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Database: UniProt
Entry: A0A2T7CUZ5_9POAL
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ID   A0A2T7CUZ5_9POAL        Unreviewed;       657 AA.
AC   A0A2T7CUZ5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE            EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN   ORFNames=GQ55_7G141300 {ECO:0000313|EMBL:PUZ47158.1};
OS   Panicum hallii var. hallii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC   Panicum sect. Panicum.
OX   NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ47158.1, ECO:0000313|Proteomes:UP000244336};
RN   [1] {ECO:0000313|EMBL:PUZ47158.1, ECO:0000313|Proteomes:UP000244336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA   Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA   Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA   Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA   Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT   "WGS assembly of Panicum hallii var. hallii HAL2.";
RL   Submitted (APR-2018) 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       Helps prevent cellular oxidative stress via its role in NAD
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00023426}.
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   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004952}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family.
CC       {ECO:0000256|ARBA:ARBA00010897}.
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DR   EMBL; CM009755; PUZ47158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7CUZ5; -.
DR   STRING; 1504633.A0A2T7CUZ5; -.
DR   EnsemblPlants; PUZ47158; PUZ47158; GQ55_7G141300.
DR   Gramene; PUZ47158; PUZ47158; GQ55_7G141300.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000244336; Chromosome 7.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01570; NAPRTase_A; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 2.
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:SF23; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   Pfam; PF17956; NAPRTase_C; 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   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244336}.
FT   DOMAIN          126..252
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          426..526
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   DOMAIN          531..642
FT                   /note="Nicotinate phosphoribosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17956"
FT   REGION          31..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   657 AA;  72116 MW;  895F06E9705E881E CRC64;
     MTSRGAGVVC LFPPVHACRL QLLQRINTVR LPAKPPNSHP APASPASFRS PVVSSRLPSP
     PGAEASPAPS SAKPTLGGAA SQELFREARM AATSAPHTSA HANGNGTHAG MAAQVGAPTN
     PMATALLTDQ YQFSMAYAYW KAGKHADRAV FDLYFRKNPF GGEFTVFAGL EECIKFIANF
     KFTEHDISFL QSVMPMCEGE FFDYLREVDC SDVEVYSIPE GSVVFPKVPL MRVEGPVAVV
     QLLETPFVNL INYASLVTTN AARHRHVAGK SKVLLEFGLR RAQGPDGAIS ASKYCFMGGF
     DATSNVLAGN LFGIPLRGTH SHAFISSYMS LDEIPDKALR SKDGSRVCQD FVSLVQEWLQ
     KIQVADSLGG VFGDTNQSEL AAFVSYALAF PSNFLALVDT YDVMRSGIPN FCAVALALHD
     LGYKASGIRL DSGDLAYLSI EARKVFRAVE EEFNVPGFGK MVITASNDLN EETIDALNKQ
     GHEVDAFGIG TYLVTCYSQA ALGCVFKLVE INSKPRIKLS EDVAKVSIPC KKRCFRLYGK
     EGYPLVDIMI RESEPSPKAG ERILCRHPFI ESKRAYVVPQ HVEELLQCYW PGRSDKPRAE
     LPSLDKIRSR CMQQLEKLRP DHIRRLNPTP YKVSVSAKLY DFIHCLWLNE APVGELQ
//
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