ID C1EAT4_MICCC Unreviewed; 310 AA.
AC C1EAT4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=MICPUN_83796 {ECO:0000313|EMBL:ACO65259.1};
OS Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO65259.1, ECO:0000313|Proteomes:UP000002009};
RN [1] {ECO:0000313|EMBL:ACO65259.1, ECO:0000313|Proteomes:UP000002009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
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; CP001328; ACO65259.1; -; Genomic_DNA.
DR RefSeq; XP_002504001.1; XM_002503955.1.
DR AlphaFoldDB; C1EAT4; -.
DR STRING; 296587.C1EAT4; -.
DR GeneID; 8244949; -.
DR KEGG; mis:MICPUN_83796; -.
DR eggNOG; KOG3008; Eukaryota.
DR InParanoid; C1EAT4; -.
DR OMA; DIVMCDN; -.
DR OrthoDB; 5473389at2759; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000002009; Chromosome 7.
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; 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:UP000002009};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT DOMAIN 42..129
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 131..306
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 150..152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 271..273
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 292..294
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ SEQUENCE 310 AA; 32607 MW; B0890AB21CBBB898 CRC64;
MSAPMSAGEA AALPYTIAPP AHPTYSIADA IKLALEEDIA DVGDISSLST IPEATVSTAT
LLAKADGVLA GQALCNQILA AVDPDVTVSW SKLDGDVIGK GDIFCEMTGK AHSILRAERV
LLNFMQRMSG IATLTKAMAD AAAPAYMLET RKTVPGLRLP DKWAVLIGGG KNHRMGLFDM
IMIKDNHIAA SGGIDKAVAN AQNFLKERGM DGVKIEVETR TMDEVRQIVD LLDDEAVVTS
AVSRVMLDNM SLDDMREAVA LIGGRVETEA SGNVTLETVH AIGQTGVTFI SSGALTHSVV
ACDISLNIST
//
