NADA_NEUCR
ID NADA_NEUCR Reviewed; 243 AA.
AC Q7S936;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Conidial surface nicotinamide adenine dinucleotide glycohydrolase {ECO:0000303|PubMed:33712585};
DE Short=NAD(P)ase {ECO:0000303|PubMed:6237174};
DE Short=NADase {ECO:0000303|PubMed:33712585};
DE AltName: Full=Diphosphopyridine nucleotidase {ECO:0000303|PubMed:14814150};
DE Short=DPNase {ECO:0000303|PubMed:14814150};
DE AltName: Full=NAD(+) hydrolase {ECO:0000303|PubMed:33712585};
DE EC=3.2.2.5 {ECO:0000269|PubMed:14814150, ECO:0000269|PubMed:33712585, ECO:0000269|PubMed:4384627, ECO:0000269|PubMed:6260480, ECO:0000269|PubMed:9193681, ECO:0000269|PubMed:9787786};
DE AltName: Full=NADP(+) hydrolase {ECO:0000303|PubMed:33712585};
DE EC=3.2.2.- {ECO:0000269|PubMed:33712585};
DE Flags: Precursor;
GN ORFNames=NCU07948;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=14814150; DOI=10.1016/s0021-9258(18)56182-2;
RA Nason A., Kaplan N.O., Colowick S.P.;
RT "Changes in enzymatic constitution in zinc-deficient Neurospora.";
RL J. Biol. Chem. 188:397-406(1951).
RN [3]
RP INDUCTION.
RX DOI=10.1002/j.1537-2197.1956.tb10471.x;
RA Zalokar M., Cochrane V.W.;
RT "Diphosphopyridine nucleotidase in the life cycle of Neurospora crassa.";
RL Am. J. Bot. 43:107-110(1956).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=4384627; DOI=10.1083/jcb.37.1.81;
RA Stine G.J.;
RT "Enzyme activities during the asexual cycle of Neurospora crassa. II.
RT NAD- and NADP-dependent glutamic dehydrogenases and nicotinamide adenine
RT dinucleotidase.";
RL J. Cell Biol. 37:81-88(1968).
RN [5]
RP INDUCTION.
RX PubMed=5111767; DOI=10.1016/0012-1606(71)90103-5;
RA Urey J.C.;
RT "Enzyme patterns and protein synthesis during synchronous conidiation in
RT Neurospora crassa.";
RL Dev. Biol. 26:17-27(1971).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=165174; DOI=10.1128/jb.122.2.695-709.1975;
RA Nelson R.E., Selitrennikoff C.P., Siegel R.W.;
RT "Mutants of Neurospora deficient in nicotinamide adenine dinucleotide
RT (phosphate) glycohydrolase.";
RL J. Bacteriol. 122:695-709(1975).
RN [7]
RP INDUCTION, AND FUNCTION.
RX PubMed=131723; DOI=10.1016/0012-1606(76)90072-5;
RA Nelson R.E., Selitrennikoff C.P., Siegel R.W.;
RT "Developmental regulation of nicotinamide adenine dinucleotide (phosphate)
RT glycohydrolase in Neurospora crassa.";
RL Dev. Biol. 50:122-133(1976).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND GLYCOSYLATION.
RX PubMed=6260480; DOI=10.1111/j.1432-1033.1981.tb05089.x;
RA Menegus F., Pace M.;
RT "Purification and some properties of NAD-glycohydrolase from conidia of
RT Neurospora crassa.";
RL Eur. J. Biochem. 113:485-490(1981).
RN [9]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=6237174; DOI=10.1099/00221287-130-6-1563;
RA Jorge J.A., Terenzi H.F.;
RT "Carbon source regulation of nicotinamide adenine dinucleotide (phosphate)
RT glycohydrolase in Neurospora crassa: induction and repression of enzyme
RT synthesis.";
RL J. Gen. Microbiol. 130:1563-1568(1984).
RN [10]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=9193681; DOI=10.1007/978-1-4419-8632-0_51;
RA Pace M., Agnellini D., Lippoli G., Berger R.L.;
RT "Hydrophobic properties of NAD glycohydrolase from neurospora crassa
RT conidia and interaction with dioxane.";
RL Adv. Exp. Med. Biol. 419:389-397(1997).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND
RP AUTO-ADP-RIBOSYLATION.
RX PubMed=9787786; DOI=10.1016/s0305-0491(98)10006-8;
RA Cho Y.S., Han M.K., Kwark O.S., Phoe M.S., Cha Y.S., An N.H., Kim U.H.;
RT "Auto-ADP-ribosylation of NAD glycohydrolase from Neurospora crassa.";
RL Comp. Biochem. Physiol. 120:175-181(1998).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND GLYCOSYLATION.
RX PubMed=33712585; DOI=10.1038/s41467-021-21307-z;
RA Stroemland O., Kallio J.P., Pschibul A., Skoge R.H., Hardardottir H.M.,
RA Sverkeli L.J., Heinekamp T., Kniemeyer O., Migaud M., Makarov M.V.,
RA Gossmann T.I., Brakhage A.A., Ziegler M.;
RT "Discovery of fungal surface NADases predominantly present in pathogenic
RT species.";
RL Nat. Commun. 12:1631-1631(2021).
RN [13]
RP ERRATUM OF PUBMED:33712585.
RX PubMed=33767192; DOI=10.1038/s41467-021-22476-7;
RA Stroemland O., Kallio J.P., Pschibul A., Skoge R.H., Hardardottir H.M.,
RA Sverkeli L.J., Heinekamp T., Kniemeyer O., Migaud M., Makarov M.V.,
RA Gossmann T.I., Brakhage A.A., Ziegler M.;
RT "Author Correction: Discovery of fungal surface NADases predominantly
RT present in pathogenic species.";
RL Nat. Commun. 12:2004-2004(2021).
CC -!- FUNCTION: Conidial surface nicotinamide adenine dinucleotide
CC glycohydrolase that cleave NAD(+) and NADP(+) but not their reduced
CC counterparts, NADH and NADPH (PubMed:6260480, PubMed:33712585). Lacks
CC both ADP-ribosyl cyclase and base exchange activity and does not
CC mediate synthesis of calcium messengers cADPR or NAADP
CC (PubMed:33712585). Its function is correlated with aerial hyphae
CC formation and conidiogenesis, but its physiological role is still
CC obscure (PubMed:165174, PubMed:131723). Is able to ADP-ribosylate
CC itself for self-inactivation (PubMed:9787786).
CC {ECO:0000269|PubMed:131723, ECO:0000269|PubMed:165174,
CC ECO:0000269|PubMed:33712585, ECO:0000269|PubMed:6260480,
CC ECO:0000269|PubMed:9787786}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5;
CC Evidence={ECO:0000269|PubMed:14814150, ECO:0000269|PubMed:33712585,
CC ECO:0000269|PubMed:4384627, ECO:0000269|PubMed:6260480,
CC ECO:0000269|PubMed:9193681, ECO:0000269|PubMed:9787786};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000269|PubMed:33712585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) +
CC nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58673; Evidence={ECO:0000269|PubMed:14814150,
CC ECO:0000269|PubMed:33712585, ECO:0000269|PubMed:4384627,
CC ECO:0000269|PubMed:6260480, ECO:0000269|PubMed:9193681,
CC ECO:0000269|PubMed:9787786};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850;
CC Evidence={ECO:0000269|PubMed:33712585};
CC -!- ACTIVITY REGULATION: Both aliphatic amines and carboxylic acids are
CC able to inhibit non-competitively the catalytic activity
CC (PubMed:9193681). The inhibition depends on the non-polar moiety of the
CC substances (PubMed:9193681). Dioxane also acts as an inhibitor of
CC NADase activity (PubMed:9193681). Auto-ADP-ribosylation acts as a
CC mechanism of self-inactivation by its substrate (PubMed:9787786).
CC {ECO:0000269|PubMed:9193681, ECO:0000269|PubMed:9787786}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4WL81}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6237174,
CC ECO:0000269|PubMed:6260480}. Note=Localizes on the surface of conidia.
CC {ECO:0000269|PubMed:6260480}.
CC -!- INDUCTION: Expression is up-regulated in mycelia grown in a zinc-
CC deficient medium (PubMed:14814150). Expression is strongly induced with
CC the formation of aerial hyphae, accumulates in conidia and decreases
CC very fast as the mature conidia germinate (Ref.3, PubMed:4384627,
CC PubMed:5111767, PubMed:131723). Induced by the presence of proteins in
CC the culture medium (PubMed:6237174). Low concentrations of sucrose or
CC glucose, Casamino acids or some amino acids such as methionine,
CC cysteine, phenylalanine and tryptophan strongly repress the expression
CC (PubMed:6237174). {ECO:0000269|PubMed:131723,
CC ECO:0000269|PubMed:14814150, ECO:0000269|PubMed:4384627,
CC ECO:0000269|PubMed:5111767, ECO:0000269|PubMed:6237174,
CC ECO:0000269|Ref.3}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:33767192,
CC ECO:0000269|PubMed:6260480}.
CC -!- PTM: Auto-ADP-ribosylated. {ECO:0000269|PubMed:9787786}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the growth of aerial hyphae,
CC conidiation or conidial germination. {ECO:0000269|PubMed:165174}.
CC -!- SIMILARITY: Belongs to the fungal surface NADase family. {ECO:0000305}.
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DR EMBL; CM002239; EAA32845.1; -; Genomic_DNA.
DR RefSeq; XP_962081.1; XM_956988.2.
DR SMR; Q7S936; -.
DR EnsemblFungi; EAA32845; EAA32845; NCU07948.
DR GeneID; 3878246; -.
DR KEGG; ncr:NCU07948; -.
DR VEuPathDB; FungiDB:NCU07948; -.
DR HOGENOM; CLU_083054_0_1_1; -.
DR InParanoid; Q7S936; -.
DR OMA; RCYPDPC; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0061810; F:NAD glycohydrolase activity; IEA:InterPro.
DR InterPro; IPR025331; TNT.
DR Pfam; PF14021; TNT; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; NAD; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..243
FT /note="Conidial surface nicotinamide adenine dinucleotide
FT glycohydrolase"
FT /id="PRO_5004292681"
FT DOMAIN 141..231
FT /note="TNT"
FT /evidence="ECO:0000255"
FT REGION 20..137
FT /note="Thump"
FT /evidence="ECO:0000250|UniProtKB:Q4WL81"
FT ACT_SITE 150
FT /evidence="ECO:0000250|UniProtKB:Q4WL81"
FT ACT_SITE 214
FT /evidence="ECO:0000250|UniProtKB:Q4WL81"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q4WL81"
FT BINDING 169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q4WL81"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 46..102
FT /evidence="ECO:0000250|UniProtKB:Q4WL81"
FT DISULFID 56..71
FT /evidence="ECO:0000250|UniProtKB:Q4WL81"
SQ SEQUENCE 243 AA; 26378 MW; 8BCF4B56BBBFD037 CRC64;
MKFTLLSTAV ALLTSTAVAL PTSSSSAGSL LNERSYVNAS STATTCPYSR RSPAYCAGTA
QNRTLSATYI CGDSRLGPVV LPQFFLPLDP ILDIYDRFGG LCPGAFLEKW FNQTGSGWWD
YPPQNGFSVD DEGNIIAANL TLQTGTFVDR FGSEYGSFLA PAAAPYLQRS LPPSNLNGDA
KFPWNYHVYS VIKPFAVLAG PIAPWFGQPG QGVQYQTYEN VATLIADGYL KAEDPQRLVP
RNY
