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Database: UniProt
Entry: A0A0D1C1Q2_USTMA
LinkDB: A0A0D1C1Q2_USTMA
Original site: A0A0D1C1Q2_USTMA 
ID   A0A0D1C1Q2_USTMA        Unreviewed;       302 AA.
AC   A0A0D1C1Q2;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating] {ECO:0000256|PIRNR:PIRNR006250};
DE            EC=2.4.2.19 {ECO:0000256|PIRNR:PIRNR006250};
DE   AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|PIRNR:PIRNR006250};
GN   ORFNames=UMAG_04262 {ECO:0000313|EMBL:KIS67767.1};
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS67767.1, ECO:0000313|Proteomes:UP000000561};
RN   [1] {ECO:0000313|EMBL:KIS67767.1, ECO:0000313|Proteomes:UP000000561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA   de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA   Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA   Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA   Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA   Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA   Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA   Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA   Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA   Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2] {ECO:0000313|Proteomes:UP000000561}
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC       {ECO:0000256|PIRNR:PIRNR006250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate;
CC         Xref=Rhea:RHEA:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29959, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC         ChEBI:CHEBI:58017; EC=2.4.2.19;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006250};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from quinolinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004893, ECO:0000256|PIRNR:PIRNR006250}.
CC   -!- SUBUNIT: Hexamer formed by 3 homodimers.
CC       {ECO:0000256|PIRNR:PIRNR006250}.
CC   -!- SIMILARITY: Belongs to the NadC/ModD family.
CC       {ECO:0000256|ARBA:ARBA00009400, ECO:0000256|PIRNR:PIRNR006250}.
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DR   EMBL; CM003151; KIS67767.1; -; Genomic_DNA.
DR   RefSeq; XP_011390730.1; XM_011392428.1.
DR   AlphaFoldDB; A0A0D1C1Q2; -.
DR   STRING; 237631.A0A0D1C1Q2; -.
DR   EnsemblFungi; KIS67767; KIS67767; UMAG_04262.
DR   GeneID; 23564501; -.
DR   KEGG; uma:UMAG_04262; -.
DR   VEuPathDB; FungiDB:UMAG_04262; -.
DR   eggNOG; KOG3008; Eukaryota.
DR   InParanoid; A0A0D1C1Q2; -.
DR   OMA; DIVMCDN; -.
DR   OrthoDB; 5473389at2759; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000000561; Chromosome 12.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IBA:GO_Central.
DR   GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR   GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central.
DR   CDD; cd01572; QPRTase; 1.
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; IPR004393; NadC.
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   NCBIfam; TIGR00078; nadC; 1.
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   PIRSF; PIRSF006250; NadC_ModD; 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   ECO:0000256|PIRNR:PIRNR006250};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|PIRNR:PIRNR006250};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          36..120
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          122..297
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   302 AA;  32944 MW;  8189A07DB57CD266 CRC64;
     MSTSIPVYAN LLPPSWKVKV SEWLAEDCPS FDWGGFVVGE DKKRATLFCK SEGILAGVPF
     FDEVFKQLDC RVSWNFREGE WLKAATAGAK VKIAVATVEG PSRKILLGER VALNTLARCS
     GIATASGLFL KKARDAGYNG IVAGTRKTTP GFRDVEKYGM LVGGVDMHRY DLSSMVMLKD
     NHIWSTGSVT NAVHSARSVC GFSLRIDVEV QSYQEAVQAI EAGADVIMLD NMEGETLISN
     AKRLKHEWSG KHKFLLESSG GIDIDNVQQG GHVDNSIDII STSSIHQSTK HVDFSLKIDP
     SS
//
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