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Bifunctional nitrilase/nitrile hydratase NIT4B (LaNIT4B) (EC 3.5.5.4) (EC 4.2.1.65) (3-cyanoalanine hydratase) (Cyanoalanine nitrilase B)

 NRL4B_LUPAN             Reviewed;         350 AA.
Q3LRV4;
03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 1.
23-MAY-2018, entry version 41.
RecName: Full=Bifunctional nitrilase/nitrile hydratase NIT4B;
Short=LaNIT4B;
EC=3.5.5.4;
EC=4.2.1.65;
AltName: Full=3-cyanoalanine hydratase;
AltName: Full=Cyanoalanine nitrilase B;
Name=NIT4B;
Lupinus angustifolius (Narrow-leaved blue lupine).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Genisteae; Lupinus.
NCBI_TaxID=3871;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC
ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
STRAIN=cv. Azuro;
PubMed=16786295; DOI=10.1007/s11103-005-6217-9;
Piotrowski M., Volmer J.J.;
"Cyanide metabolism in higher plants: cyanoalanine hydratase is a NIT4
homolog.";
Plant Mol. Biol. 61:111-122(2006).
[2]
IDENTIFICATION.
PubMed=24826896; DOI=10.1371/journal.pone.0097250;
Shearer A.G., Altman T., Rhee C.D.;
"Finding sequences for over 270 orphan enzymes.";
PLoS ONE 9:E97250-E97250(2014).
-!- FUNCTION: Involved in the cyanide detoxification pathway. Has
nitrilase and nitrile-hydratase activity in the ratio 3.3:1,
producing both asparagine and aspartic acid from beta-cyano-L-
alanine (Ala(CN)). Can also use 3-phenylpropionitrile as
substrate, but not indole-3-acetonitrile.
{ECO:0000269|PubMed:16786295}.
-!- CATALYTIC ACTIVITY: L-asparagine = 3-cyanoalanine + H(2)O.
{ECO:0000269|PubMed:16786295}.
-!- CATALYTIC ACTIVITY: 3-cyano-L-alanine + 2 H(2)O = L-aspartate +
NH(3). {ECO:0000269|PubMed:16786295}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.93 mM for Ala(CN) {ECO:0000269|PubMed:16786295};
Vmax=114.6 nmol/sec/mg enzyme for the nitrilase activity
{ECO:0000269|PubMed:16786295};
-!- TISSUE SPECIFICITY: Highly expressed in leaves and cotyledons,
lower expression in stems and roots.
{ECO:0000269|PubMed:16786295}.
-!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
Nitrilase family. {ECO:0000305}.
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EMBL; DQ186678; ABA28312.1; -; mRNA.
EMBL; DQ241760; ABB51980.1; -; Genomic_DNA.
RefSeq; XP_019451519.1; XM_019595974.1.
ProteinModelPortal; Q3LRV4; -.
SMR; Q3LRV4; -.
GeneID; 109353638; -.
KEGG; lang:109353638; -.
KO; K13035; -.
BioCyc; MetaCyc:MONOMER-17622; -.
BRENDA; 3.5.5.4; 3090.
GO; GO:0047558; F:3-cyanoalanine hydratase activity; IDA:UniProtKB.
GO; GO:0047427; F:cyanoalanine nitrilase activity; IDA:UniProtKB.
GO; GO:0019500; P:cyanide catabolic process; IDA:UniProtKB.
GO; GO:0051410; P:detoxification of nitrogen compound; IDA:UniProtKB.
Gene3D; 3.60.110.10; -; 1.
InterPro; IPR003010; C-N_Hydrolase.
InterPro; IPR036526; C-N_Hydrolase_sf.
InterPro; IPR000132; Nitrilase/CN_hydratase_CS.
Pfam; PF00795; CN_hydrolase; 1.
SUPFAM; SSF56317; SSF56317; 1.
PROSITE; PS50263; CN_HYDROLASE; 1.
PROSITE; PS00920; NITRIL_CHT_1; 1.
PROSITE; PS00921; NITRIL_CHT_2; 1.
1: Evidence at protein level;
Hydrolase; Lyase.
CHAIN 1 350 Bifunctional nitrilase/nitrile hydratase
NIT4B.
/FTId=PRO_0000430147.
DOMAIN 30 302 CN hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
COMPBIAS 250 253 Poly-Pro.
ACT_SITE 70 70 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 157 157 {ECO:0000255|PROSITE-ProRule:PRU00054}.
ACT_SITE 191 191 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00054, ECO:0000255|PROSITE-
ProRule:PRU10105}.
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


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