NMNA3_HUMAN
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 03-AUG-2022, entry version 160.
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}.
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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. [Q96T66-2]
DR RefSeq; XP_011511093.1; XM_011512791.2. [Q96T66-2]
DR RefSeq; XP_016861824.1; XM_017006335.1. [Q96T66-1]
DR RefSeq; XP_016861825.1; XM_017006336.1. [Q96T66-1]
DR RefSeq; XP_016861826.1; XM_017006337.1. [Q96T66-1]
DR RefSeq; XP_016861827.1; XM_017006338.1. [Q96T66-2]
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 STRING; 9606.ENSP00000340523; -.
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; Q96T66; -.
DR PeptideAtlas; Q96T66; -.
DR PRIDE; Q96T66; -.
DR ProteomicsDB; 78200; -. [Q96T66-1]
DR ProteomicsDB; 78201; -. [Q96T66-2]
DR ProteomicsDB; 78202; -. [Q96T66-3]
DR Antibodypedia; 33465; 191 antibodies from 28 providers.
DR DNASU; 349565; -.
DR Ensembl; ENST00000296202.11; ENSP00000296202.6; ENSG00000163864.17. [Q96T66-1]
DR Ensembl; ENST00000339837.9; ENSP00000340523.5; ENSG00000163864.17. [Q96T66-2]
DR Ensembl; ENST00000413939.6; ENSP00000412953.2; ENSG00000163864.17. [Q96T66-3]
DR GeneID; 349565; -.
DR KEGG; hsa:349565; -.
DR UCSC; uc003etj.4; human. [Q96T66-1]
DR CTD; 349565; -.
DR DisGeNET; 349565; -.
DR GeneCards; NMNAT3; -.
DR HGNC; HGNC:20989; NMNAT3.
DR HPA; ENSG00000163864; Tissue enhanced (brain).
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 PhylomeDB; Q96T66; -.
DR TreeFam; TF315035; -.
DR BioCyc; MetaCyc:HS08953-MON; -.
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 1078 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 left testis and 160 other tissues.
DR ExpressionAtlas; Q96T66; baseline and differential.
DR Genevisible; Q96T66; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 CDD; cd09286; NMNAT_Eukarya; 1.
DR Gene3D; 3.40.50.620; -; 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 Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00482; TIGR00482; 1.
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 13..15
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 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 53..55
FT /ligand="substrate"
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..93
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12574164"
FT BINDING 135..137
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 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..148
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12574164"
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
