ID Q2UZQ5_9NOCA Unreviewed; 203 AA.
AC Q2UZQ5;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 13-SEP-2023, entry version 58.
DE RecName: Full=nitrile hydratase {ECO:0000256|ARBA:ARBA00013079};
DE EC=4.2.1.84 {ECO:0000256|ARBA:ARBA00013079};
GN Name=nhha {ECO:0000313|EMBL:CAE46768.2};
OS Rhodococcus pyridinivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=103816 {ECO:0000313|EMBL:CAE46768.2};
RN [1] {ECO:0000313|EMBL:CAE46768.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MW3 {ECO:0000313|EMBL:CAE46768.2};
RA Precigou S., Wieser M., Pommares P., Goulas P., Duran R.;
RT "A novel Rhodococcus pyridinovorans with high nitrile hydratase activity.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAE75933.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S85-2 {ECO:0000313|EMBL:BAE75933.1};
RX PubMed=16402166; DOI=10.1007/s00253-005-0298-x;
RA Kohyama E., Yoshimura A., Aoshima D., Yoshida T., Kawamoto H., Nagasawa T.;
RT "Convenient treatment of acetonitrile-containing wastes using the tandem
RT combination of nitrile hydratase and amidase-producing microorganisms.";
RL Appl. Microbiol. Biotechnol. 72:600-606(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amide = a nitrile + H2O; Xref=Rhea:RHEA:12673,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18379, ChEBI:CHEBI:65285; EC=4.2.1.84;
CC Evidence={ECO:0000256|ARBA:ARBA00001410};
CC -!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
CC {ECO:0000256|ARBA:ARBA00009363}.
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DR EMBL; AB211984; BAE75933.1; -; Genomic_DNA.
DR EMBL; AJ582605; CAE46768.2; -; Genomic_DNA.
DR AlphaFoldDB; Q2UZQ5; -.
DR SMR; Q2UZQ5; -.
DR BRENDA; 4.2.1.84; 7679.
DR GO; GO:0080109; F:indole-3-acetonitrile nitrile hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.90.330.10; Nitrile hydratase alpha /Thiocyanate hydrolase gamma; 1.
DR InterPro; IPR036648; CN_Hdrase_a/SCN_Hdrase_g_sf.
DR InterPro; IPR004232; CN_Hdrtase_a/SCN_Hdrlase_g.
DR InterPro; IPR023900; CN_Hdrtase_asu/SCN_Hdrlase_gsu.
DR InterPro; IPR018141; Nitrile_hydratase_asu.
DR NCBIfam; TIGR01323; nitrile_alph; 1.
DR Pfam; PF02979; NHase_alpha; 1.
DR PIRSF; PIRSF001426; NHase_alpha; 1.
DR SUPFAM; SSF56209; Nitrile hydratase alpha chain; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|PIRSR:PIRSR001426-1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CAE46768.2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001426-1}.
FT DOMAIN 10..192
FT /note="Nitrile hydratase alpha /Thiocyanate hydrolase
FT gamma"
FT /evidence="ECO:0000259|Pfam:PF02979"
FT BINDING 102
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|PIRSR:PIRSR001426-1"
FT BINDING 105
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|PIRSR:PIRSR001426-1"
FT BINDING 106
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|PIRSR:PIRSR001426-1"
FT BINDING 107
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|PIRSR:PIRSR001426-1"
SQ SEQUENCE 203 AA; 22835 MW; 515ED2A4863E6C98 CRC64;
MSEHVNKYTE YEARTKAIET LLYERGLITP AAVDRVVSYY ENEIGPMGGA KVVAKSWVDP
EYRKWLEEDA TAAMASLGYA GEQAHQISAV FNDSQTHHVV VCTLCSCYPW PVLGLPPAWY
KSMEYRSRVV ADPRGVLKRD FGFDIPDEVE VRVWDSSSEI RYIVIPERPA GTDGWSEEEL
TKLVSRDSMI GVSNALTPQE VIV
//
