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Database: UniProt
Entry: A0A0C1UR11_9CYAN
LinkDB: A0A0C1UR11_9CYAN
Original site: A0A0C1UR11_9CYAN 
ID   A0A0C1UR11_9CYAN        Unreviewed;       459 AA.
AC   A0A0C1UR11;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=QQ91_014610 {ECO:0000313|EMBL:NEV68343.1};
OS   Lyngbya confervoides BDU141951.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX   NCBI_TaxID=1574623 {ECO:0000313|EMBL:NEV68343.1, ECO:0000313|Proteomes:UP000031561};
RN   [1] {ECO:0000313|EMBL:NEV68343.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BDU141951 {ECO:0000313|EMBL:NEV68343.1};
RA   Malar M.C., Sen D., Tripathy S.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:NEV68343.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BDU141951 {ECO:0000313|EMBL:NEV68343.1};
RX   PubMed=25745003;
RA   Chandrababunaidu M.M., Sen D., Tripathy S.;
RT   "Draft Genome Sequence of Filamentous Marine Cyanobacterium Lyngbya
RT   confervoides Strain BDU141951.";
RL   Genome Announc. 3:e00066-e00015(2015).
RN   [3] {ECO:0000313|EMBL:NEV68343.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BDU141951 {ECO:0000313|EMBL:NEV68343.1};
RA   Sarangi A.N., Ghosh S., Mukherjee M., Tripathy S.;
RL   Submitted (FEB-2020) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NEV68343.1}.
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DR   EMBL; JTHE02000003; NEV68343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1UR11; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000031561; Unassembled WGS sequence.
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; 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:NEV68343.1};
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}.
FT   DOMAIN          15..142
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          163..278
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   DOMAIN          383..441
FT                   /note="Nicotinate phosphoribosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17956"
SQ   SEQUENCE   459 AA;  49612 MW;  72C940322B2DA772 CRC64;
     MSLSPLQVLP EDYSLLTDLY QLTMSACYVG EGLDQRRASF ELFTRRLPPN FGYLIAMGLT
     QAIEYLEAFT FSDRHLEQLQ ATGIFAHAPA AFWETLRHAK FTGDVWAVPE GTAVFANEPL
     LRIEAPLWQA QVVETYLLNT LNYQTLIATR AARLRDVAGP EAKLLEFGTR RAFSPQGALW
     AARAAIAGGL DSTSNVLAAL QLGQKPTGTM AHALVMAIAA LEGSETDAFE AFHRYFPGAP
     LLIDTFNTVA AAQHLANQRQ QGQAALAGVR LDSGDIAGLS QQVRELLPDI PIFASGDIDE
     YEIVRLKQSG AVIDGYGLGT RLVTGSPVNG VYKLVEIDGI PVMKESSSKV TYPGRKQIFR
     QYAGDRATHD FLALTTESPP PGAQPLLQPV MQQGQLITPL EDLPAIAQRT AQSVASLSPA
     VRQVQDPGPY TVETTPALAQ LTQATRHQTK STVPSGGQS
//
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