ID S5LX89_9MOLU Unreviewed; 347 AA.
AC S5LX89;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN Name=pncB {ECO:0000313|EMBL:AGR42429.1};
GN ORFNames=SDIMI_v3c07250 {ECO:0000313|EMBL:AGR42429.1};
OS Spiroplasma diminutum CUAS-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276221 {ECO:0000313|EMBL:AGR42429.1, ECO:0000313|Proteomes:UP000014983};
RN [1] {ECO:0000313|EMBL:AGR42429.1, ECO:0000313|Proteomes:UP000014983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CUAS-1 {ECO:0000313|EMBL:AGR42429.1};
RX PubMed=23873917; DOI=10.1093/gbe/evt108;
RA Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT "Comparison of metabolic capacities and inference of gene content evolution
RT in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL Genome Biol. Evol. 5:1512-1523(2013).
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; CP005076; AGR42429.1; -; Genomic_DNA.
DR RefSeq; WP_020836660.1; NC_021833.1.
DR AlphaFoldDB; S5LX89; -.
DR STRING; 1276221.SDIMI_v3c07250; -.
DR KEGG; sdi:SDIMI_v3c07250; -.
DR PATRIC; fig|1276221.3.peg.727; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_043773_1_0_14; -.
DR InParanoid; S5LX89; -.
DR OrthoDB; 9770610at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000014983; Chromosome.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR PANTHER; PTHR43202:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43202; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE; 1.
DR Pfam; PF02749; QRPTase_N; 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:AGR42429.1};
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:UP000014983};
KW Transferase {ECO:0000313|EMBL:AGR42429.1}.
FT DOMAIN 42..110
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
SQ SEQUENCE 347 AA; 39350 MW; EDF08C923F6C7774 CRC64;
MKNKFNIDLK IFENYYSADY FKKTREILNK FKPNQLVTMQ WFQRKENTVI CGIEVIKEIL
RLSEVKDLNV EAVEEGEVVN SLEPVLKITG KYNNFAHFEG LFDGILSRAS TIATNAKKII
NVANGKMVLN MNDRMDYYTN QQIDGYASSI GGITNLVTEA SFEFLESQPN LNGTMPHALI
ASFDGDLLKA TEAYKEVFPN NNLVVLVDYN NDCINDSLRV CNNFRNEVYA VRLDTSPSLV
DKSLQNLNEK DNELHGVNPT LVKLLREKLD ENGHKNVKII VSSGFDENKI KYFEDLNTPV
DIYGVGEAIT KNKIAFTGDI VLIDGKKQSK FGRENVLSNK IKSIKYN
//
