ID   NHAA_RHOSO              Reviewed;         199 AA.
AC   Q53118;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Nitrile hydratase subunit alpha;
DE            Short=NHase;
DE            Short=Nitrilase;
DE            EC=4.2.1.84;
GN   Name=nthA;
OS   Rhodococcus sp.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1938876; DOI=10.1128/jb.173.21.6694-6704.1991;
RA   Mayaux J.-F., Cerbelaud E., Soubrier F., Yeh P., Blanche F., Petre D.;
RT   "Purification, cloning, and primary structure of a new enantiomer-selective
RT   amidase from a Rhodococcus strain: structural evidence for a conserved
RT   genetic coupling with nitrile hydratase.";
RL   J. Bacteriol. 173:6694-6704(1991).
CC   -!- FUNCTION: NHase catalyzes the hydration of various nitrile compounds to
CC       the corresponding amides. Industrial production of acrylamide is now
CC       being developed using some of the enzymes of this class.
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   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC       Note=Binds 1 Fe(3+) ion per subunit.;
CC   -!- ACTIVITY REGULATION: Inactivated by oxidation of Cys-107 to a sulfenic
CC       acid.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC   -!- PTM: Oxidation on Cys-105 is essential for the activity. {ECO:0000250}.
CC   -!- PTM: Oxidation on Cys-107 stabilizes the Fe-NO ligand coordinated in
CC       the inactive form. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
CC       {ECO:0000305}.
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DR   EMBL; M74531; AAA26185.1; -; Genomic_DNA.
DR   PIR; C41326; C41326.
DR   AlphaFoldDB; Q53118; -.
DR   SMR; Q53118; -.
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; -; 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   Pfam; PF02979; NHase_alpha; 1.
DR   PIRSF; PIRSF001426; NHase_alpha; 1.
DR   SUPFAM; SSF56209; SSF56209; 1.
DR   TIGRFAMs; TIGR01323; nitrile_alph; 1.
PE   3: Inferred from homology;
KW   Iron; Lyase; Metal-binding; Oxidation.
FT   CHAIN           1..199
FT                   /note="Nitrile hydratase subunit alpha"
FT                   /id="PRO_0000186826"
FT   BINDING         102
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         105
FT                   /note="Cysteine sulfinic acid (-SO2H)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         107
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   199 AA;  22490 MW;  2A284C71CDC88DAD CRC64;
     MNNIIPTQEE IAARVKALES ILIEQNVIST AMVDRMVEIY EEEVGPKLGA KVVAKAWTDS
     EFKARLLDDA TEACKELGIS GLQGEDMVVL EDTDDVHHAI VCTLCSCYPW PVLGLPPNWY
     KEPAYRARIV REPRTVLSEE FNYHLPESTE IRIWDTSSEM RYWVLPQRPE GTEGWSEEQL
     AELVTRDSMI GVGPVKTPA