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Nitrilase (EC 3.5.5.1) (PaNit)

 NITR_PYRAB              Reviewed;         262 AA.
Q9UYV8;
11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-FEB-2018, entry version 94.
RecName: Full=Nitrilase;
EC=3.5.5.1;
AltName: Full=PaNit;
OrderedLocusNames=PYRAB13990; ORFNames=PAB1449;
Pyrococcus abyssi (strain GE5 / Orsay).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Pyrococcus.
NCBI_TaxID=272844;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GE5 / Orsay;
PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C.,
Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
"An integrated analysis of the genome of the hyperthermophilic
archaeon Pyrococcus abyssi.";
Mol. Microbiol. 47:1495-1512(2003).
[2]
GENOME REANNOTATION.
STRAIN=GE5 / Orsay;
PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
Gao J., Wang J.;
"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5
and Pyrococcus furiosus DSM 3638.";
Curr. Microbiol. 64:118-129(2012).
[3]
IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION, AND SUBUNIT.
PubMed=16495079; DOI=10.1016/j.pep.2006.01.006;
Mueller P., Egorova K., Vorgias C.E., Boutou E., Trauthwein H.,
Verseck S., Antranikian G.;
"Cloning, overexpression, and characterization of a thermoactive
nitrilase from the hyperthermophilic archaeon Pyrococcus abyssi.";
Protein Expr. Purif. 47:672-681(2006).
[4]
X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF APOENZYME AND IN COMPLEXES
WITH ACETATE, SUBUNIT, DOCKING STUDIES, REACTION MECHANISM, AND ACTIVE
SITES.
STRAIN=GE5 / Orsay;
PubMed=21095228; DOI=10.1016/j.jsb.2010.11.017;
Raczynska J.E., Vorgias C.E., Antranikian G., Rypniewski W.;
"Crystallographic analysis of a thermoactive nitrilase.";
J. Struct. Biol. 173:294-302(2011).
-!- FUNCTION: Nitrilase that hydrolyzes preferentially aliphatic
nitriles like malononitrile and fumaronitrile in vitro. These
dinitriles are converted to the corresponding monoacid
mononitriles, showing the enzyme is regioselective. Cannot
hydrolyze compounds with a nitrile group bound to an aromatic ring
or amino acid. Its biological role is unknown.
{ECO:0000269|PubMed:16495079}.
-!- CATALYTIC ACTIVITY: A nitrile + 2 H(2)O = a carboxylate + NH(3).
{ECO:0000269|PubMed:16495079}.
-!- ENZYME REGULATION: Enzymatic activity is inhibited in the presence
of acetone, methanol and metal ions such as Ag(2+) and Hg(2+). Is
also inhibited by various thiol reagents such as DTNB, p-
chloromercuribenzoate, p-hydroxymercuribenzoate, iodacetamide and
iodacetate. EDTA has no influence on activity.
{ECO:0000269|PubMed:16495079}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.47 mM for malononitrile {ECO:0000269|PubMed:16495079};
KM=9.48 mM for fumaronitrile {ECO:0000269|PubMed:16495079};
pH dependence:
Optimum pH is 7.4. Active within the pH range of 4.5-8.5.
{ECO:0000269|PubMed:16495079};
Temperature dependence:
Optimum temperature is 80 degrees Celsius. Active at a broad
temperature range (60-90 degrees Celsius). Highly thermostable
with a half-life of 25 hours at 70 degrees Celsius, 9 hours at
80 degrees Celsius, and 6 hours at 90 degrees Celsius. Shows a
Tm of 112.7 degrees Celsius. {ECO:0000269|PubMed:16495079};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16495079,
ECO:0000269|PubMed:21095228}.
-!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
{ECO:0000305}.
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EMBL; AJ248287; CAB50304.1; -; Genomic_DNA.
EMBL; HE613800; CCE70842.1; -; Genomic_DNA.
PIR; C75051; C75051.
RefSeq; WP_010868514.1; NC_000868.1.
PDB; 3IVZ; X-ray; 1.57 A; A/B=1-262.
PDB; 3IW3; X-ray; 1.80 A; A/B=1-262.
PDB; 3KI8; X-ray; 1.60 A; A/B=1-262.
PDB; 3KLC; X-ray; 1.76 A; A/B=1-262.
PDBsum; 3IVZ; -.
PDBsum; 3IW3; -.
PDBsum; 3KI8; -.
PDBsum; 3KLC; -.
ProteinModelPortal; Q9UYV8; -.
SMR; Q9UYV8; -.
STRING; 272844.PAB1449; -.
EnsemblBacteria; CAB50304; CAB50304; PAB1449.
GeneID; 1496788; -.
KEGG; pab:PAB1449; -.
PATRIC; fig|272844.11.peg.1486; -.
eggNOG; arCOG00062; Archaea.
eggNOG; COG0388; LUCA.
HOGENOM; HOG000222700; -.
OMA; TGKDHWQ; -.
OrthoDB; POG093Z0FOF; -.
BioCyc; PABY272844:G1GT8-1536-MONOMER; -.
EvolutionaryTrace; Q9UYV8; -.
Proteomes; UP000000810; Chromosome.
Proteomes; UP000009139; Chromosome.
GO; GO:0000257; F:nitrilase activity; IEA:UniProtKB-EC.
GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
Gene3D; 3.60.110.10; -; 1.
InterPro; IPR003010; C-N_Hydrolase.
InterPro; IPR036526; C-N_Hydrolase_sf.
Pfam; PF00795; CN_hydrolase; 1.
SUPFAM; SSF56317; SSF56317; 1.
PROSITE; PS50263; CN_HYDROLASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase.
CHAIN 1 262 Nitrilase.
/FTId=PRO_0000429328.
DOMAIN 2 237 CN hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
REGION 173 174 Substrate binding. {ECO:0000255}.
ACT_SITE 42 42 Proton acceptor.
{ECO:0000305|PubMed:21095228}.
ACT_SITE 113 113 Proton donor.
{ECO:0000305|PubMed:21095228}.
ACT_SITE 146 146 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00054,
ECO:0000269|PubMed:21095228}.
STRAND 3 8 {ECO:0000244|PDB:3IVZ}.
HELIX 16 32 {ECO:0000244|PDB:3IVZ}.
STRAND 36 39 {ECO:0000244|PDB:3IVZ}.
TURN 42 46 {ECO:0000244|PDB:3IVZ}.
HELIX 53 59 {ECO:0000244|PDB:3IVZ}.
TURN 63 65 {ECO:0000244|PDB:3IVZ}.
HELIX 67 79 {ECO:0000244|PDB:3IVZ}.
STRAND 82 91 {ECO:0000244|PDB:3IVZ}.
STRAND 94 103 {ECO:0000244|PDB:3IVZ}.
STRAND 106 112 {ECO:0000244|PDB:3IVZ}.
HELIX 118 122 {ECO:0000244|PDB:3IVZ}.
STRAND 133 135 {ECO:0000244|PDB:3IVZ}.
STRAND 140 143 {ECO:0000244|PDB:3IVZ}.
HELIX 146 150 {ECO:0000244|PDB:3IVZ}.
HELIX 152 160 {ECO:0000244|PDB:3IVZ}.
STRAND 164 170 {ECO:0000244|PDB:3IVZ}.
HELIX 177 188 {ECO:0000244|PDB:3IVZ}.
STRAND 191 196 {ECO:0000244|PDB:3IVZ}.
STRAND 199 201 {ECO:0000244|PDB:3IVZ}.
STRAND 211 213 {ECO:0000244|PDB:3IVZ}.
STRAND 219 222 {ECO:0000244|PDB:3IVZ}.
STRAND 229 234 {ECO:0000244|PDB:3IVZ}.
HELIX 237 241 {ECO:0000244|PDB:3IVZ}.
STRAND 244 246 {ECO:0000244|PDB:3IVZ}.
HELIX 251 254 {ECO:0000244|PDB:3IVZ}.
HELIX 257 259 {ECO:0000244|PDB:3IVZ}.
SEQUENCE 262 AA; 29798 MW; C2EFA86AACF51D4F CRC64;
MVKVAYVQMN PQILEPDKNY SKAEKLIKEA SKQGAQLVVL PELFDTGYNF ETREEVFEIA
QKIPEGETTT FLMDVARDTG VYIVAGTAEK DGDVLYNSAV VVGPRGFIGK YRKIHLFYRE
KFFFEPGDLG FRVFDLGFMK VGVMICFDWF FPESARTLAL KGADVIAHPA NLVMPYAPRA
MPIRALENKV YTVTADRVGE ERGLKFIGKS LIASPKAEVL SMASETEEEV GVAEIDLYLV
RNKRINDLND IFKDRREEYY FR


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