ID U2RH08_9FUSO Unreviewed; 463 AA.
AC U2RH08;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
GN ORFNames=HMPREF1984_00897 {ECO:0000313|EMBL:ERK67864.1};
OS Leptotrichia sp. oral taxon 215 str. W9775.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1321779 {ECO:0000313|EMBL:ERK67864.1, ECO:0000313|Proteomes:UP000016640};
RN [1] {ECO:0000313|EMBL:ERK67864.1, ECO:0000313|Proteomes:UP000016640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9775 {ECO:0000313|EMBL:ERK67864.1,
RC ECO:0000313|Proteomes:UP000016640};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC {ECO:0000256|RuleBase:RU365100}.
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:RU365100};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU365100}.
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:RU365100}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU365100}.
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:ERK67864.1}.
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DR EMBL; AWVR01000029; ERK67864.1; -; Genomic_DNA.
DR AlphaFoldDB; U2RH08; -.
DR STRING; 1321779.HMPREF1984_00897; -.
DR PATRIC; fig|1321779.3.peg.865; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_025154_2_1_0; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000016640; 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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR NCBIfam; TIGR01513; NAPRTase_put; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000313|EMBL:ERK67864.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365100};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU365100};
KW Reference proteome {ECO:0000313|Proteomes:UP000016640};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:ERK67864.1}.
FT DOMAIN 12..136
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 160..362
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT COILED 436..463
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 463 AA; 53161 MW; 825FDBB3D56D5D2B CRC64;
MRLLMDRFFK FLNSDRYQYA ESEIYLKNNM HNQTAVFDVF LRTKNENDCA IVYGISDVLE
LIEILNETSY KDRKKYLSEL SDNEDFIEYM ANMKFTGSIR GVKEGEIIFS NEPILTITAP
LIQGKILETP ILNILNYQIL TATVTSKIVQ AAGGRDVLFF GTRRVPGFEA AMSMTKACYV
TGCISHSNIM GEYFYNLKST GTMTHGFIQS FGMDKDSEYR AFDQFIKTYS HKKYPLVMLV
DTYDTMKSGI TAAIRAFRDN GINDGYEGMY GIRIDSGNLE ELSKKCRKIL NENGFFKAKI
ILTGGLDEQR IKELIENGAE VDVFGVGDAI ALPEKEISTV YKMSKIDETD VMKISDEEQK
TSLPGSKELY RIYENNDFTD VIMLEKETPE GKNVKKLTVD YIKNGEKIEE NCRLLGLEEA
KKYYKDNLLY LQKIYSEKEK RNRVKLSENL KKLKEDLIKS KKS
//
