ID PNCB_THEAC Reviewed; 392 AA. AC Q9HJ28; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 120. DE RecName: Full=Putative nicotinate phosphoribosyltransferase; DE Short=NAPRTase; DE EC=6.3.4.21 {ECO:0000250|UniProtKB:P22253}; GN OrderedLocusNames=Ta1145; OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC OS 15155 / AMRC-C165). OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales; OC Thermoplasmataceae; Thermoplasma. OX NCBI_TaxID=273075; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165; RX PubMed=11029001; DOI=10.1038/35035069; RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.; RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma RT acidophilum."; RL Nature 407:508-513(2000). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES WITH RP NICOTINATE MONONUCLEOTIDE AND PRPP, DOMAIN, AND SUBUNIT. RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165; RX PubMed=15753098; DOI=10.1074/jbc.m501622200; RA Shin D.H., Oganesyan N., Jancarik J., Yokota H., Kim R., Kim S.H.; RT "Crystal structure of a nicotinate phosphoribosyltransferase from RT Thermoplasma acidophilum."; RL J. Biol. Chem. 280:18326-18335(2005). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC. RG Berkeley structural genomics center (BSGC); RT "Crystal structure of a zinc ion bound nicotinate phosphoribosyltransferase RT from Thermoplasma acidophilum."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide CC from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of CC ATP. {ECO:0000250|UniProtKB:P22253}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + CC nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + CC phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017, CC ChEBI:CHEBI:456216; EC=6.3.4.21; CC Evidence={ECO:0000250|UniProtKB:P22253}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D- CC ribonucleotide from nicotinate: step 1/1. CC {ECO:0000250|UniProtKB:P22253}. CC -!- SUBUNIT: Homodimer. Forms a trimer of dimers in the crystal. CC {ECO:0000269|PubMed:15753098}. CC -!- DOMAIN: Consists of three domains, an N-terminal domain, a central CC functional domain, and a unique C-terminal domain containing a zinc CC knuckle-like motif containing 4 cysteines. CC {ECO:0000269|PubMed:15753098}. CC -!- PTM: Transiently phosphorylated on a His residue during the reaction CC cycle. Phosphorylation strongly increases the affinity for substrates CC and increases the rate of nicotinate D-ribonucleotide production. CC Dephosphorylation regenerates the low-affinity form of the enzyme, CC leading to product release. {ECO:0000250|UniProtKB:P22253}. CC -!- SIMILARITY: Belongs to the NAPRTase family. Highly divergent. CC {ECO:0000305}. CC -!- CAUTION: Although this protein is stated to be a nicotinate CC phosphoribosyltransferase, it has not been functionally characterized, CC and it might be a quinolinate phosphoribosyltransferase (QPRTase). CC {ECO:0000305|PubMed:15753098}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL445066; CAC12271.1; -; Genomic_DNA. DR RefSeq; WP_010901554.1; NC_002578.1. DR PDB; 1YTD; X-ray; 2.80 A; A=1-392. DR PDB; 1YTE; X-ray; 2.75 A; A=1-392. DR PDB; 1YTK; X-ray; 2.65 A; A=1-392. DR PDB; 2I1O; X-ray; 2.40 A; A=1-392. DR PDBsum; 1YTD; -. DR PDBsum; 1YTE; -. DR PDBsum; 1YTK; -. DR PDBsum; 2I1O; -. DR AlphaFoldDB; Q9HJ28; -. DR SMR; Q9HJ28; -. DR STRING; 273075.gene:9572367; -. DR PaxDb; 273075-Ta1145; -. DR EnsemblBacteria; CAC12271; CAC12271; CAC12271. DR GeneID; 1456649; -. DR KEGG; tac:Ta1145; -. DR eggNOG; arCOG01481; Archaea. DR HOGENOM; CLU_043773_0_0_2; -. DR InParanoid; Q9HJ28; -. DR OrthoDB; 371831at2157; -. DR BRENDA; 6.3.4.21; 6324. DR UniPathway; UPA00253; UER00457. DR EvolutionaryTrace; Q9HJ28; -. DR Proteomes; UP000001024; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01571; NAPRTase_B; 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; IPR035809; NAPRTase_arc-type. DR InterPro; IPR007229; Nic_PRibTrfase-Fam. DR InterPro; IPR036068; Nicotinate_pribotase-like_C. DR InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf. DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C. DR PANTHER; PTHR43202:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR43202; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE; 1. DR Pfam; PF01729; QRPTase_C; 1. DR PIRSF; PIRSF000484; NAPRT; 1. DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1. DR SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase; Zinc. FT CHAIN 1..392 FT /note="Putative nicotinate phosphoribosyltransferase" FT /id="PRO_0000410976" FT BINDING 21 FT /ligand="nicotinate" FT /ligand_id="ChEBI:CHEBI:32544" FT /evidence="ECO:0000305|PubMed:15753098" FT BINDING 138 FT /ligand="nicotinate" FT /ligand_id="ChEBI:CHEBI:32544" FT /evidence="ECO:0000305|PubMed:15753098" FT BINDING 179 FT /ligand="nicotinate" FT /ligand_id="ChEBI:CHEBI:32544" FT /evidence="ECO:0000305|PubMed:15753098, FT ECO:0007744|PDB:1YTK" FT BINDING 235 FT /ligand="nicotinate" FT /ligand_id="ChEBI:CHEBI:32544" FT /evidence="ECO:0000305|PubMed:15753098, FT ECO:0007744|PDB:1YTK" FT BINDING 240 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000305|PubMed:15753098" FT BINDING 272 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000305|PubMed:15753098, FT ECO:0007744|PDB:1YTK" FT BINDING 293 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000305|PubMed:15753098, FT ECO:0007744|PDB:1YTK" FT BINDING 330 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|Ref.3" FT BINDING 330 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.3" FT BINDING 333 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|Ref.3" FT BINDING 348 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.3" FT BINDING 350 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|Ref.3" FT BINDING 350 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.3" FT MOD_RES 182 FT /note="Phosphohistidine" FT /evidence="ECO:0000250|UniProtKB:P22253" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 9..13 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 21..29 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 30..35 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 37..44 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 57..64 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 91..98 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 99..102 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 106..130 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 148..157 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 166..172 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 182..188 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 190..199 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 217..225 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 233..236 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 246..259 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 265..272 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 275..283 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 288..291 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 293..296 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 303..310 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 325..330 FT /evidence="ECO:0007829|PDB:2I1O" FT TURN 331..333 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 336..340 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:1YTK" FT STRAND 349..352 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 359..363 FT /evidence="ECO:0007829|PDB:2I1O" FT STRAND 366..369 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 374..384 FT /evidence="ECO:0007829|PDB:2I1O" FT HELIX 385..388 FT /evidence="ECO:0007829|PDB:2I1O" SQ SEQUENCE 392 AA; 43297 MW; CC9BCD4E77E7C9AA CRC64; MNVFNTASDE DIKKGLASDV YFERTISAIG DKCNDLRVAM EATVSGPLDT WINFTGLDEV LKLLEGLDVD LYAIPEGTIL FPRDANGLPV PFIRVEGRYC DFGMYETAIL GFICQASGIS TKASKVRLAA GDSPFFSFGI RRMHPAISPM IDRSAYIGGA DGVSGILGAK LIDQDPVGTM PHALSIMLGD EEAWKLTLEN TKNGQKSVLL IDTYMDEKFA AIKIAEMFDK VDYIRLDTPS SRRGNFEALI REVRWELALR GRSDIKIMVS GGLDENTVKK LREAGAEAFG VGTSISSAKP FDFAMDIVEV NGKPETKRGK MSGRKNVLRC TSCHRIEVVP ANVQEKTCIC GGSMQNLLVK YLSHGKRTSE YPRPKEIRSR SMKELEYFKD IS //