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Database: UniProt
Entry: A0A267DFL5_9PLAT
LinkDB: A0A267DFL5_9PLAT
Original site: A0A267DFL5_9PLAT 
ID   A0A267DFL5_9PLAT        Unreviewed;       605 AA.
AC   A0A267DFL5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|ARBA:ARBA00033102};
GN   ORFNames=BOX15_Mlig016991g2 {ECO:0000313|EMBL:PAA47946.1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA47946.1, ECO:0000313|Proteomes:UP000215902};
RN   [1] {ECO:0000313|EMBL:PAA47946.1, ECO:0000313|Proteomes:UP000215902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DV1 {ECO:0000313|EMBL:PAA47946.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:PAA47946.1};
RA   Berezikov E.;
RT   "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT   model organism for stem cell research.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC       {ECO:0000256|ARBA:ARBA00003237}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004790}.
CC   -!- SIMILARITY: Belongs to the NadC/ModD family.
CC       {ECO:0000256|ARBA:ARBA00009400}.
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:PAA47946.1}.
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DR   EMBL; NIVC01004281; PAA47946.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A267DFL5; -.
DR   STRING; 282301.A0A267DFL5; -.
DR   UniPathway; UPA00253; -.
DR   Proteomes; UP000215902; Unassembled WGS sequence.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.90.1170.20; Quinolinate phosphoribosyl transferase, N-terminal domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR027277; NadC/ModD.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR   InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR   InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR   PANTHER; PTHR32179; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE [CARBOXYLATING]; 1.
DR   PANTHER; PTHR32179:SF3; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE [CARBOXYLATING]; 1.
DR   Pfam; PF01729; QRPTase_C; 1.
DR   Pfam; PF02749; QRPTase_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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          66..138
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          141..304
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
FT   REGION          353..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   605 AA;  61337 MW;  B1F87EBD5DD647BD CRC64;
     MTHITSLSAI KNIVKLWIEE DNIISNSGGV FVQFDSNASR LNFHNTGENG QTCEDDTEVN
     SFNEHPVLCA VIFETKGVLA GVPFADALLT RLRCEASWSV AEGAYISSVP QRVATISGSP
     VCLARARRLL PAVLSRASGL ATYANRLVEK AALCDWPGSV CADSDSRCTP GQRLLERHGL
     LVGGVRPSAS STASTGGAVV IVDTTAAGGG GGSGVASALA GARRCAAPFG RVAAVCADEA
     EALRACRLGA DLVMLECSSA EVCTAAARAV KAAHPGTLVQ ARQLAASDLA AYFTADIDVV
     CVDASPAQLR SDWPEVALRP IAAGTAAFSD AAATAAVAAA AVAAAAAMPA RKRRRCASQD
     SNPPRPPTAP VLGSTAAATA AAAAAAVAKQ PRLDLATSAT GSAGVGGGSS NPTTPTPQMV
     NSCRELVPVF NTDRRNSQQS EQSEQPQQRR QRRESPPQPP LSAAASAAAS AAVSAAVAAS
     AARAAAAVAG GAARPAAVLS VPYGFLRVPV SGVAGTPIRM VAPQSRAAAA AAAAAAAAAA
     AYRNAQHRQP MTPAAAMAMR FGSVGYGTSV SAAQLLMGPW LCKVCRGANM YTTVCRHCSR
     NRGLY
//
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