PNCB_THEAC
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 03-AUG-2022, entry version 114.
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}.
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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.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 OMA; EVRWTLD; -.
DR OrthoDB; 56885at2157; -.
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; -; 1.
DR Gene3D; 3.90.1170.20; -; 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 Pfam; PF01729; QRPTase_C; 1.
DR PIRSF; PIRSF000484; NAPRT; 1.
DR SUPFAM; SSF51690; SSF51690; 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
