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Cobalt-containing nitrile hydratase subunit alpha (L-NHase) (L-nitrilase) (EC 4.2.1.84)

 NHAA_PSETH              Reviewed;         204 AA.
Q7SID2;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 77.
RecName: Full=Cobalt-containing nitrile hydratase subunit alpha;
Short=L-NHase;
Short=L-nitrilase;
EC=4.2.1.84;
Pseudonocardia thermophila.
Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
Pseudonocardia.
NCBI_TaxID=1848 {ECO:0000312|PDB:1IRE};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, CATALYTIC
ACTIVITY, AND COFACTOR.
STRAIN=ATCC 19285 / CBS 277.66 / DSM 43832 / JCM 3095 / NCIMB 10079;
Yamaki T., Oikawa T., Ito K., Nakamura T.;
"Cloning and sequencing of a nitrile hydratase gene from
Pseudonocardia thermophila JCM3095.";
J. Ferment. Bioeng. 83:474-477(1997).
[2] {ECO:0000312|PDB:1IRE}
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND OXIDATION AT CYS-111 AND
CYS-113.
STRAIN=ATCC 19285 / CBS 277.66 / DSM 43832 / JCM 3095 / NCIMB 10079;
PubMed=11700034; DOI=10.1006/bbrc.2001.5897;
Miyanaga A., Fushinobu S., Ito K., Wakagi T.;
"Crystal structure of cobalt-containing nitrile hydratase.";
Biochem. Biophys. Res. Commun. 288:1169-1174(2001).
-!- FUNCTION: NHase catalyzes the hydration of various nitrile
compounds to the corresponding amides. {ECO:0000305}.
-!- CATALYTIC ACTIVITY:
Reaction=an aliphatic amide = a nitrile + H2O;
Xref=Rhea:RHEA:12673, ChEBI:CHEBI:15377, ChEBI:CHEBI:18379,
ChEBI:CHEBI:65285; EC=4.2.1.84; Evidence={ECO:0000269|Ref.1,
ECO:0000305};
-!- COFACTOR:
Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|Ref.1};
Note=Binds 1 Co(2+) ion per heterodimer. {ECO:0000269|Ref.1};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Temperature dependence:
Optimum temperature is 60 degrees Celsius.;
-!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
{ECO:0000269|PubMed:11700034}.
-!- INTERACTION:
Q7SID3:-; NbExp=5; IntAct=EBI-1032292, EBI-1032285;
-!- BIOTECHNOLOGY: Industrial production of acrylamide is now being
developed using some of these enzymes. {ECO:0000305}.
-!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
{ECO:0000305}.
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PDB; 1IRE; X-ray; 1.80 A; A=1-204.
PDB; 1UGP; X-ray; 1.63 A; A=2-204.
PDB; 1UGQ; X-ray; 2.00 A; A=2-204.
PDB; 1UGR; X-ray; 1.80 A; A=2-204.
PDB; 1UGS; X-ray; 2.00 A; A=2-204.
PDB; 3VYH; X-ray; 1.63 A; A=1-204.
PDB; 4OB0; X-ray; 1.20 A; A=1-204.
PDB; 4OB1; X-ray; 1.63 A; A=1-204.
PDB; 4OB2; X-ray; 1.52 A; A=2-204.
PDB; 4OB3; X-ray; 1.92 A; A=1-204.
PDBsum; 1IRE; -.
PDBsum; 1UGP; -.
PDBsum; 1UGQ; -.
PDBsum; 1UGR; -.
PDBsum; 1UGS; -.
PDBsum; 3VYH; -.
PDBsum; 4OB0; -.
PDBsum; 4OB1; -.
PDBsum; 4OB2; -.
PDBsum; 4OB3; -.
ProteinModelPortal; Q7SID2; -.
SMR; Q7SID2; -.
IntAct; Q7SID2; 1.
BRENDA; 4.2.1.84; 5208.
EvolutionaryTrace; Q7SID2; -.
GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
GO; GO:0080109; F:indole-3-acetonitrile nitrile hydratase activity; IEA:UniProtKB-EC.
GO; GO:0018822; F:nitrile hydratase activity; IDA:UniProtKB.
GO; GO:0050899; P:nitrile catabolic process; IDA:UniProtKB.
Gene3D; 3.90.330.10; -; 1.
InterPro; IPR036648; CN_Hdrase_a/SCN_Hdrase_g_sf.
InterPro; IPR004232; CN_Hdrtase_a/SCN_Hdrlase_g.
InterPro; IPR023900; CN_Hdrtase_asu/SCN_Hdrlase_gsu.
InterPro; IPR018141; Nitrile_hydratase_asu.
Pfam; PF02979; NHase_alpha; 1.
PIRSF; PIRSF001426; NHase_alpha; 1.
ProDom; PD007559; CN_Hdrtase_asu/SCN_Hdrlase_gsu; 1.
SUPFAM; SSF56209; SSF56209; 1.
TIGRFAMs; TIGR01323; nitrile_alph; 1.
1: Evidence at protein level;
3D-structure; Cobalt; Direct protein sequencing; Lyase; Metal-binding;
Oxidation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.1}.
CHAIN 2 204 Cobalt-containing nitrile hydratase
subunit alpha.
/FTId=PRO_0000186822.
METAL 108 108 Cobalt.
METAL 111 111 Cobalt. {ECO:0000269|PubMed:11700034}.
METAL 112 112 Cobalt. {ECO:0000269|PubMed:11700034}.
METAL 113 113 Cobalt.
MOD_RES 111 111 Cysteine sulfinic acid (-SO2H).
{ECO:0000269|PubMed:11700034}.
MOD_RES 113 113 Cysteine sulfenic acid (-SOH).
{ECO:0000269|PubMed:11700034}.
CONFLICT 111 111 C -> A (in Ref. 2). {ECO:0000305}.
HELIX 10 30 {ECO:0000244|PDB:4OB0}.
HELIX 36 48 {ECO:0000244|PDB:4OB0}.
HELIX 52 64 {ECO:0000244|PDB:4OB0}.
HELIX 66 74 {ECO:0000244|PDB:4OB0}.
HELIX 76 81 {ECO:0000244|PDB:4OB0}.
TURN 82 84 {ECO:0000244|PDB:4OB0}.
STRAND 91 97 {ECO:0000244|PDB:4OB0}.
STRAND 100 107 {ECO:0000244|PDB:4OB0}.
STRAND 109 111 {ECO:0000244|PDB:1IRE}.
HELIX 116 119 {ECO:0000244|PDB:4OB0}.
HELIX 124 127 {ECO:0000244|PDB:4OB0}.
HELIX 129 135 {ECO:0000244|PDB:4OB0}.
HELIX 139 147 {ECO:0000244|PDB:4OB0}.
STRAND 155 161 {ECO:0000244|PDB:4OB0}.
STRAND 164 171 {ECO:0000244|PDB:4OB0}.
HELIX 183 187 {ECO:0000244|PDB:4OB0}.
HELIX 192 196 {ECO:0000244|PDB:4OB0}.
STRAND 197 199 {ECO:0000244|PDB:1UGR}.
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


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