ID A0A182P4P9_9DIPT Unreviewed; 761 AA.
AC A0A182P4P9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00021569};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI001885-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI001885-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI001885-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182P4P9; -.
DR STRING; 199890.A0A182P4P9; -.
DR EnsemblMetazoa; AEPI001885-RA; AEPI001885-PA; AEPI001885.
DR VEuPathDB; VectorBase:AEPI001885; -.
DR OrthoDB; 1333333at2759; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
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:SF1; 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; 2.
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}.
FT DOMAIN 32..159
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 533..633
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 638..746
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
FT REGION 377..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 84789 MW; 5277751728B47ECA CRC64;
MSLNRELSED SAFAAGRNSW NRHYHNSVVQ PLLTDLYQIT MAYAYWKSGK IDDQAVFDLF
FRTNPFQGEF TIFAGLEECL KFLDSFHYSE TDIEYLKHAL PQGIEDEFFE YLSHLTAKDV
TLYAIEEGSV AFPRVPLIKV AGPLIIVQLL ETTLLTLVNY ASLMATNAAR YRMVAGKHIH
LLEFGLRRAQ GPDGGLSASK YSYIGGFDGT SNVLAGKLFN IPVKGTHAHA YITSFTGIDE
LKTRVLPHKE DGTTRDLLEL AMEHRAALAS VLDVSTDESS EGELAAMVSF AIAFPDGFMA
LVDTYDVKSD KLLGEVADEL CEPADSVVCD SLCSGRLHDQ DGNDSVHPPS TILPEIPEEE
CNGCCAEDDD AQTQCTLHAE SEQQEDGEQV EEESSAQDEP DPEESCPPPS ITVEDENDAV
TPAEEFELPA VKESDENGNE DIEDQNIRST TEEKEEVDDL TALESANPVP EDTEEEVEEE
VGGEDENFRC ANCEALNTMI HHLKSVGKSF RSGLLNFCAV ALALNDQGYR AIGIRIDSGD
LAYLSCLARE TFERIAERFK LPWFSKLTIV ASNDINEETI LSLNEQGHKI DCFGIGTHLV
TCQRQPALGC VYKMVEINNQ PRIKLSQDVG KVTMPGSKNV FRLYGADGHA LIDLLQRVDE
NPPEVGQKVL CRHPFQESKR AYVIPTQVEP LYRVYWTEGR VAQVLPSLEE VRERVQASLR
TLRQDHKRTL NPTPYKVAVS DNLYNFIHEL WLQNAPIGEL S
//
