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Database: UniProt
Entry: K2RQU6_MACPH
LinkDB: K2RQU6_MACPH
Original site: K2RQU6_MACPH 
ID   K2RQU6_MACPH            Unreviewed;       501 AA.
AC   K2RQU6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236};
DE            EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236};
GN   ORFNames=MPH_05768 {ECO:0000313|EMBL:EKG17078.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG17078.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG17078.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG17078.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKG17078.1}.
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DR   EMBL; AHHD01000257; EKG17078.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2RQU6; -.
DR   STRING; 1126212.K2RQU6; -.
DR   VEuPathDB; FungiDB:MPH_05768; -.
DR   eggNOG; KOG2511; Eukaryota.
DR   HOGENOM; CLU_030991_0_0_1; -.
DR   InParanoid; K2RQU6; -.
DR   OrthoDB; 1333333at2759; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000007129; 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   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   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:UP000007129}.
FT   DOMAIN          20..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          349..475
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   REGION          304..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  55462 MW;  0F8A3DDD4D4EF1B7 CRC64;
     MADVGNGGAA ALPEGVNSLL DTDLYKLTMQ CCVLKYFPTV DVTYSFTNRT PHMRFTRAAY
     RWLQSQIDKL GNLAFSQEEL DFLKKSCTYL NDQYLRYLRT FRLHPDKQIR LSFRADKDTG
     ADEDIGDLDL QTEGLWVETI LYEIPLLALI SEAYFKFCDT DWSHSGQLDK AYNKGLQLLE
     NGCIFSEFGS RRRRDYHTHD LVMQGLLRAA QDAEAKGWAG KLSGTSNVHF AMKYNVPPVG
     TVAHEWFMGV AAVTNNYEDA NEIALSYWVG TFGEGVLSIA LTDTFGTPNF LKAFKKPIPT
     YTTAEPGSAA TTASVSGSST LSETASLGTT EPPIHAPIHR RDGTYTDVPT FAQSFTGVRQ
     DSGDPRDFIK MMRKFYDEEA IQGKKVIVFS DSLNIELCLE YKKAAEAEGF QPTFGVGTFL
     TNDFVRESTG QKSVPLNIVI KIASAAGRAA VKISDNMGKN TGDKATVAEV KRRLGYVEKE
     WAGGDERTRW GTDSAAASKS S
//
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