ID M3J6D7_CANMX Unreviewed; 419 AA.
AC M3J6D7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU003838};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU003838};
GN ORFNames=G210_2000 {ECO:0000313|EMBL:EMG47593.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG47593.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG47593.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide
CC from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of
CC ATP. {ECO:0000256|RuleBase:RU003838}.
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 ECO:0000256|RuleBase:RU003838};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU003838}.
CC -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC cycle. Phosphorylation strongly increases the affinity for substrates
CC and increases the rate of nicotinate D-ribonucleotide production.
CC Dephosphorylation regenerates the low-affinity form of the enzyme,
CC leading to product release. {ECO:0000256|RuleBase:RU003838}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU003838}.
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:EMG47593.1}.
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DR EMBL; AOGT01001479; EMG47593.1; -; Genomic_DNA.
DR AlphaFoldDB; M3J6D7; -.
DR STRING; 1245528.M3J6D7; -.
DR eggNOG; KOG2511; Eukaryota.
DR HOGENOM; CLU_030991_0_0_1; -.
DR OMA; IEHCLEY; -.
DR OrthoDB; 1333333at2759; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01401; PncB_like; 1.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR HAMAP; MF_00570; NAPRTase; 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 NCBIfam; TIGR01514; NAPRTase; 1.
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 Glycosyltransferase {ECO:0000313|EMBL:EMG47593.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU003838};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU003838};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW Transferase {ECO:0000313|EMBL:EMG47593.1}.
FT DOMAIN 11..132
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 164..402
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
SQ SEQUENCE 419 AA; 48083 MW; 63003857E78300FC CRC64;
MTDDQVIKSL LDTDLYKLFM HAAVNKQFPD IQVKYRYTNR TPQLKLNHEA VIWLKNQIAL
LGNLRFATEE IAYLKKVLPQ LPEEYITYLA DFKLDPSSQI KYLGEDHEFE LEIEGKWNDT
ILYEIPILAL VSEAYFKFVD TDWNYDGQYE LAQGKARQLI EHGCNFSEFG TRRRRSFETQ
EIVIKAIKDV QRETNSKLVA GTSNVYFAMK YDLAPIGTVA HEWYMGIASI TQDYKHANKL
AMDYWIDTFG AKYAGLALTD TFGTDNYLSM FVPPYVNTYS GVRQDSGDPE LYAEKIAKHY
ESLGISENTK IICFSDSLNV EKCLKYKQKS DSLGLISTFG IGTFFTNDFK KISTGEKSQP
LNIVIKIKEA NGQPSIKISD NIGKNMGDET TVQRVKEELG YTERTWGEGD ETHRWTKDP
//
