ID NMNA3_HUMAN Reviewed; 252 AA. AC Q96T66; B3KVR6; D3DNF2; D3DNF3; Q8N4G1; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 169. DE RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 {ECO:0000305}; DE Short=NMN/NaMN adenylyltransferase 3; DE AltName: Full=Nicotinamide-nucleotide adenylyltransferase 3; DE Short=NMN adenylyltransferase 3; DE AltName: Full=Nicotinate-nucleotide adenylyltransferase 3; DE Short=NaMN adenylyltransferase 3; DE EC=2.7.7.18 {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; DE AltName: Full=Pyridine nucleotide adenylyltransferase 3; DE Short=PNAT-3; DE EC=2.7.7.1 {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; GN Name=NMNAT3 {ECO:0000312|HGNC:HGNC:20989}; ORFNames=FKSG76; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Wang Y.-G., Gong L.; RT "Identification of FKSG76, a novel gene encoding a NMN RT adenylyltransferase."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain cortex; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Colon, and Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16118205; DOI=10.1074/jbc.m508660200; RA Berger F., Lau C., Dahlmann M., Ziegler M.; RT "Subcellular compartmentation and differential catalytic properties of the RT three human nicotinamide mononucleotide adenylyltransferase isoforms."; RL J. Biol. Chem. 280:36334-36341(2005). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, RP ACTIVITY REGULATION, AND COFACTOR. RX PubMed=17402747; DOI=10.1021/bi6023379; RA Sorci L., Cimadamore F., Scotti S., Petrelli R., Cappellacci L., RA Franchetti P., Orsomando G., Magni G.; RT "Initial-rate kinetics of human NMN-adenylyltransferases: substrate and RT metal ion specificity, inhibition by products and multisubstrate analogues, RT and isozyme contributions to NAD+ biosynthesis."; RL Biochemistry 46:4912-4922(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NMN; NAD AND ATP RP ANALOG, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY. RX PubMed=12574164; DOI=10.1074/jbc.m300073200; RA Zhang X., Kurnasov O.V., Karthikeyan S., Grishin N.V., Osterman A.L., RA Zhang H.; RT "Structural characterization of a human cytosolic NMN/NaMN RT adenylyltransferase and implication in human NAD biosynthesis."; RL J. Biol. Chem. 278:13503-13511(2003). CC -!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide CC mononucleotide (NMN) and ATP. Can also use the deamidated form; CC nicotinic acid mononucleotide (NaMN) as substrate with the same CC efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can CC also use GTP and ITP as nucleotide donors. Also catalyzes the reverse CC reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the CC pyrophosphorolytic activity, can use NAD(+), NADH, NaAD, nicotinic acid CC adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide CC (NGD) as substrates. Fails to cleave phosphorylated dinucleotides CC NADP(+), NADPH and NaADP(+). Protects against axonal degeneration CC following injury. {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate CC + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1; CC Evidence={ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21361; CC Evidence={ECO:0000305|PubMed:16118205, ECO:0000305|PubMed:17402747}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21362; CC Evidence={ECO:0000305|PubMed:16118205, ECO:0000305|PubMed:17402747}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) CC + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502, CC ChEBI:CHEBI:58437; EC=2.7.7.18; CC Evidence={ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22861; CC Evidence={ECO:0000305|PubMed:16118205, ECO:0000305|PubMed:17402747}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22862; CC Evidence={ECO:0000305|PubMed:16118205, ECO:0000305|PubMed:17402747}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:17402747}; CC Note=Divalent metal cations. Mg(2+) confers the highest activity. CC {ECO:0000269|PubMed:17402747}; CC -!- ACTIVITY REGULATION: Activity is strongly inhibited by galotannin. CC Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')- CC tetraphosphate (Nap4AD). {ECO:0000269|PubMed:17402747}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=209 uM for NMN {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=130 uM for NAD(+) {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=29 uM for ATP {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=390 uM for PPi {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=276 uM for GTP {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=350 uM for ITP {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=111 uM for NaMN {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=130 uM for NMNH {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=2.01 uM for triazofurin monophosphate CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; CC Vmax=3.6 umol/min/mg enzyme for NAD synthesis CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; CC Vmax=12.8 umol/min/mg enzyme for pyrophosphorolytic NAD(+) cleavage CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; CC Vmax=2.9 umol/min/mg enzyme for pyrophosphorolytic NADH cleavage CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC nicotinamide D-ribonucleotide: step 1/1. {ECO:0000305|PubMed:16118205, CC ECO:0000305|PubMed:17402747}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) CC from nicotinate D-ribonucleotide: step 1/1. CC {ECO:0000305|PubMed:16118205, ECO:0000305|PubMed:17402747}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12574164}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12574164, CC ECO:0000269|PubMed:16118205}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96T66-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96T66-2; Sequence=VSP_010267; CC Name=3; CC IsoId=Q96T66-3; Sequence=VSP_043203; CC -!- TISSUE SPECIFICITY: Expressed in lung and spleen with lower levels in CC placenta and kidney. {ECO:0000269|PubMed:12574164, CC ECO:0000269|PubMed:16118205}. CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family. CC {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; AF345564; AAK52726.1; -; mRNA. DR EMBL; AK123208; BAG53878.1; -; mRNA. DR EMBL; AC046134; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC110716; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW79023.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79024.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79025.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79030.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79031.1; -; Genomic_DNA. DR EMBL; BC034374; AAH34374.1; -; mRNA. DR CCDS; CCDS3111.1; -. [Q96T66-2] DR CCDS; CCDS56282.1; -. [Q96T66-3] DR CCDS; CCDS82846.1; -. [Q96T66-1] DR RefSeq; NP_001186976.1; NM_001200047.2. [Q96T66-3] DR RefSeq; NP_001307440.1; NM_001320511.1. [Q96T66-1] DR RefSeq; NP_001307441.1; NM_001320512.1. [Q96T66-1] DR RefSeq; NP_835471.1; NM_178177.4. [Q96T66-2] DR RefSeq; XP_011511092.1; XM_011512790.1. DR RefSeq; XP_011511093.1; XM_011512791.2. DR RefSeq; XP_016861824.1; XM_017006335.1. DR RefSeq; XP_016861825.1; XM_017006336.1. DR RefSeq; XP_016861826.1; XM_017006337.1. DR RefSeq; XP_016861827.1; XM_017006338.1. DR PDB; 1NUP; X-ray; 1.90 A; A/B=1-252. DR PDB; 1NUQ; X-ray; 1.90 A; A/B=1-252. DR PDB; 1NUR; X-ray; 2.15 A; A/B=1-252. DR PDB; 1NUS; X-ray; 2.20 A; A/B=1-252. DR PDB; 1NUT; X-ray; 1.90 A; A/B=1-252. DR PDB; 1NUU; X-ray; 1.90 A; A/B=1-252. DR PDBsum; 1NUP; -. DR PDBsum; 1NUQ; -. DR PDBsum; 1NUR; -. DR PDBsum; 1NUS; -. DR PDBsum; 1NUT; -. DR PDBsum; 1NUU; -. DR AlphaFoldDB; Q96T66; -. DR SMR; Q96T66; -. DR BioGRID; 131564; 9. DR IntAct; Q96T66; 4. DR DrugBank; DB02596; alpha,beta-Methyleneadenosine 5'-triphosphate. DR DrugBank; DB04099; Deamido-Nad. DR DrugBank; DB03227; Nicotinamide Mononucleotide. DR iPTMnet; Q96T66; -. DR PhosphoSitePlus; Q96T66; -. DR BioMuta; NMNAT3; -. DR DMDM; 116242680; -. DR EPD; Q96T66; -. DR jPOST; Q96T66; -. DR MassIVE; Q96T66; -. DR MaxQB; Q96T66; -. DR PaxDb; 9606-ENSP00000340523; -. DR PeptideAtlas; Q96T66; -. DR ProteomicsDB; 78200; -. [Q96T66-1] DR ProteomicsDB; 78201; -. [Q96T66-2] DR ProteomicsDB; 78202; -. [Q96T66-3] DR Pumba; Q96T66; -. DR Antibodypedia; 33465; 211 antibodies from 28 providers. DR DNASU; 349565; -. DR Ensembl; ENST00000296202.12; ENSP00000296202.6; ENSG00000163864.18. [Q96T66-1] DR Ensembl; ENST00000339837.9; ENSP00000340523.5; ENSG00000163864.18. [Q96T66-2] DR Ensembl; ENST00000413939.6; ENSP00000412953.2; ENSG00000163864.18. [Q96T66-3] DR Ensembl; ENST00000704800.1; ENSP00000516041.1; ENSG00000163864.18. [Q96T66-1] DR GeneID; 349565; -. DR KEGG; hsa:349565; -. DR MANE-Select; ENST00000704800.1; ENSP00000516041.1; NM_001401600.1; NP_001388529.1. DR UCSC; uc003etj.4; human. [Q96T66-1] DR AGR; HGNC:20989; -. DR CTD; 349565; -. DR DisGeNET; 349565; -. DR GeneCards; NMNAT3; -. DR HGNC; HGNC:20989; NMNAT3. DR HPA; ENSG00000163864; Low tissue specificity. DR MIM; 608702; gene. DR neXtProt; NX_Q96T66; -. DR OpenTargets; ENSG00000163864; -. DR PharmGKB; PA134952303; -. DR VEuPathDB; HostDB:ENSG00000163864; -. DR eggNOG; KOG3199; Eukaryota. DR GeneTree; ENSGT00950000183179; -. DR HOGENOM; CLU_033366_3_1_1; -. DR InParanoid; Q96T66; -. DR OrthoDB; 5488885at2759; -. DR PhylomeDB; Q96T66; -. DR TreeFam; TF315035; -. DR BioCyc; MetaCyc:HS08953-MONOMER; -. DR BRENDA; 2.7.7.1; 2681. DR BRENDA; 2.7.7.18; 2681. DR PathwayCommons; Q96T66; -. DR Reactome; R-HSA-196807; Nicotinate metabolism. DR SABIO-RK; Q96T66; -. DR SignaLink; Q96T66; -. DR UniPathway; UPA00253; UER00332. DR UniPathway; UPA00253; UER00600. DR BioGRID-ORCS; 349565; 10 hits in 1157 CRISPR screens. DR ChiTaRS; NMNAT3; human. DR EvolutionaryTrace; Q96T66; -. DR GenomeRNAi; 349565; -. DR Pharos; Q96T66; Tbio. DR PRO; PR:Q96T66; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q96T66; Protein. DR Bgee; ENSG00000163864; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 162 other cell types or tissues. DR ExpressionAtlas; Q96T66; baseline and differential. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IBA:GO_Central. DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:UniProtKB. DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central. DR GO; GO:0009165; P:nucleotide biosynthetic process; IC:UniProtKB. DR GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0009611; P:response to wounding; IEA:Ensembl. DR CDD; cd09286; NMNAT_Eukarya; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR005248; NadD/NMNAT. DR InterPro; IPR045094; NMNAT_euk. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR NCBIfam; TIGR00482; nicotinate (nicotinamide) nucleotide adenylyltransferase; 1. DR PANTHER; PTHR12039; NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE; 1. DR PANTHER; PTHR12039:SF7; NICOTINAMIDE_NICOTINIC ACID MONONUCLEOTIDE ADENYLYLTRANSFERASE 3; 1. DR Pfam; PF01467; CTP_transf_like; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR Genevisible; Q96T66; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Magnesium; Mitochondrion; KW NAD; Nucleotide-binding; Nucleotidyltransferase; KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase. FT CHAIN 1..252 FT /note="Nicotinamide/nicotinic acid mononucleotide FT adenylyltransferase 3" FT /id="PRO_0000135016" FT BINDING 14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12574164, FT ECO:0007744|PDB:1NUU" FT BINDING 15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12574164, FT ECO:0007744|PDB:1NUU" FT BINDING 22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:12574164" FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:12574164" FT BINDING 90 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12574164, FT ECO:0007744|PDB:1NUU" FT BINDING 93 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12574164, FT ECO:0007744|PDB:1NUU" FT BINDING 135 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12574164, FT ECO:0007744|PDB:1NUU" FT BINDING 137 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12574164, FT ECO:0007744|PDB:1NUU" FT BINDING 140 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000269|PubMed:12574164" FT BINDING 147 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12574164, FT ECO:0007744|PDB:1NUU" FT BINDING 148 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12574164, FT ECO:0007744|PDB:1NUU" FT BINDING 167 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12574164, FT ECO:0007744|PDB:1NUU" FT BINDING 198 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:12574164, FT ECO:0007744|PDB:1NUU" FT BINDING 203..206 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:12574164" FT VAR_SEQ 1..37 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010267" FT VAR_SEQ 37..125 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043203" FT CONFLICT 169 FT /note="G -> S (in Ref. 1; AAK52726)" FT /evidence="ECO:0000305" FT STRAND 5..13 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 20..35 FT /evidence="ECO:0007829|PDB:1NUP" FT STRAND 37..48 FT /evidence="ECO:0007829|PDB:1NUP" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 61..71 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:1NUP" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 83..86 FT /evidence="ECO:0007829|PDB:1NUP" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 93..104 FT /evidence="ECO:0007829|PDB:1NUP" FT STRAND 129..135 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 136..141 FT /evidence="ECO:0007829|PDB:1NUP" FT TURN 145..147 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 150..159 FT /evidence="ECO:0007829|PDB:1NUP" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 172..178 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 180..184 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:1NUP" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 202..210 FT /evidence="ECO:0007829|PDB:1NUP" FT HELIX 221..229 FT /evidence="ECO:0007829|PDB:1NUP" FT TURN 230..233 FT /evidence="ECO:0007829|PDB:1NUQ" SQ SEQUENCE 252 AA; 28322 MW; 6402CFB2FE789CF4 CRC64; MKSRIPVVLL ACGSFNPITN MHLRMFEVAR DHLHQTGMYQ VIQGIISPVN DTYGKKDLAA SHHRVAMARL ALQTSDWIRV DPWESEQAQW METVKVLRHH HSKLLRSPPQ MEGPDHGKAL FSTPAAVPEL KLLCGADVLK TFQTPNLWKD AHIQEIVEKF GLVCVGRVGH DPKGYIAESP ILRMHQHNIH LAKEPVQNEI SATYIRRALG QGQSVKYLIP DAVITYIKDH GLYTKGSTWK GKSTQSTEGK TS //