ID G1UA11_CANAX Unreviewed; 421 AA.
AC G1UA11;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 Name=CaJ7.0462 {ECO:0000313|EMBL:BAE44905.1};
GN ORFNames=CaO19.7176 {ECO:0000313|EMBL:BAE44905.1}, FOB64_006590
GN {ECO:0000313|EMBL:KAF6061153.1};
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476 {ECO:0000313|EMBL:BAE44905.1};
RN [1] {ECO:0000313|EMBL:BAE44905.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15937140; DOI=10.1534/genetics.104.034652;
RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA Mikami Y.;
RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT syntenic analysis against the Saccharomyces cerevisiae genome.";
RL Genetics 170:1525-1537(2005).
RN [2] {ECO:0000313|EMBL:KAF6061153.1, ECO:0000313|Proteomes:UP000536275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_656 {ECO:0000313|EMBL:KAF6061153.1,
RC ECO:0000313|Proteomes:UP000536275};
RA Campos J., Goldberg B., Tallon L., Sadzewicz L., Vavikolanu K., Mehta A.,
RA Aluvathingal J., Nadendla S., Nandy P., Geyer C., Yan Y., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-2020) 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}.
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DR EMBL; AP006852; BAE44905.1; -; Genomic_DNA.
DR EMBL; JABWAD010000066; KAF6061153.1; -; Genomic_DNA.
DR AlphaFoldDB; G1UA11; -.
DR SMR; G1UA11; -.
DR EnsemblFungi; C7_04040C_A-T; C7_04040C_A-T-p1; C7_04040C_A.
DR VEuPathDB; FungiDB:C7_04040C_A; -.
DR VEuPathDB; FungiDB:CAWG_05733; -.
DR OMA; IEHCLEY; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000536275; Unassembled WGS sequence.
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-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
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 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:KAF6061153.1};
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:UP000536275};
KW Transferase {ECO:0000313|EMBL:KAF6061153.1}.
FT DOMAIN 14..136
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 168..406
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
SQ SEQUENCE 421 AA; 48340 MW; AF8857BD0BDC7589 CRC64;
MNGTEDKPVI KSFLDTDLYK LFMHAAVNKQ FPDVPVKYRY TNRTPQLKLN SQAISWLKKQ
IEYLGDLRFS AEEILYLHRV LPQLPSDYLE YLADFKLVPS SQIKYLDNDE GDFELEIVGK
WNDTILYEIP LLALVSEAYF KFVDTDWNYE GQYALAQKKA KQLISNECNF SEFGTRRRRS
YESQEIVIKA IKDVQIDTQS KYIAGTSNVY FAMKYDLPPI GTVAHEWYMG IASITQDYVH
ANKLAMDYWI DTFGAKYAGL ALTDTFGTDN YLTMFVAPYV NEYSGVRQDS GDPELYAEKI
ARHYEKMGIA KNTKIICFSD SLNVEKCLKY KNTADKLGLI STFGIGTFFT NDFNKLSNGE
KSQPMNIVIK IKEANGKPAI KISDNIGKNM GDQATVDRVK QELGYTERTW SEGDETHRWS
K
//
