ID B5ICN9_ACIB4 Unreviewed; 391 AA.
AC B5ICN9;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN OrderedLocusNames=Aboo_1313 {ECO:0000313|EMBL:ADD09121.1};
OS Aciduliprofundum boonei (strain DSM 19572 / T469).
OC Archaea; Candidatus Thermoplasmatota; DHVE2 group; Aciduliprofundum.
OX NCBI_TaxID=439481 {ECO:0000313|EMBL:ADD09121.1, ECO:0000313|Proteomes:UP000001400};
RN [1] {ECO:0000313|Proteomes:UP000001400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19572 / T469 {ECO:0000313|Proteomes:UP000001400};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.;
RT "Complete sequence of Aciduliprofundum boonei T469.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001941; ADD09121.1; -; Genomic_DNA.
DR RefSeq; WP_008083841.1; NC_013926.1.
DR AlphaFoldDB; B5ICN9; -.
DR STRING; 439481.Aboo_1313; -.
DR GeneID; 8828275; -.
DR KEGG; abi:Aboo_1313; -.
DR eggNOG; arCOG01481; Archaea.
DR HOGENOM; CLU_043773_0_0_2; -.
DR OrthoDB; 371831at2157; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000001400; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000001400};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADD09121.1}.
FT DOMAIN 118..305
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
SQ SEQUENCE 391 AA; 43742 MW; 7C1E308CE37E9907 CRC64;
MKFHMANEDD IRNGRTTDVY FVRTKEILER NKIKKKVYAE FTVANPPYDW VVFAGLDEVI
ELLKGKNVNL YALPEGTIFP RRDENGIPIP VMAIEGDYKE FAVYETPMLG FICQASGIAT
KAARIKQAAG DYVVLSFGVR RMHPAIAPLI DRASYIGGCD GVSSIIGAEH IGKKPSGTMP
HALILTLGEE EAWKKFDEFV EEGVPRIALI DTFGDEKFES IKAAQILKDL VAVRLDTPSS
RRGNFEDIIR EVRWELDIRG YKDVGIFVSG GLDEDSVRRL RNAGATGFGV GTSLSNAKTI
DYAMDIVEIE GKPMAKKGKF SGAKKVYRCK NCGRFFVSYK EHMDTCPVCG GKLENMLKPY
LIDGEPVGEY PSVDDIRNYV LWQLKEFYGE E
//