ID   NHA2_RHORH              Reviewed;         207 AA.
AC   P29378;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Low-molecular weight cobalt-containing nitrile hydratase subunit alpha;
DE            Short=L-NHase;
DE            Short=L-nitrilase;
DE            EC=4.2.1.84;
OS   Rhodococcus rhodochrous.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=J1;
RX   PubMed=1840499; DOI=10.1016/0167-4781(91)90208-4;
RA   Kobayashi M., Nishiyama M., Nagasawa T., Horinouchi S., Beppu T.,
RA   Yamada H.;
RT   "Cloning, nucleotide sequence and expression in Escherichia coli of two
RT   cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous
RT   J1.";
RL   Biochim. Biophys. Acta 1129:23-33(1991).
CC   -!- FUNCTION: NHase catalyzes the hydration of various nitrile compounds to
CC       the corresponding amides.
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   -!- INTERACTION:
CC       P29378; P96453: nhlE; NbExp=2; IntAct=EBI-15729943, EBI-15729982;
CC       P29378; P29379; NbExp=2; IntAct=EBI-15729943, EBI-15729954;
CC   -!- INDUCTION: By cobalt and urea or cyclohexanecarboxamide.
CC   -!- BIOTECHNOLOGY: Industrial production of acrylamide is now being
CC       developed using some of these enzymes.
CC   -!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
CC       {ECO:0000305}.
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DR   EMBL; X64360; CAA45712.1; -; Genomic_DNA.
DR   PIR; S19716; S19716.
DR   AlphaFoldDB; P29378; -.
DR   SMR; P29378; -.
DR   DIP; DIP-46299N; -.
DR   IntAct; P29378; 2.
DR   BRENDA; 4.2.1.84; 5395.
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   Cobalt; Direct protein sequencing; Lyase; Metal-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..207
FT                   /note="Low-molecular weight cobalt-containing nitrile
FT                   hydratase subunit alpha"
FT                   /id="PRO_0000186825"
FT   BINDING         109
FT                   /ligand="Co(3+)"
FT                   /ligand_id="ChEBI:CHEBI:49415"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Co(3+)"
FT                   /ligand_id="ChEBI:CHEBI:49415"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Co(3+)"
FT                   /ligand_id="ChEBI:CHEBI:49415"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="Co(3+)"
FT                   /ligand_id="ChEBI:CHEBI:49415"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   207 AA;  22848 MW;  B8E2BBFFF15B3D95 CRC64;
     MTAHNPVQGT LPRSNEEIAA RVKAMEAILV DKGLISTDAI DHMSSVYENE VGPQLGAKIV
     ARAWVDPEFK QRLLTDATSA CREMGVGGMQ GEEMVVLENT GTVHNMVVCT LCSCYPWPVL
     GLPPNWYKYP AYRARAVRDP RGVLAEFGYT PDPDVEIRIW DSSAELRYWV LPQRPAGTEN
     FTEEQLADLV TRDSLIGVSV PTTPSKA