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Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (NMN/NaMN adenylyltransferase 3) (Nicotinamide-nucleotide adenylyltransferase 3) (NMN adenylyltransferase 3) (Nicotinate-nucleotide adenylyltransferase 3) (NaMN adenylyltransferase 3) (EC 2.7.7.18) (Pyridine nucleotide adenylyltransferase 3) (PNAT-3) (EC 2.7.7.1)

 NMNA3_HUMAN             Reviewed;         252 AA.
Q96T66; B3KVR6; D3DNF2; D3DNF3; Q8N4G1;
10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
27-SEP-2017, entry version 132.
RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 {ECO:0000305};
Short=NMN/NaMN adenylyltransferase 3;
AltName: Full=Nicotinamide-nucleotide adenylyltransferase 3;
Short=NMN adenylyltransferase 3;
AltName: Full=Nicotinate-nucleotide adenylyltransferase 3;
Short=NaMN adenylyltransferase 3;
EC=2.7.7.18;
AltName: Full=Pyridine nucleotide adenylyltransferase 3;
Short=PNAT-3;
EC=2.7.7.1;
Name=NMNAT3; ORFNames=FKSG76;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Wang Y.-G., Gong L.;
"Identification of FKSG76, a novel gene encoding a NMN
adenylyltransferase.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain cortex;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16118205; DOI=10.1074/jbc.M508660200;
Berger F., Lau C., Dahlmann M., Ziegler M.;
"Subcellular compartmentation and differential catalytic properties of
the three human nicotinamide mononucleotide adenylyltransferase
isoforms.";
J. Biol. Chem. 280:36334-36341(2005).
[7]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND
COFACTOR.
PubMed=17402747; DOI=10.1021/bi6023379;
Sorci L., Cimadamore F., Scotti S., Petrelli R., Cappellacci L.,
Franchetti P., Orsomando G., Magni G.;
"Initial-rate kinetics of human NMN-adenylyltransferases: substrate
and metal ion specificity, inhibition by products and multisubstrate
analogues, and isozyme contributions to NAD+ biosynthesis.";
Biochemistry 46:4912-4922(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NMN; NAD AND ATP
ANALOG, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=12574164; DOI=10.1074/jbc.M300073200;
Zhang X., Kurnasov O.V., Karthikeyan S., Grishin N.V., Osterman A.L.,
Zhang H.;
"Structural characterization of a human cytosolic NMN/NaMN
adenylyltransferase and implication in human NAD biosynthesis.";
J. Biol. Chem. 278:13503-13511(2003).
-!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide
mononucleotide (NMN) and ATP. Can also use the deamidated form;
nicotinic acid mononucleotide (NaMN) as substrate with the same
efficiency. Can use triazofurin monophosphate (TrMP) as substrate.
Can also use GTP and ITP as nucleotide donors. Also catalyzes the
reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+).
For the pyrophosphorolytic activity, can use NAD(+), NADH, NaAD,
nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide
guanine dinucleotide (NGD) as substrates. Fails to cleave
phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Protects
against axonal degeneration following injury.
{ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+).
-!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide =
diphosphate + deamido-NAD(+).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17402747};
Note=Divalent metal cations. Mg(2+) confers the highest activity.
{ECO:0000269|PubMed:17402747};
-!- ENZYME REGULATION: Activity is strongly inhibited by galotannin.
Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-
tetraphosphate (Nap4AD). {ECO:0000269|PubMed:17402747}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=209 uM for NMN {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=130 uM for NAD(+) {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=29 uM for ATP {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=390 uM for PPi {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=276 uM for GTP {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=350 uM for ITP {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=111 uM for NaMN {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=130 uM for NMNH {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
KM=2.01 uM for triazofurin monophosphate
{ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
Vmax=3.6 umol/min/mg enzyme for NAD synthesis
{ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
Vmax=12.8 umol/min/mg enzyme for pyrophosphorolytic NAD(+)
cleavage {ECO:0000269|PubMed:16118205,
ECO:0000269|PubMed:17402747};
Vmax=2.9 umol/min/mg enzyme for pyrophosphorolytic NADH cleavage
{ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
nicotinamide D-ribonucleotide: step 1/1.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-
NAD(+) from nicotinate D-ribonucleotide: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12574164}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12574164,
ECO:0000269|PubMed:16118205}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q96T66-1; Sequence=Displayed;
Name=2;
IsoId=Q96T66-2; Sequence=VSP_010267;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q96T66-3; Sequence=VSP_043203;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in lung and spleen with lower levels
in placenta and kidney. {ECO:0000269|PubMed:12574164,
ECO:0000269|PubMed:16118205}.
-!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
family. {ECO:0000305}.
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EMBL; AF345564; AAK52726.1; -; mRNA.
EMBL; AK123208; BAG53878.1; -; mRNA.
EMBL; AC046134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC110716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79023.1; -; Genomic_DNA.
EMBL; CH471052; EAW79024.1; -; Genomic_DNA.
EMBL; CH471052; EAW79025.1; -; Genomic_DNA.
EMBL; CH471052; EAW79030.1; -; Genomic_DNA.
EMBL; CH471052; EAW79031.1; -; Genomic_DNA.
EMBL; BC034374; AAH34374.1; -; mRNA.
CCDS; CCDS3111.1; -. [Q96T66-2]
CCDS; CCDS56282.1; -. [Q96T66-3]
CCDS; CCDS82846.1; -. [Q96T66-1]
RefSeq; NP_001186976.1; NM_001200047.2. [Q96T66-3]
RefSeq; NP_001307440.1; NM_001320511.1. [Q96T66-1]
RefSeq; NP_001307441.1; NM_001320512.1. [Q96T66-1]
RefSeq; NP_835471.1; NM_178177.4. [Q96T66-2]
RefSeq; XP_011511092.1; XM_011512790.1. [Q96T66-2]
RefSeq; XP_011511093.1; XM_011512791.2. [Q96T66-2]
RefSeq; XP_016861824.1; XM_017006335.1. [Q96T66-1]
RefSeq; XP_016861825.1; XM_017006336.1. [Q96T66-1]
RefSeq; XP_016861826.1; XM_017006337.1. [Q96T66-1]
RefSeq; XP_016861827.1; XM_017006338.1. [Q96T66-2]
UniGene; Hs.208673; -.
UniGene; Hs.745268; -.
PDB; 1NUP; X-ray; 1.90 A; A/B=1-252.
PDB; 1NUQ; X-ray; 1.90 A; A/B=1-252.
PDB; 1NUR; X-ray; 2.15 A; A/B=1-252.
PDB; 1NUS; X-ray; 2.20 A; A/B=1-252.
PDB; 1NUT; X-ray; 1.90 A; A/B=1-252.
PDB; 1NUU; X-ray; 1.90 A; A/B=1-252.
PDBsum; 1NUP; -.
PDBsum; 1NUQ; -.
PDBsum; 1NUR; -.
PDBsum; 1NUS; -.
PDBsum; 1NUT; -.
PDBsum; 1NUU; -.
ProteinModelPortal; Q96T66; -.
SMR; Q96T66; -.
BioGrid; 131564; 4.
STRING; 9606.ENSP00000340523; -.
DrugBank; DB04099; Deamido-Nad+.
DrugBank; DB03227; Nicotinamide Mononucleotide.
iPTMnet; Q96T66; -.
PhosphoSitePlus; Q96T66; -.
DMDM; 116242680; -.
EPD; Q96T66; -.
MaxQB; Q96T66; -.
PaxDb; Q96T66; -.
PeptideAtlas; Q96T66; -.
PRIDE; Q96T66; -.
DNASU; 349565; -.
Ensembl; ENST00000296202; ENSP00000296202; ENSG00000163864. [Q96T66-1]
Ensembl; ENST00000339837; ENSP00000340523; ENSG00000163864. [Q96T66-2]
Ensembl; ENST00000413939; ENSP00000412953; ENSG00000163864. [Q96T66-3]
GeneID; 349565; -.
KEGG; hsa:349565; -.
UCSC; uc003etj.4; human. [Q96T66-1]
CTD; 349565; -.
DisGeNET; 349565; -.
EuPathDB; HostDB:ENSG00000163864.14; -.
GeneCards; NMNAT3; -.
HGNC; HGNC:20989; NMNAT3.
HPA; HPA039077; -.
HPA; HPA057402; -.
MIM; 608702; gene.
neXtProt; NX_Q96T66; -.
OpenTargets; ENSG00000163864; -.
PharmGKB; PA134952303; -.
eggNOG; KOG3199; Eukaryota.
eggNOG; COG1057; LUCA.
GeneTree; ENSGT00530000063189; -.
HOGENOM; HOG000216047; -.
HOVERGEN; HBG052640; -.
InParanoid; Q96T66; -.
KO; K06210; -.
OMA; SHHRVAM; -.
OrthoDB; EOG091G0JTI; -.
PhylomeDB; Q96T66; -.
TreeFam; TF315035; -.
BioCyc; MetaCyc:HS08953-MONOMER; -.
BRENDA; 2.7.7.1; 2681.
BRENDA; 2.7.7.18; 2681.
Reactome; R-HSA-196807; Nicotinate metabolism.
SABIO-RK; Q96T66; -.
UniPathway; UPA00253; UER00332.
UniPathway; UPA00253; UER00600.
ChiTaRS; NMNAT3; human.
EvolutionaryTrace; Q96T66; -.
GenomeRNAi; 349565; -.
PRO; PR:Q96T66; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000163864; -.
CleanEx; HS_NMNAT3; -.
ExpressionAtlas; Q96T66; baseline and differential.
Genevisible; Q96T66; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IBA:GO_Central.
GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:UniProtKB.
GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
GO; GO:0009435; P:NAD biosynthetic process; IC:UniProtKB.
GO; GO:0019674; P:NAD metabolic process; TAS:Reactome.
GO; GO:0009611; P:response to wounding; IEA:Ensembl.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR004821; Cyt_trans-like.
InterPro; IPR005248; NadD/NMNAT.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF01467; CTP_transf_like; 1.
TIGRFAMs; TIGR00482; TIGR00482; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Magnesium; Mitochondrion; NAD; Nucleotide-binding;
Nucleotidyltransferase; Pyridine nucleotide biosynthesis;
Reference proteome; Transferase.
CHAIN 1 252 Nicotinamide/nicotinic acid
mononucleotide adenylyltransferase 3.
/FTId=PRO_0000135016.
NP_BIND 13 15 ATP. {ECO:0000269|PubMed:12574164}.
NP_BIND 135 137 ATP. {ECO:0000269|PubMed:12574164}.
NP_BIND 203 206 ATP. {ECO:0000269|PubMed:12574164}.
REGION 53 55 Substrate binding.
{ECO:0000269|PubMed:12574164}.
REGION 90 93 Substrate binding.
{ECO:0000269|PubMed:12574164}.
REGION 147 148 Substrate binding.
{ECO:0000269|PubMed:12574164}.
BINDING 22 22 ATP. {ECO:0000269|PubMed:12574164}.
BINDING 56 56 ATP. {ECO:0000269|PubMed:12574164}.
BINDING 140 140 ATP; shared with dimeric partner.
{ECO:0000269|PubMed:12574164}.
VAR_SEQ 1 37 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010267.
VAR_SEQ 37 125 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043203.
CONFLICT 169 169 G -> S (in Ref. 1; AAK52726).
{ECO:0000305}.
STRAND 5 13 {ECO:0000244|PDB:1NUP}.
HELIX 20 35 {ECO:0000244|PDB:1NUP}.
STRAND 37 48 {ECO:0000244|PDB:1NUP}.
STRAND 54 56 {ECO:0000244|PDB:1NUP}.
HELIX 61 71 {ECO:0000244|PDB:1NUP}.
HELIX 72 74 {ECO:0000244|PDB:1NUP}.
STRAND 76 80 {ECO:0000244|PDB:1NUP}.
HELIX 83 86 {ECO:0000244|PDB:1NUP}.
STRAND 87 89 {ECO:0000244|PDB:1NUP}.
HELIX 93 104 {ECO:0000244|PDB:1NUP}.
STRAND 129 135 {ECO:0000244|PDB:1NUP}.
HELIX 136 141 {ECO:0000244|PDB:1NUP}.
TURN 145 147 {ECO:0000244|PDB:1NUP}.
HELIX 150 159 {ECO:0000244|PDB:1NUP}.
STRAND 162 165 {ECO:0000244|PDB:1NUP}.
HELIX 172 178 {ECO:0000244|PDB:1NUP}.
HELIX 180 184 {ECO:0000244|PDB:1NUP}.
HELIX 186 188 {ECO:0000244|PDB:1NUP}.
STRAND 189 192 {ECO:0000244|PDB:1NUP}.
HELIX 202 210 {ECO:0000244|PDB:1NUP}.
HELIX 221 229 {ECO:0000244|PDB:1NUP}.
TURN 230 233 {ECO:0000244|PDB:1NUQ}.
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


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EIAAB27399 Bos taurus,Bovine,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 1,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 1,NMNAT1
EIAAB27401 Bos taurus,Bovine,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 2,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 2,NMNAT2
EIAAB27402 NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 2,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 2,Nmnat2,Rat,Rattus norvegicus
EIAAB27405 Mouse,Mus musculus,NaMN adenylyltransferase 1,Nicotinamide mononucleotide adenylyltransferase 3,Nicotinate-nucleotide adenylyltransferase 1,NMN adenylyltransferase 3,Nmnat3
EIAAB27403 C1orf15,Homo sapiens,Human,KIAA0479,NaMN adenylyltransferase 2,Nicotinamide mononucleotide adenylyltransferase 2,Nicotinate-nucleotide adenylyltransferase 2,NMN adenylyltransferase 2,NMNAT2
REN-384 Recombinant Human Nicotinamide Nucleotide Adenylyltransferase 1 5
enz-384 Recombinant Human Nicotinamide Nucleotide Adenylyltransferase 1 5
enz-384 Recombinant Human Nicotinamide Nucleotide Adenylyltransferase 1 1mg
E13387h Human Nicotinamide Nucleotide Adenylyltransferase 96T
enz-384 Recombinant Human Nicotinamide Nucleotide Adenylyltransferase 1 20
E13388h Human Nicotinamide Nucleotide Adenylyltransferase 96T
NMS NMNAT3 Gene nicotinamide nucleotide adenylyltransferase 3
enz-384 Recombinant Human Nicotinamide Nucleotide Adenylyltransferase 1 ENZYMES 5
OETENZ-384 Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant 5
enz-384 Recombinant Human Nicotinamide Nucleotide Adenylyltransferase 1 NMNAT1 20
OETENZ-384 Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant 20
enz-384 Recombinant Human Nicotinamide Nucleotide Adenylyltransferase 1 ENZYMES 20
7-03225 Recombinant Human Nicotinamide Nucleotide Adenylyltransferase 1 1mg
ant-018 Mouse Anti Human Nicotinamide Nucleotide Adenylyltransferase 1 100
enz-384 Recombinant Human Nicotinamide Nucleotide Adenylyltransferase 1 NMNAT1 5
NMNAT3 NMNAT1 Gene nicotinamide nucleotide adenylyltransferase 1


 

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