ID U7Q5H9_SPOS1 Unreviewed; 501 AA.
AC U7Q5H9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN ORFNames=HMPREF1624_00256 {ECO:0000313|EMBL:ERT01961.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT01961.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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; KI440842; ERT01961.1; -; Genomic_DNA.
DR AlphaFoldDB; U7Q5H9; -.
DR STRING; 1391915.U7Q5H9; -.
DR eggNOG; KOG2511; Eukaryota.
DR HOGENOM; CLU_030991_0_0_1; -.
DR OrthoDB; 1333333at2759; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000018087; Unassembled WGS sequence.
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 CDD; cd01401; PncB_like; 1.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 2.
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; 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:ERT01961.1};
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:UP000018087};
KW Transferase {ECO:0000313|EMBL:ERT01961.1}.
FT DOMAIN 17..151
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 185..296
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 341..473
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT REGION 476..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 55486 MW; F30254E633CAE857 CRC64;
MDFNSSSPYP EGVISFLDTD LYKLTMQCAV LKYYKDVPVT YSFTNRTPEK KLSRTAYQWL
SDQVRKLGNI SLSDEELAFL KLHCPYLTPA YLDFLKEFRL NPREEVTIAF VPVSPSSSGT
ESPDDLGDVD IAIRGAWVDT ILYEIPILAL TSEAYFKFMD TDWNYDGQQE LAFDKGMRLL
EAGCVLSEFG TRRRRDYHTQ ALVFRGLVQA SREAAERGLP GKLSGTSNVH LAMRFNIPPV
GTVAHEWFMG IAALSGEYRQ ATEEALCRWV GCFGDGVLGI ALTDTFGTPE FLREFGKPVR
RLEGDAQAPA AQTTTTARPV LVSAADSFTS AASDAPSQPA TGQQTNKTYA RIFTGVRQDS
GDPTAYVKLM REFYDAQGIT DKKVIVFSDS LNLERCLEYK KVSEAAGFQP TFGVGTYLTN
DFVNLTTGLK SVPLNIVIKL SSANGHPAVK ISDNAGKNTG DKATVDRVKR ELGYVEKDWE
GGDETRRWGQ EGDQPDQPIK A
//
