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Database: UniProt
Entry: G0EFT4_PYRF1
LinkDB: G0EFT4_PYRF1
Original site: G0EFT4_PYRF1 
ID   G0EFT4_PYRF1            Unreviewed;       298 AA.
AC   G0EFT4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
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   OrderedLocusNames=Pyrfu_0383 {ECO:0000313|EMBL:AEM38255.1};
OS   Pyrolobus fumarii (strain DSM 11204 / 1A).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Pyrolobus.
OX   NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM38255.1, ECO:0000313|Proteomes:UP000001037};
RN   [1] {ECO:0000313|EMBL:AEM38255.1, ECO:0000313|Proteomes:UP000001037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX   PubMed=21886865;
RA   Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA   Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H.,
RA   Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT   Pyrolobus fumarii type strain (1A).";
RL   Stand. Genomic Sci. 4:381-392(2011).
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; CP002838; AEM38255.1; -; Genomic_DNA.
DR   RefSeq; WP_014025932.1; NC_015931.1.
DR   AlphaFoldDB; G0EFT4; -.
DR   STRING; 694429.Pyrfu_0383; -.
DR   GeneID; 11140029; -.
DR   KEGG; pfm:Pyrfu_0383; -.
DR   eggNOG; arCOG01482; Archaea.
DR   HOGENOM; CLU_039622_2_0_2; -.
DR   InParanoid; G0EFT4; -.
DR   OMA; LYDMIML; -.
DR   OrthoDB; 115072at2157; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000001037; Chromosome.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01568; QPRTase_NadC; 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:UP000001037};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          19..105
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          107..278
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   298 AA;  32955 MW;  E7C4C37B3E49186E CRC64;
     MSYELFYREF LRWLREDIPE WDLTTEAVRL RGVKARGRIV CKSGCVAACV EEVAYSLERL
     GLSVELQARS GEWVEPGSDM MLLVGDAATI LEVERVTLNT LIYACSIATT TRRLVEMVRR
     VNPRVRVAAT RKTVPGFRYC SKRAVEAGGG DTHRLTLSDA ILVKDNHVAL IGSVGEAVRR
     VVGRKSFVHR VEVEVHNVEE ALAAVETGAD AILIDNQPPS VVRAILEELE KRGLRDRVVV
     EVSGGITSEN ILEYARLNVD VISTSFITMS PERVDISLVV EPLDNRREGG SPGTRALS
//
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