ID G7VFF6_9CREN Unreviewed; 386 AA.
AC G7VFF6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN ORFNames=P186_1543 {ECO:0000313|EMBL:AET32962.1};
OS Pyrobaculum ferrireducens.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET32962.1, ECO:0000313|Proteomes:UP000005867};
RN [1] {ECO:0000313|EMBL:AET32962.1, ECO:0000313|Proteomes:UP000005867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1860 {ECO:0000313|EMBL:AET32962.1,
RC ECO:0000313|Proteomes:UP000005867};
RX PubMed=22247528; DOI=10.1128/JB.06465-11;
RA Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT pyrobaculum able to grow with various electron acceptors.";
RL J. Bacteriol. 194:727-728(2012).
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:0000256|ARBA:ARBA00001240};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952}.
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DR EMBL; CP003098; AET32962.1; -; Genomic_DNA.
DR AlphaFoldDB; G7VFF6; -.
DR STRING; 1104324.P186_1543; -.
DR KEGG; pyr:P186_1543; -.
DR eggNOG; arCOG01481; Archaea.
DR HOGENOM; CLU_043773_0_0_2; -.
DR OrthoDB; 371831at2157; -.
DR BioCyc; PSP1104324:GJSN-1515-MONOMER; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000005867; Chromosome.
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: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; 2.
DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:AET32962.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AET32962.1}.
FT DOMAIN 114..306
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
SQ SEQUENCE 386 AA; 42605 MW; 089F7EED1A4C8623 CRC64;
MLHTASPSDI LSGRTTDIYF ARTVEVLKNA GFADVRVRAE FHVASLPRGF KWAVFTGLKE
VVEILRGRRI TLYALPEGTL FYENDPIMVI EGPYLEFAVL ETAILGVVRH YSSISTKAAR
VKKIAGEKTC LFFGARALHP AIQPMADRAA YIGGCDGVAT VMGAELLGIK PSGTMPHALM
IIFRAVAGDH TLAWVWFDKT VPSEVPRIVL ADTFLDEREE ALLAAKLLGE RLHGVRLDTP
GSRRGNIRRI VEEVRWALDL NGYRNVKIFV SGGLDEPQVE ALRDVVDGFG VGTSIAFPPS
VDVSMDIVEV EVGGRWIPIT KRGKLPGFKQ LYRCGIRHVA VPWGSPPPCG EPLLVKWIED
GRVVREIPGE AEIRKYVLEQ LSEVEL
//
