ID   NRL4B_LUPAN             Reviewed;         350 AA.
AC   Q3LRV4;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Bifunctional nitrilase/nitrile hydratase NIT4B;
DE            Short=LaNIT4B;
DE            EC=3.5.5.4;
DE            EC=4.2.1.65;
DE   AltName: Full=3-cyanoalanine hydratase;
DE   AltName: Full=Cyanoalanine nitrilase B;
GN   Name=NIT4B;
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, AND 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 3.3:1, 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=0.93 mM for Ala(CN) {ECO:0000269|PubMed:16786295};
CC         Vmax=114.6 nmol/sec/mg enzyme for the nitrilase activity
CC         {ECO:0000269|PubMed:16786295};
CC   -!- TISSUE SPECIFICITY: Highly expressed in leaves and cotyledons, lower
CC       expression in stems and roots. {ECO:0000269|PubMed:16786295}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Nitrilase family. {ECO:0000305}.
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DR   EMBL; DQ186678; ABA28312.1; -; mRNA.
DR   EMBL; DQ241760; ABB51980.1; -; Genomic_DNA.
DR   RefSeq; XP_019451519.1; XM_019595974.1.
DR   AlphaFoldDB; Q3LRV4; -.
DR   SMR; Q3LRV4; -.
DR   EnsemblPlants; OIW05882; OIW05882; TanjilG_23668.
DR   GeneID; 109353638; -.
DR   Gramene; OIW05882; OIW05882; TanjilG_23668.
DR   KEGG; lang:109353638; -.
DR   OrthoDB; 1001274at2759; -.
DR   BioCyc; MetaCyc:MON-17622; -.
DR   BRENDA; 3.5.5.4; 3090.
DR   SABIO-RK; Q3LRV4; -.
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..350
FT                   /note="Bifunctional nitrilase/nitrile hydratase NIT4B"
FT                   /id="PRO_0000430147"
FT   DOMAIN          30..302
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        191
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054,
FT                   ECO:0000255|PROSITE-ProRule:PRU10105"
SQ   SEQUENCE   350 AA;  38055 MW;  D3FCC3FBA02C9455 CRC64;
     MALVTTTPTV NDEPLFAEVD MASYFTSTTV RATVVQASTI FYDTPATLDK AERLLVQAAS
     YGAQIVVFPE AFIGGYPRGS NFGVSIGNRT AKGKEEFRKY HSAAIDVPGP EVDRLSAMAG
     KYKVYLVMGV IERDGYTLYC TVLFFDSQGR YLGKHRKVMP TALERIIWGF GDGSTIPVFQ
     TPIGKIGAAI CWENKMPLLR TAMYAKGVEI YCAPTADSRD LWQASTTHIA LEGGCFVLSA
     NQFCRRKDYP PPPEYVFSGT EEDLTPDSVV SAGGSVIISP SGAVLAGPNY EGEALISADL
     DLGEIARAKF DFDVVGHYSR SEVLSLIVKD HPTNPVTFTS TSTKIEDQTK