT AGAVPAMLRV TWDAMTNPTS HSHASTAFLT DMYELTMLDA
     ALQDGTAQRQ CSFEVFSRKL PGERRYGVVA GTARILEALS RFRFTREQLE AADFLSDTAK
     DYLSNYSFSG HIDGYREGEL YFPYSPIMTV RGTFAECVIL ETIILSILNS DSAVASAASR
     MVTAADGRPI MEMGSRRTNE SAAVSAARAA YIAGFDTTSN MEAATRYGIP PAGTAAHAWM
     LLHVDEDGTP DEKAAFRAQV DSLGPGTTLL VDTFDITQGV ANALEAAGTE LGAVRIDSGD
     LGIVSRRVRS QLDQAGAYNT KIIVSSDLDE FAIAGLRGDP VDGFGVGTSV VTGSGSPTAG
     MVYKLVEVEG HPVAKRSSGK ITYGGTKSAL RAYRSSGVAV SELVCPFDSQ ITQRPGLEYR
     RMDIPLMRDG AVVEGLGGLD AAREHLAEAR TTLPWEGLAL SRDEPAIATH FVGFPEPED
//
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