ID E4ZSR8_LEPMJ Unreviewed; 494 AA.
AC E4ZSR8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN ORFNames=LEMA_P119970.1 {ECO:0000313|EMBL:CBX94506.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
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; FP929123; CBX94506.1; -; Genomic_DNA.
DR RefSeq; XP_003837950.1; XM_003837902.1.
DR AlphaFoldDB; E4ZSR8; -.
DR STRING; 985895.E4ZSR8; -.
DR EnsemblFungi; CBX94506; CBX94506; LEMA_P119970.1.
DR GeneID; 13291182; -.
DR eggNOG; KOG2511; Eukaryota.
DR HOGENOM; CLU_030991_0_0_1; -.
DR InParanoid; E4ZSR8; -.
DR OMA; IEHCLEY; -.
DR OrthoDB; 1333333at2759; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019358; P:nicotinate nucleotide salvage; IEA:EnsemblFungi.
DR GO; GO:0000183; P:rDNA heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:EnsemblFungi.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 2.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR040727; NAPRTase_N.
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; 2.
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 Glycosyltransferase {ECO:0000313|EMBL:CBX94506.1};
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:UP000002668};
KW Transferase {ECO:0000313|EMBL:CBX94506.1}.
FT DOMAIN 18..149
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 183..294
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 343..472
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT REGION 473..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 54646 MW; 8B7FBC8E36B271F6 CRC64;
MASHIDSTNL PEGVFSLLDT DLYKLTMQCC ILKFFPNVSV TYSFTNRTPD KKLSRAAFKW
LQIQVGKLEH ISVTDEEIGF LKTHCTYLND QYLQFLSTFR LKPSKQLRLS FQPVHDTGSD
DDRGEFHIHT EGLWLDTILY EIPLLALVSE AYFKFVETDW SHAGQVDKAY QKGRSLLEGG
CIFSEFGTRR RRDYHTQDLV LQGLRRAADE GAKAGWTGKL SGTSNVHFAM KHGLVPIGTV
AHEWFMGVAA ITNNYESANE IALEYWTATF GAGVLSIALT DTFGTPTFLK AFKKRIPAVT
TAIPGGGTTM ASASATTDID AVQSMASTNP PIEAPLNGKL ESQKTYAEVF TGVRQDSGDP
LEFVRMMREF YDQQGIKDKK TIVFSDSLNL ELCFKYKAAA EEAGFQPTFG VGTFLTNDFV
ETSSGKKSVP LNIVIKIASA SGRHAVKISD NIGKNTGDKA TVDEVKQRLG YTEKSWAGGD
EKTRWGSSEQ ATRG
//
