ID Q8ZTS7_PYRAE Unreviewed; 515 AA.
AC Q8ZTS7;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=nicotinate-nucleotide diphosphorylase (carboxylating) {ECO:0000256|ARBA:ARBA00011944};
DE EC=2.4.2.19 {ECO:0000256|ARBA:ARBA00011944};
GN OrderedLocusNames=PAE3114 {ECO:0000313|EMBL:AAL64682.1};
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306 {ECO:0000313|EMBL:AAL64682.1, ECO:0000313|Proteomes:UP000002439};
RN [1] {ECO:0000313|EMBL:AAL64682.1, ECO:0000313|Proteomes:UP000002439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC IM2 {ECO:0000313|Proteomes:UP000002439};
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004893}.
CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008331}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family.
CC {ECO:0000256|ARBA:ARBA00009400}.
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DR EMBL; AE009441; AAL64682.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZTS7; -.
DR STRING; 178306.PAE3114; -.
DR EnsemblBacteria; AAL64682; AAL64682; PAE3114.
DR KEGG; pai:PAE3114; -.
DR PATRIC; fig|178306.9.peg.2341; -.
DR eggNOG; arCOG00254; Archaea.
DR eggNOG; arCOG01482; Archaea.
DR HOGENOM; CLU_531718_0_0_2; -.
DR InParanoid; Q8ZTS7; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central.
DR CDD; cd01572; QPRTase; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.1170.20; Quinolinate phosphoribosyl transferase, N-terminal domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR002811; Asp_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; PF01958; Asp_DH_C; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR Pfam; PF01729; QRPTase_C; 1.
DR Pfam; PF02749; QRPTase_N; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000002439};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..104
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 106..273
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
FT DOMAIN 285..373
FT /note="Aspartate/homoserine dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03447"
FT DOMAIN 417..492
FT /note="Aspartate dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01958"
SQ SEQUENCE 515 AA; 56491 MW; 77F8136F9F39D6F7 CRC64;
MIEARLFAFE LLDELRKDLP FIDWASAALP GKTIEACVVA KAEGVAAGVD EAAEFLKLLG
FQITLRLPEG AEIKPGVKIL CFRGEASEAL KVERVLLNLL MHASGIATYT RKLVAKAKSA
NPRVIVAATR KTLPFLRYIE KKAVWIGGGD PHRFSLSDST LFKDNHRKFI PLEHMASSKR
PFVHKAEVEV NTAEDAVRAA EMGFDIIMLD NMTPEEVERA AKLLAERGLR GRVILEASGN
ITEDNIHLYA PYVDVISVGR LTHSAPALDM SLEVYDDKVK VGLIGYGRLG KALVELVRDD
RDLEFVAVYD TDKEKCIEAE KSRGIRCVST IDELIALSEV IVEAASAQAV LEYGCKILEA
GRHLIVASVG ALSKLPKCGR GYVFAISGAA GGVDIVASTR GAVKHVVHKA AFRVAESGEA
EELYWKYPQS LNLSMTYKLA GAERVEVELR GDAPEDRIIH EVEIVHKWGR VYIKAENYAK
GTTSYSAALS LYNTLRNVAK FLRGSRIIIG TFAVL
//
