ID   A0A183QZ74_9TREM        Unreviewed;       533 AA.
AC   A0A183QZ74;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|ARBA:ARBA00033102};
OS   Schistosoma rodhaini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000899401-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SROB_0000899401-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A183QZ74; -.
DR   STRING; 6188.A0A183QZ74; -.
DR   WBParaSite; SROB_0000899401-mRNA-1; SROB_0000899401-mRNA-1; SROB_0000899401.
DR   UniPathway; UPA00253; -.
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          32..109
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          111..273
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
FT   REGION          294..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  57681 MW;  4BBF92F079987CFD CRC64;
     MACPLVINKN SVKALAAWWL SNESSLNYVG LTPKSGRGKV YIDMHSPGII VGMPFVDAIL
     KESSCEIEWH VCEGQTVKSC PVRVATISGA DEDVFFCENL VISVLSRASG IATLASRIQL
     ILQEVSWKGT IYMPDRRTPG FGLVEEYAMM ISGVSERKAS VSVRCQNMDA ESLKTAIDEV
     RSRVGSIPVH VACSRLDEAC LAAGAGADIL LTGLSAKEIL DIATQVKESF PEIQVIASGF
     FDDSDVKLCA TRYVDHLTSL KLCNGYAFVD FQMAYVKDKL VENAETTNFV VLLEENESPS
     PPKSKSPGPQ PTEEVASSIP APLKKPRLVD DEGDTPKSAK LNGTPTRNTN PTAPDPNWST
     FPNAANAQNQ KRVQRILRHP QYTPPQRSNV PRSQTPGGFP FFMSNPRLMP PTSTPTRAPA
     MLLQPGLNIN NQVSNVLTPP SNQQNISMRL PMVPPQLQQP PQSMSQRMPS NPPGMLNTNQ
     PMGGGFLNNI QPPHNQPPNW QMIPGGPGGH PMGAIGLGMR VGGPGGQNVN NCR
//