NHAA_PSETH
ID NHAA_PSETH Reviewed; 204 AA.
AC Q7SID2;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cobalt-containing nitrile hydratase subunit alpha;
DE Short=L-NHase;
DE Short=L-nitrilase;
DE EC=4.2.1.84;
OS Pseudonocardia thermophila.
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Pseudonocardia.
OX NCBI_TaxID=1848 {ECO:0000312|PDB:1IRE};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, CATALYTIC
RP ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC 19285 / DSM 43832 / JCM 3095 / CBS 277.66 / NBRC 15559 / NCIMB
RC 10079 / NRRL B-1978;
RA Yamaki T., Oikawa T., Ito K., Nakamura T.;
RT "Cloning and sequencing of a nitrile hydratase gene from Pseudonocardia
RT thermophila JCM3095.";
RL J. Ferment. Bioeng. 83:474-477(1997).
RN [2] {ECO:0000312|PDB:1IRE}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH COBALT, OXIDATION AT
RP CYS-111 AND CYS-113, AND COFACTOR.
RC STRAIN=ATCC 19285 / DSM 43832 / JCM 3095 / CBS 277.66 / NBRC 15559 / NCIMB
RC 10079 / NRRL B-1978;
RX PubMed=11700034; DOI=10.1006/bbrc.2001.5897;
RA Miyanaga A., Fushinobu S., Ito K., Wakagi T.;
RT "Crystal structure of cobalt-containing nitrile hydratase.";
RL Biochem. Biophys. Res. Commun. 288:1169-1174(2001).
CC -!- FUNCTION: NHase catalyzes the hydration of various nitrile compounds to
CC the corresponding amides. {ECO:0000305}.
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:0000269|Ref.1, ECO:0000305};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:11700034, ECO:0000269|Ref.1};
CC Note=Binds 1 Co(2+) ion per heterodimer. {ECO:0000269|PubMed:11700034,
CC ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.;
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000269|PubMed:11700034}.
CC -!- INTERACTION:
CC Q7SID2; Q7SID3; NbExp=5; IntAct=EBI-1032292, EBI-1032285;
CC -!- BIOTECHNOLOGY: Industrial production of acrylamide is now being
CC developed using some of these enzymes. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
CC {ECO:0000305}.
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DR PDB; 1IRE; X-ray; 1.80 A; A=1-204.
DR PDB; 1UGP; X-ray; 1.63 A; A=2-204.
DR PDB; 1UGQ; X-ray; 2.00 A; A=2-204.
DR PDB; 1UGR; X-ray; 1.80 A; A=2-204.
DR PDB; 1UGS; X-ray; 2.00 A; A=2-204.
DR PDB; 3VYH; X-ray; 1.63 A; A=1-204.
DR PDB; 4OB0; X-ray; 1.20 A; A=1-204.
DR PDB; 4OB1; X-ray; 1.63 A; A=1-204.
DR PDB; 4OB2; X-ray; 1.52 A; A=2-204.
DR PDB; 4OB3; X-ray; 1.92 A; A=1-204.
DR PDB; 7SJZ; X-ray; 1.85 A; A=1-204.
DR PDBsum; 1IRE; -.
DR PDBsum; 1UGP; -.
DR PDBsum; 1UGQ; -.
DR PDBsum; 1UGR; -.
DR PDBsum; 1UGS; -.
DR PDBsum; 3VYH; -.
DR PDBsum; 4OB0; -.
DR PDBsum; 4OB1; -.
DR PDBsum; 4OB2; -.
DR PDBsum; 4OB3; -.
DR PDBsum; 7SJZ; -.
DR AlphaFoldDB; Q7SID2; -.
DR SMR; Q7SID2; -.
DR IntAct; Q7SID2; 1.
DR STRING; 1848.SAMN05443637_10361; -.
DR BRENDA; 4.2.1.84; 5208.
DR EvolutionaryTrace; Q7SID2; -.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0080109; F:indole-3-acetonitrile nitrile hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0018822; F:nitrile hydratase activity; IDA:UniProtKB.
DR GO; GO:0050899; P:nitrile catabolic process; IDA:UniProtKB.
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 3D-structure; Cobalt; Direct protein sequencing; Lyase; Metal-binding;
KW Oxidation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..204
FT /note="Cobalt-containing nitrile hydratase subunit alpha"
FT /id="PRO_0000186822"
FT BINDING 108
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:11700034"
FT BINDING 111
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:11700034"
FT BINDING 112
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:11700034"
FT BINDING 113
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:11700034"
FT MOD_RES 111
FT /note="Cysteine sulfinic acid (-SO2H)"
FT /evidence="ECO:0000269|PubMed:11700034"
FT MOD_RES 113
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000269|PubMed:11700034"
FT CONFLICT 111
FT /note="C -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 10..30
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:4OB0"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:4OB0"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:4OB0"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:4OB0"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1IRE"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:4OB0"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:4OB0"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:4OB0"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:1UGR"
SQ SEQUENCE 204 AA; 23145 MW; BE390BBB7AEDD1BB CRC64;
MTENILRKSD EEIQKEITAR VKALESMLIE QGILTTSMID RMAEIYENEV GPHLGAKVVV
KAWTDPEFKK RLLADGTEAC KELGIGGLQG EDMMWVENTD EVHHVVVCTL CSCYPWPVLG
LPPNWFKEPQ YRSRVVREPR QLLKEEFGFE VPPSKEIKVW DSSSEMRFVV LPQRPAGTDG
WSEEELATLV TRESMIGVEP AKAV
