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Database: UniProt
Entry: A0A1Y0IN26_9BACL
LinkDB: A0A1Y0IN26_9BACL
Original site: A0A1Y0IN26_9BACL 
ID   A0A1Y0IN26_9BACL        Unreviewed;       481 AA.
AC   A0A1Y0IN26;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=CBW65_06365 {ECO:0000313|EMBL:ARU60754.1};
OS   Tumebacillus avium.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1903704 {ECO:0000313|EMBL:ARU60754.1, ECO:0000313|Proteomes:UP000195437};
RN   [1] {ECO:0000313|Proteomes:UP000195437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR23208 {ECO:0000313|Proteomes:UP000195437};
RA   Sung H.;
RL   Submitted (MAY-2017) 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; CP021434; ARU60754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0IN26; -.
DR   KEGG; tum:CBW65_06365; -.
DR   OrthoDB; 9770610at2; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000195437; 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:ARU60754.1};
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   Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:ARU60754.1}.
FT   DOMAIN          6..131
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          154..341
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   DOMAIN          359..468
FT                   /note="Nicotinate phosphoribosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17956"
SQ   SEQUENCE   481 AA;  54344 MW;  568D662FD1266C37 CRC64;
     MENLTLNTDN YQLAMAYAHF QNGTHNQQTV FEMYFRNLPF GSGYAVFAGL ERVAAYLRSL
     HFSDEMILFL QKQPEGYSAE FLEELRNFRF TGTLRAVREG SVVFPNEPLL QVEARVLEAQ
     IIETALLNAV NFQTLIATKA ARIRQEVGPE SYLIEMGTRR AHEADAAVWG TRAAYIAGFD
     STSNMQAGMQ FGIPTKGTHA HSWVQTHETE LEAFRRFAEV FPESTTLLVD TYNTLGSGLP
     NAIQVAKELE QRGKKLFGIR LDSGDIAYQS KVARKMLDEA GLSYVKIAAS NDLDEHTILH
     LKVQGAQVDI WGVGTKLITA YDQPALGGVY KLVERELHGK MEPSIKISGN PEKITTPYRK
     KVYRILNARG KAQGDYLALP EETDVTKGER IKLFDPVHTH VHKFVEGYTA VPLLETIFDE
     GKLVYALPEI GAVKAYHQTQ LEQFDGEYLR NLNPEKYHVN LSERLWTRKR ELIEMYGEAA
     R
//
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