ID   NHAA_PSEPU              Reviewed;         210 AA.
AC   P97051;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Nitrile hydratase subunit alpha;
DE            Short=NHase;
DE            Short=Nitrilase;
DE            EC=4.2.1.84;
GN   Name=nthA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 18668;
RX   PubMed=9154927; DOI=10.1021/bi962794t;
RA   Payne M.S., Wu S., Fallon R.D., Tudor G., Stieglitz B., Turner I.M. Jr.,
RA   Nelson M.J.;
RT   "A stereoselective cobalt-containing nitrile hydratase.";
RL   Biochemistry 36:5447-5454(1997).
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=Co(3+); Xref=ChEBI:CHEBI:49415;
CC       Note=Binds 1 Co(3+) ion per subunit.;
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC   -!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U89363; AAC18418.1; -; Genomic_DNA.
DR   AlphaFoldDB; P97051; -.
DR   SMR; P97051; -.
DR   BRENDA; 4.2.1.84; 5092.
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   Cobalt; Lyase; Metal-binding.
FT   CHAIN           1..210
FT                   /note="Nitrile hydratase subunit alpha"
FT                   /id="PRO_0000186821"
FT   BINDING         112
FT                   /ligand="Co(3+)"
FT                   /ligand_id="ChEBI:CHEBI:49415"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Co(3+)"
FT                   /ligand_id="ChEBI:CHEBI:49415"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="Co(3+)"
FT                   /ligand_id="ChEBI:CHEBI:49415"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Co(3+)"
FT                   /ligand_id="ChEBI:CHEBI:49415"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  22982 MW;  48585F0EC0EA71D1 CRC64;
     MGQSHTHDHH HDGYQAPPED IALRVKALES LLIEKGLVDP AAMDLVVQTY EHKVGPRNGA
     KVVAKAWVDP AYKARLLADA TAAIAELGFS GVQGEDMVIL ENTPAVHNVF VCTLCSCYPW
     PTLGLPPAWY KAAAYRSRMV SDPRGVLAEF GLVIPANKEI RVWDTTAELR YMVLPERPGT
     EAYSEEQLAE LVTRDSMIGT GLPTQPTPSH