ID   NRL4A_LUPAN             Reviewed;         349 AA.
AC   Q5QGZ8; Q6QDB7;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Bifunctional nitrilase/nitrile hydratase NIT4A;
DE            Short=LaNIT4A;
DE            EC=3.5.5.4;
DE            EC=4.2.1.65;
DE   AltName: Full=3-cyanoalanine hydratase;
DE   AltName: Full=Cyanoalanine nitrilase A;
GN   Name=NIT4A;
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Azuro;
RX   PubMed=16786295; DOI=10.1007/s11103-005-6217-9;
RA   Piotrowski M., Volmer J.J.;
RT   "Cyanide metabolism in higher plants: cyanoalanine hydratase is a NIT4
RT   homolog.";
RL   Plant Mol. Biol. 61:111-122(2006).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA   Shearer A.G., Altman T., Rhee C.D.;
RT   "Finding sequences for over 270 orphan enzymes.";
RL   PLoS ONE 9:E97250-E97250(2014).
CC   -!- FUNCTION: Involved in the cyanide detoxification pathway. Has nitrilase
CC       and nitrile-hydratase activity in the ratio 4.0:1, producing both
CC       asparagine and aspartic acid from beta-cyano-L-alanine (Ala(CN)). Can
CC       also use 3-phenylpropionitrile as substrate, but not indole-3-
CC       acetonitrile. {ECO:0000269|PubMed:16786295}.
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         Evidence={ECO:0000269|PubMed:16786295};
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         Evidence={ECO:0000269|PubMed:16786295};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.18 mM for Ala(CN) {ECO:0000269|PubMed:16786295};
CC         Vmax=477.7 nmol/sec/mg enzyme for the nitrilase activity
CC         {ECO:0000269|PubMed:16786295};
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16786295}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; AY547301; AAT36331.1; -; mRNA.
DR   EMBL; DQ241759; ABB51979.1; -; Genomic_DNA.
DR   EMBL; AY547303; AAS55944.1; -; Genomic_DNA.
DR   RefSeq; XP_019448859.1; XM_019593314.1.
DR   AlphaFoldDB; Q5QGZ8; -.
DR   SMR; Q5QGZ8; -.
DR   EnsemblPlants; OIW08474; OIW08474; TanjilG_03150.
DR   GeneID; 109351736; -.
DR   Gramene; OIW08474; OIW08474; TanjilG_03150.
DR   KEGG; lang:109351736; -.
DR   OrthoDB; 1001274at2759; -.
DR   BioCyc; MetaCyc:MON-17621; -.
DR   BRENDA; 3.5.5.4; 3090.
DR   BRENDA; 4.2.1.65; 3090.
DR   SABIO-RK; Q5QGZ8; -.
DR   GO; GO:0047558; F:3-cyanoalanine hydratase activity; IDA:UniProtKB.
DR   GO; GO:0047427; F:cyanoalanine nitrilase activity; IDA:UniProtKB.
DR   GO; GO:0019500; P:cyanide catabolic process; IDA:UniProtKB.
DR   GO; GO:0051410; P:detoxification of nitrogen compound; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Hydrolase; Lyase.
FT   CHAIN           1..349
FT                   /note="Bifunctional nitrilase/nitrile hydratase NIT4A"
FT                   /id="PRO_0000430146"
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                   /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;  37762 MW;  BEC5FEFC46D52068 CRC64;
     MALVTTPTVN DGPLFAEVNM SSDFNAPTVR ATVVQASTIF YDTPATLDKA ERLLAEAASY
     GAQIVVFPEA FIGGYPRGSN FGVSIGNRTA KGKEDFRKYH SAAIDVPGPE VDRLAALAGK
     YKVYLVMGVI ERDGYTLYCT VLFFGAQGRY LGKHRKLMPT ALERIIWGFG DGSTIPVFET
     PIGKIGAAIC WENKMPLLRT AMYAKGVEIY CAPTADSREV WQASMTHIAL EGGCFVLSAN
     QFCRRRDYPP PPEYVFEGTE ENLTPDSVVC AGGSVIISPS GAVLAGPSYE GEALISADLD
     LGEIARAKFD FDVVGHYSRP EVLSLVVKDH PTNPVTFTSA STKIEDKTK