ID A0A1Y2VBG3_9PEZI Unreviewed; 466 AA.
AC A0A1Y2VBG3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN ORFNames=M434DRAFT_10993 {ECO:0000313|EMBL:OTA94088.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA94088.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA94088.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA94088.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897}.
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DR EMBL; KZ112461; OTA94088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VBG3; -.
DR STRING; 1001938.A0A1Y2VBG3; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000194361; Unassembled WGS sequence.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01401; PncB_like; 1.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR006406; Nic_PRibTrfase.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 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 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:UP000194361}.
FT DOMAIN 18..149
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 184..441
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
SQ SEQUENCE 466 AA; 52655 MW; 031D46594F791C9F CRC64;
MEHFDWSTPF PEGVISFLDT DLYKLTMQCA VFKYYPDVPV TYAFTNRTPE KKLSRKAFSW
LCEQISKLGN ISLSDDELRY LQTHCKYLSP QYLDFLKEFR LKPRDQLNPT FNPIGANTGA
EDELGDIHIE IKGKWVDTIL YEIPLLALTS EAYFKFMDTD WNYEGQEKKA YDKGMRLLEA
GCIVSEFGTR RRRDYHTQAL VFRGLVKSSK DAEKRGLPGK LSGTSNVHLA MRFNLPPVGT
VAHEWFMGIA AITDDYPNAT EEALRRWIGC FGEGVLGIAL TDTFGTPEFL KAFSKPIRYL
PDTPNIPPTN EGGRPRTYAE VYAGVRQDSG DPANFVKLMR EFYEKQGIKD KKTIVFSDSL
NIEKCIEYKR ISEEQGFQPT FGVGTYLTND FVQLTTGKKS VPLNIVIKLS SAAGNPAIKI
SDNIGKNTGD SEKVAQVKEL LGYVEKEWAG GDETSRWGKA DDVVQS
//
