ID   NHAA_PSECL              Reviewed;         200 AA.
AC   P27764;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Nitrile hydratase subunit alpha;
DE            Short=NHase;
DE            Short=Nitrilase;
DE            EC=4.2.1.84;
GN   Name=nthA;
OS   Pseudomonas chlororaphis (Pseudomonas aureofaciens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26 AND
RP   164-178.
RC   STRAIN=B23;
RX   PubMed=2013568; DOI=10.1128/jb.173.8.2465-2472.1991;
RA   Nishiyama M., Horinouchi S., Kobayashi M., Nagasawa T., Yamada H.,
RA   Beppu T.;
RT   "Cloning and characterization of genes responsible for metabolism of
RT   nitrile compounds from Pseudomonas chlororaphis B23.";
RL   J. Bacteriol. 173:2465-2472(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-110 to a sulfenic
CC       acid.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC   -!- PTM: Oxidation on Cys-108 is essential for the activity. {ECO:0000250}.
CC   -!- PTM: Oxidation on Cys-110 stabilizes the Fe-NO ligand coordinated in
CC       the inactive form.
CC   -!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
CC       {ECO:0000305}.
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DR   EMBL; D90216; BAA14245.1; -; Genomic_DNA.
DR   PIR; A42725; A42725.
DR   AlphaFoldDB; P27764; -.
DR   SMR; P27764; -.
DR   BioCyc; MetaCyc:MON-15567; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Lyase; Metal-binding; Oxidation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2013568"
FT   CHAIN           2..200
FT                   /note="Nitrile hydratase subunit alpha"
FT                   /id="PRO_0000186820"
FT   BINDING         105
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         108
FT                   /note="Cysteine sulfinic acid (-SO2H)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         110
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   200 AA;  22117 MW;  12A80064CFCB0EFE CRC64;
     MSTSISTTAT PSTPGERAWA LFQVLKSKEL IPEGYVEQLT QLMAHDWSPE NGARVVAKAW
     VDPQFRALLL KDGTAACAQF GYTGPQGEYI VALEDTPGVK NVIVCSLCSC TNWPVLGLPP
     EWYKGFEFRA RLVREGRTVL RELGTELPSD TVIKVWDTSA ESRYLVLPQR PEGSEHMSEE
     QLQQLVTKDV LIGVALPRVG