ID   NAMPT_MYCGE             Reviewed;         450 AA.
AC   P47283; Q49463;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 116.
DE   RecName: Full=Nicotinamide phosphoribosyltransferase {ECO:0000250|UniProtKB:Q6FDK2};
DE            Short=NAmPRTase {ECO:0000250|UniProtKB:Q6FDK2};
DE            Short=NMPRT {ECO:0000250|UniProtKB:Q6FDK2};
DE            Short=Nampt {ECO:0000250|UniProtKB:Q6FDK2};
DE            EC=2.4.2.12 {ECO:0000250|UniProtKB:Q6FDK2};
GN   OrderedLocusNames=MG037;
OS   Mycoplasmoides genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 /
OS   G37) (Mycoplasma genitalium).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-166.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(1993).
CC   -!- FUNCTION: Catalyzes the condensation of nicotinamide with 5-
CC       phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an
CC       intermediate in the biosynthesis of NAD.
CC       {ECO:0000250|UniProtKB:Q6FDK2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-nicotinamide D-ribonucleotide + diphosphate = 5-phospho-
CC         alpha-D-ribose 1-diphosphate + nicotinamide + H(+);
CC         Xref=Rhea:RHEA:16149, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.12;
CC         Evidence={ECO:0000250|UniProtKB:Q6FDK2};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide D-
CC       ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and
CC       nicotinamide: step 1/1. {ECO:0000250|UniProtKB:Q6FDK2}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L43967; AAC71253.1; -; Genomic_DNA.
DR   EMBL; U01814; AAD12352.1; -; Genomic_DNA.
DR   PIR; A64204; A64204.
DR   AlphaFoldDB; P47283; -.
DR   SMR; P47283; -.
DR   STRING; 243273.MG_037; -.
DR   KEGG; mge:MG_037; -.
DR   eggNOG; COG1488; Bacteria.
DR   HOGENOM; CLU_012550_2_0_14; -.
DR   InParanoid; P47283; -.
DR   OrthoDB; 394882at2; -.
DR   UniPathway; UPA00253; UER00890.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0047280; F:nicotinamide phosphoribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0009435; P:NAD+ biosynthetic process; IBA:GO_Central.
DR   CDD; cd01569; PBEF_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041525; N/Namide_PRibTrfase.
DR   InterPro; IPR016471; Nicotinamide_PRibTrfase.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   NCBIfam; NF006629; PRK09198.1; 1.
DR   PANTHER; PTHR43816; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43816:SF1; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   PIRSF; PIRSF005943; NMPRT; 1.
DR   SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Pyridine nucleotide biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..450
FT                   /note="Nicotinamide phosphoribosyltransferase"
FT                   /id="PRO_0000205859"
FT   BINDING         210
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000250|UniProtKB:P43490"
FT   BINDING         233
FT                   /ligand="beta-nicotinamide D-ribonucleotide"
FT                   /ligand_id="ChEBI:CHEBI:14649"
FT                   /evidence="ECO:0000250|UniProtKB:P43490"
FT   BINDING         249
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000250|UniProtKB:P43490"
FT   BINDING         310..312
FT                   /ligand="beta-nicotinamide D-ribonucleotide"
FT                   /ligand_id="ChEBI:CHEBI:14649"
FT                   /evidence="ECO:0000250|UniProtKB:P43490"
FT   BINDING         310
FT                   /ligand="diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:33019"
FT                   /evidence="ECO:0000250|UniProtKB:P43490"
FT   BINDING         364..365
FT                   /ligand="beta-nicotinamide D-ribonucleotide"
FT                   /ligand_id="ChEBI:CHEBI:14649"
FT                   /evidence="ECO:0000250|UniProtKB:P43490"
FT   BINDING         403
FT                   /ligand="beta-nicotinamide D-ribonucleotide"
FT                   /ligand_id="ChEBI:CHEBI:14649"
FT                   /evidence="ECO:0000250|UniProtKB:P43490"
FT   CONFLICT        52..55
FT                   /note="EFVW -> GVCL (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  51801 MW;  F33E45676CA16491 CRC64;
     MMDKRTSEIE FHLKNLLACD AYKLSHRLMY PQDTQNLYSM LTARGVYGDF KEFVWNHDFA
     KEILLNVFNG FVNSVIEVKK NKLLAAALTD KLVSVFNDHE LANEFTQHIC HLASFLEKNK
     KMPLVAKIHE SDQSLPFRTP LITIEGVENI PNNFVWLVNY FETVLLENIW LFQTASTVAK
     RIKSLLEKYA KETADETSFI NFQCHDFSMR GMSSLQSALY VARAHLQYFT GSDTILGGDN
     SRSILASEHS VMCADGSKHE LKTFQRLLEK FKDKKLSLVI DSYDMWNVLD NIIPRLKNLI
     LMRGATLYLR ADSGNYQTLI CNPNYKKQDK STWAMIDYLD HHFSSTINKK GYKVLNKKIG
     IIYGDGITYQ KIEWILNCLK NHGYCSSNII FGVGSSTYQN LNRDTLGFVY KLTAIKRNNR
     WIGVKKTPIT DLSKSSKGGR YKTKRLITVY
//