NADC_MYCTU
ID NADC_MYCTU Reviewed; 285 AA.
AC P9WJJ7; L0T8R5; O06594;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE EC=2.4.2.19 {ECO:0000305|PubMed:9862811};
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE Short=QAPRTase;
GN Name=nadC; OrderedLocusNames=Rv1596; ORFNames=MTCY336.08c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3] {ECO:0007744|PDB:1QPN, ECO:0007744|PDB:1QPO, ECO:0007744|PDB:1QPQ, ECO:0007744|PDB:1QPR}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9862811; DOI=10.1016/s0969-2126(98)00156-7;
RA Sharma V., Grubmeyer C., Sacchettini J.C.;
RT "Crystal structure of quinolinic acid phosphoribosyltransferase from
RT Mycobacterium tuberculosis: a potential tb drug target.";
RL Structure 6:1587-1599(1998).
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {ECO:0000250}.
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:0000305|PubMed:9862811};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC -!- SUBUNIT: Homodimer. Hexamer formed by 3 homodimers.
CC {ECO:0000269|PubMed:9862811}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44360.1; -; Genomic_DNA.
DR PIR; F70543; F70543.
DR RefSeq; NP_216112.1; NC_000962.3.
DR RefSeq; WP_003898939.1; NZ_NVQJ01000016.1.
DR PDB; 1QPN; X-ray; 2.60 A; A/B/C/D/E/F=2-285.
DR PDB; 1QPO; X-ray; 2.40 A; A/B/C/D/E/F=2-285.
DR PDB; 1QPQ; X-ray; 2.45 A; A/B/C/D/E/F=2-285.
DR PDB; 1QPR; X-ray; 2.45 A; A/B/C/D/E/F=2-285.
DR PDBsum; 1QPN; -.
DR PDBsum; 1QPO; -.
DR PDBsum; 1QPQ; -.
DR PDBsum; 1QPR; -.
DR AlphaFoldDB; P9WJJ7; -.
DR SMR; P9WJJ7; -.
DR STRING; 83332.Rv1596; -.
DR DrugBank; DB04294; 5-Phosphoribosyl-1-(Beta-Methylene) Pyrophosphate.
DR DrugBank; DB02382; Namn.
DR DrugBank; DB02746; Phthalic Acid.
DR DrugBank; DB01796; Quinolinic Acid.
DR PaxDb; P9WJJ7; -.
DR DNASU; 886281; -.
DR GeneID; 886281; -.
DR KEGG; mtu:Rv1596; -.
DR TubercuList; Rv1596; -.
DR eggNOG; COG0157; Bacteria.
DR OMA; DMIMLKD; -.
DR PhylomeDB; P9WJJ7; -.
DR BRENDA; 2.4.2.19; 3445.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IDA:MTBBASE.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:MTBBASE.
DR GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central.
DR CDD; cd01572; QPRTase; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.90.1170.20; -; 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 PANTHER; PTHR32179; PTHR32179; 1.
DR Pfam; PF01729; QRPTase_C; 1.
DR Pfam; PF02749; QRPTase_N; 1.
DR PIRSF; PIRSF006250; NadC_ModD; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR00078; nadC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..285
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000155946"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9862811"
FT BINDING 138..140
FT /ligand="substrate"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9862811"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9862811"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9862811"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9862811"
FT BINDING 248..250
FT /ligand="substrate"
FT BINDING 269..271
FT /ligand="substrate"
FT HELIX 5..23
FT /evidence="ECO:0007829|PDB:1QPO"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:1QPO"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1QPO"
FT HELIX 97..127
FT /evidence="ECO:0007829|PDB:1QPO"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1QPO"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1QPQ"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:1QPO"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:1QPO"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1QPO"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:1QPO"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:1QPO"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:1QPO"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1QPO"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1QPO"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1QPO"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:1QPO"
SQ SEQUENCE 285 AA; 29951 MW; 45DE3335EC1C522F CRC64;
MGLSDWELAA ARAAIARGLD EDLRYGPDVT TLATVPASAT TTASLVTREA GVVAGLDVAL
LTLNEVLGTN GYRVLDRVED GARVPPGEAL MTLEAQTRGL LTAERTMLNL VGHLSGIATA
TAAWVDAVRG TKAKIRDTRK TLPGLRALQK YAVRTGGGVN HRLGLGDAAL IKDNHVAAAG
SVVDALRAVR NAAPDLPCEV EVDSLEQLDA VLPEKPELIL LDNFAVWQTQ TAVQRRDSRA
PTVMLESSGG LSLQTAATYA ETGVDYLAVG ALTHSVRVLD IGLDM
