NRL4A_TOBAC
ID NRL4A_TOBAC Reviewed; 349 AA.
AC Q42965;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Bifunctional nitrilase/nitrile hydratase NIT4A;
DE Short=TNIT4A;
DE EC=3.5.5.1;
DE EC=3.5.5.4;
DE EC=4.2.1.65;
DE AltName: Full=3-cyanoalanine hydratase;
DE AltName: Full=Cyanoalanine nitrilase A;
DE AltName: Full=Nitrilase 4A;
GN Name=NIT4A;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. SR1; TISSUE=Leaf;
RA Tsunoda H., Yamaguchi K.;
RT "The cDNA sequence of an auxin-producing nitrilase homologue in tobacco.";
RL (er) Plant Gene Register PGR95-058(1995).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10574458; DOI=10.1093/dnares/6.5.313;
RA Dohmoto M., Sano J., Tsunoda H., Yamaguchi K.;
RT "Structural analysis of the TNIT4 genes encoding nitrilase-like protein
RT from tobacco.";
RL DNA Res. 6:313-317(1999).
RN [3]
RP FUNCTION.
RX PubMed=11089910; DOI=10.1093/dnares/7.5.283;
RA Dohmoto M., Tsunoda H., Isaji G., Chiba R., Yamaguchi K.;
RT "Genes encoding nitrilase-like proteins from tobacco.";
RL DNA Res. 7:283-289(2000).
RN [4]
RP FUNCTION.
RX PubMed=11060302; DOI=10.1074/jbc.m007890200;
RA Piotrowski M., Schoenfelder S., Weiler E.W.;
RT "The Arabidopsis thaliana isogene NIT4 and its orthologs in tobacco encode
RT beta-cyano-L-alanine hydratase/nitrilase.";
RL J. Biol. Chem. 276:2616-2621(2001).
CC -!- FUNCTION: Highly specific for beta-cyano-L-alanine (Ala(CN)). Low
CC activity with 3-phenylpropionitrile (PPN). Not associated with auxin
CC production but may be involved in cyanide detoxification.
CC {ECO:0000269|PubMed:10574458, ECO:0000269|PubMed:11060302,
CC ECO:0000269|PubMed:11089910}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nitrile + 2 H2O = a carboxylate + NH4(+);
CC Xref=Rhea:RHEA:21724, ChEBI:CHEBI:15377, ChEBI:CHEBI:18379,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29067; EC=3.5.5.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10105};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-cyano-L-alanine + 2 H2O = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:11188, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:77860; EC=3.5.5.4;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparagine = 3-cyano-L-alanine + H2O; Xref=Rhea:RHEA:15385,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58048, ChEBI:CHEBI:77860; EC=4.2.1.65;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Tightly associated with the plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, cotyledons, leaves and
CC flowers. {ECO:0000269|PubMed:10574458}.
CC -!- INDUCTION: Not induced by abscisic acid or by 1-aminocyclopropane-1-
CC carboxylic acid (ACC). {ECO:0000269|PubMed:10574458}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC Nitrilase family. {ECO:0000305}.
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DR EMBL; D63331; BAA09645.1; -; mRNA.
DR PIR; T03736; T03736.
DR RefSeq; NP_001312683.1; NM_001325754.1.
DR AlphaFoldDB; Q42965; -.
DR SMR; Q42965; -.
DR STRING; 4097.Q42965; -.
DR GeneID; 107804379; -.
DR KEGG; nta:107804379; -.
DR PhylomeDB; Q42965; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047558; F:3-cyanoalanine hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0047427; F:cyanoalanine nitrilase activity; IEA:UniProtKB-EC.
DR GO; GO:0080061; F:indole-3-acetonitrile nitrilase activity; IEA:UniProtKB-EC.
DR GO; GO:0000257; F:nitrilase activity; IBA:GO_Central.
DR GO; GO:0018822; F:nitrile hydratase activity; IBA:GO_Central.
DR GO; GO:0051410; P:detoxification of nitrogen compound; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd07564; nitrilases_CHs; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR000132; Nitrilase/CN_hydratase_CS.
DR InterPro; IPR044149; Nitrilases_CHs.
DR PANTHER; PTHR46044; PTHR46044; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
DR PROSITE; PS00920; NITRIL_CHT_1; 1.
DR PROSITE; PS00921; NITRIL_CHT_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Hydrolase; Lyase; Membrane; Reference proteome.
FT CHAIN 1..349
FT /note="Bifunctional nitrilase/nitrile hydratase NIT4A"
FT /id="PRO_0000204040"
FT DOMAIN 29..301
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 69
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 156
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 190
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT ECO:0000255|PROSITE-ProRule:PRU10105"
SQ SEQUENCE 349 AA; 37555 MW; 8CEE7B014AD9C81F CRC64;
MALVPTPAVN EGPLFAEVDM GDNSSTPTVR ATVVQASTIF YDTPATLVKA ERLLAEAASY
GAQLVVFPEA FIGGYPRGST FGVSIGNRTA KGKEEFRKYH ASAIDVPGPE VDRLAAMAGK
YKVYLVMGVI ERDGYTLYCT VLFFDSQGHF LGKHRKIMPT ALERIIWGFG DGSTIPVYDT
PLGKIGAAIC WENRMPLLRT AMYAKGIEIY CAPTADSRDV WQASMTHIAL EGGCFVLSAN
QFCRRKDYPP PPEYVFSGTE EDLTPDSIVC AGGSVIISPS GAVLAGPNYV GEALISADLD
LGEIARAKFD FDVVGHYARP EVLSLIVRDH AVSPVSFTST SSKAESSPK
