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Database: UniProt
Entry: B2J8Z4_NOSP7
LinkDB: B2J8Z4_NOSP7
Original site: B2J8Z4_NOSP7 
ID   B2J8Z4_NOSP7            Unreviewed;       471 AA.
AC   B2J8Z4;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 96.
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   OrderedLocusNames=Npun_F5709 {ECO:0000313|EMBL:ACC84010.1};
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC84010.1, ECO:0000313|Proteomes:UP000001191};
RN   [1] {ECO:0000313|Proteomes:UP000001191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACC84010.1, ECO:0000313|Proteomes:UP000001191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RX   PubMed=23463784; DOI=10.1104/pp.112.213116;
RA   Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.;
RT   "A Nostoc punctiforme Sugar Transporter Necessary to Establish a
RT   Cyanobacterium-Plant Symbiosis.";
RL   Plant Physiol. 161:1984-1992(2013).
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; CP001037; ACC84010.1; -; Genomic_DNA.
DR   RefSeq; WP_012411953.1; NC_010628.1.
DR   AlphaFoldDB; B2J8Z4; -.
DR   STRING; 63737.Npun_F5709; -.
DR   EnsemblBacteria; ACC84010; ACC84010; Npun_F5709.
DR   KEGG; npu:Npun_F5709; -.
DR   eggNOG; COG1488; Bacteria.
DR   HOGENOM; CLU_025154_3_1_3; -.
DR   OrthoDB; 9770610at2; -.
DR   PhylomeDB; B2J8Z4; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000001191; 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; 3.
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:ACC84010.1};
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:UP000001191};
KW   Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:ACC84010.1}.
FT   DOMAIN          30..157
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          179..297
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   DOMAIN          396..453
FT                   /note="Nicotinate phosphoribosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17956"
SQ   SEQUENCE   471 AA;  51099 MW;  D4751BFEFF354F7F CRC64;
     MTTLPDLDYV YKQQSQQNQE LNLSADDYSL LTDLYQLTMA ACYTGEGIEQ RRASFELSVR
     RLPEGFGYLI AMGLTQALEY LAKIRFSSAQ IAALQATGIF AHAGDRFWSL LAEGKFTGDV
     WAVPEGTAVF ANQPLLRVEA PLWQAQLVET YLLNTINYQT LIATKAARLR DIAGESATLL
     EFGTRRAFSP QGSLWAARAA LAGGLDSTSN VLAALQLGQQ PSGTMAHALV MALSAIEGTE
     EQAFSAFHRY FPGAPLLIDT YDTIAAAGRL AEKVNSGEMQ LTGVRLDSGD LVTLSKQVRS
     LLPGVPIFAS GDLDEWEIAR LKAAGAEIDG YGLGTRLVTG SPVNGVYKLV DIDGIPVMKQ
     SSGKVTYPGR KQIFRSYTGG KVKADRLGLL GESSQEEEPL LQLVVQEGQR VQPLESLATI
     RQRTAVSVAS LPQQTRLLDH PVAVEVEISE ALRVLTEETK KRTAEALSTQ R
//
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