NRL4B_TOBAC
ID NRL4B_TOBAC Reviewed; 348 AA.
AC Q42966;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Bifunctional nitrilase/nitrile hydratase NIT4B;
DE Short=TNIT4B;
DE EC=3.5.5.1;
DE EC=3.5.5.4;
DE AltName: Full=Cyanoalanine nitrilase B;
DE AltName: Full=Nitrilase 4B;
GN Name=NIT4B;
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.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
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=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 -!- 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 -!- 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; D83078; BAA11770.1; -; mRNA.
DR PIR; T03739; T03739.
DR RefSeq; NP_001313199.1; NM_001326270.1.
DR AlphaFoldDB; Q42966; -.
DR SMR; Q42966; -.
DR STRING; 4097.Q42966; -.
DR GeneID; 107832013; -.
DR KEGG; nta:107832013; -.
DR OMA; PKGLDFG; -.
DR Proteomes; UP000084051; Unplaced.
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 Hydrolase; Reference proteome.
FT CHAIN 1..348
FT /note="Bifunctional nitrilase/nitrile hydratase NIT4B"
FT /id="PRO_0000352512"
FT DOMAIN 29..300
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 348 AA; 37534 MW; C60EE246CB87D793 CRC64;
MALVPTPVVN EGPMFAEVDM GDNSSTPTVR ATVVQASTIF YDTPATLDKA ERLLAEAASY
GAQLVVFPEA FIGGYPRGST FGVSIGNRTA KGKEEFRKYH ASAIDVPGPE VDRLAAMAGK
YKVYLVMGVI ERDGYTLYCT VLFFDSQGHY LGKHRKIMPT ALERIIWGFG DGSTIPVYDT
PLGKIGAAIC WENRMPLLRT AMYAKGIEIY CAPTADSRDV WQASMTHIAL EGGCFVLSAN
QFCRRKDYPP PPEYVFSGTE DLTPDSIVCA GGSVIISPSG AVLAGPNYEG EALISADLDL
GEIARAKFDF DVVGHYARPE VLSLIVRDHA VSPVSFTSTS SKAESSPK
