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Nitrile hydratase subunit alpha (NHase) (Nitrilase) (EC 4.2.1.84)

 NHAA_RHOER              Reviewed;         207 AA.
P13448;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 122.
RecName: Full=Nitrile hydratase subunit alpha;
Short=NHase;
Short=Nitrilase;
EC=4.2.1.84;
Name=nthA;
Rhodococcus erythropolis (Arthrobacter picolinophilus).
Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
Rhodococcus.
NCBI_TaxID=1833;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=N-774;
PubMed=2659343; DOI=10.1111/j.1432-1033.1989.tb14761.x;
Ikehata O., Nishiyama M., Horinouchi S., Beppu T.;
"Primary structure of nitrile hydratase deduced from the nucleotide
sequence of a Rhodococcus species and its expression in Escherichia
coli.";
Eur. J. Biochem. 181:563-570(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=N-774;
PubMed=2001397; DOI=10.1016/0167-4781(91)90058-T;
Hashimoto Y., Nishiyama M., Ikehata O., Horinouchi S., Beppu T.;
"Cloning and characterization of an amidase gene from Rhodococcus
species N-774 and its expression in Escherichia coli.";
Biochim. Biophys. Acta 1088:225-233(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ACV2;
Bigey F., Chebrou H., Arnaud A., Galzy P.;
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=N-771;
PubMed=10101282; DOI=10.1093/oxfordjournals.jbchem.a022339;
Nojiri M., Yohda M., Odaka M., Matsushita Y., Tsujimura M.,
Yoshida T., Dohmae N., Takio K., Endo I.;
"Functional expression of nitrile hydratase in Escherichia coli:
requirement of a nitrile hydratase activator and post-translational
modification of a ligand cysteine.";
J. Biochem. 125:696-704(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
STRAIN=Brevibacterium sp. R312;
PubMed=2254253; DOI=10.1128/jb.172.12.6764-6773.1990;
Mayaux J.-F., Cerbelaud E., Soubrier F., Faucher D., Petre D.;
"Purification, cloning, and primary structure of an enantiomer-
selective amidase from Brevibacterium sp. strain R312: structural
evidence for genetic coupling with nitrile hydratase.";
J. Bacteriol. 172:6764-6773(1990).
[6]
PROTEIN SEQUENCE OF 2-20.
STRAIN=N-774;
PubMed=2920826; DOI=10.1016/0014-5793(89)81218-9;
Endo T., Watanabe I.;
"Nitrile hydratase of Rhodococcus sp. N-774. Purification and amino
acid sequences.";
FEBS Lett. 243:61-64(1989).
[7]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
STRAIN=Brevibacterium sp. R312;
PubMed=9195885; DOI=10.1016/S0969-2126(97)00223-2;
Huang W., Jia J., Cummings J., Nelson M., Schneider G., Lindqvist Y.;
"Crystal structure of nitrile hydratase reveals a novel iron centre in
a novel fold.";
Structure 5:691-699(1997).
[8]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), IDENTIFICATION BY MASS
SPECTROMETRY, OXIDATION AT CYS-113 AND CYS-115, AND LIGAND-BINDING.
PubMed=9586994; DOI=10.1038/nsb0598-347;
Nagashima S., Nakasako M., Dohmae N., Tsujimura M., Takio K.,
Odaka M., Yohda M., Kamiya N., Endo I.;
"Novel non-heme iron center of nitrile hydratase with a claw setting
of oxygen atoms.";
Nat. Struct. Biol. 5:347-351(1998).
[9]
EPR SPECTROSCOPY OF 106-129, IDENTIFICATION BY MASS SPECTROMETRY, AND
OXIDATION AT CYS-113.
STRAIN=N-771;
PubMed=9368004; DOI=10.1074/jbc.272.47.29454;
Tsujimura M., Dohmae N., Odaka M., Chijimatsu M., Takio K., Yohda M.,
Hoshino M., Nagashima S., Endo I.;
"Structure of the photoreactive iron center of the nitrile hydratase
from Rhodococcus sp. N-771. Evidence of a novel post-translational
modification in the cysteine ligand.";
J. Biol. Chem. 272:29454-29459(1997).
-!- FUNCTION: NHase catalyzes the hydration of various nitrile
compounds to the corresponding amides. Industrial production of
acrylamide is now being developed using some of the enzymes of
this class.
-!- 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;
-!- COFACTOR:
Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
Note=Binds 1 Fe(3+) ion per subunit.;
-!- ACTIVITY REGULATION: Inactivated by nitrosylation of the iron
center in the dark and activated by photo-induced nitric oxide
(NO) release. Inactivated by oxidation of Cys-115 to a sulfenic
acid.
-!- SUBUNIT: Heterodimer of an alpha and a beta chain.
-!- PTM: Oxidation on Cys-113 is essential for the activity.
{ECO:0000269|PubMed:9368004, ECO:0000269|PubMed:9586994}.
-!- PTM: Oxidation on Cys-115 stabilizes the Fe-NO ligand coordinated
in the inactive form. {ECO:0000269|PubMed:9586994}.
-!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X14668; CAA32797.1; -; Genomic_DNA.
EMBL; X54074; CAA38010.1; -; Genomic_DNA.
EMBL; Z48769; CAA88685.1; -; Genomic_DNA.
EMBL; AB016078; BAA36597.1; -; Genomic_DNA.
EMBL; M60264; AAA62722.1; -; Genomic_DNA.
PIR; B37806; B37806.
PDB; 1AHJ; X-ray; 2.65 A; A/C/E/G=1-207.
PDB; 2AHJ; X-ray; 1.70 A; A/C=2-207.
PDB; 2CYZ; X-ray; 1.55 A; A=2-207.
PDB; 2CZ0; X-ray; 1.50 A; A=2-207.
PDB; 2CZ1; X-ray; 1.39 A; A=2-207.
PDB; 2CZ6; X-ray; 1.50 A; A=2-207.
PDB; 2CZ7; X-ray; 1.80 A; A=2-207.
PDB; 2D0Q; X-ray; 1.65 A; A=2-207.
PDB; 2QDY; X-ray; 1.30 A; A=1-207.
PDB; 2ZCF; X-ray; 1.43 A; A=2-207.
PDB; 2ZPB; X-ray; 1.30 A; A=2-207.
PDB; 2ZPE; X-ray; 1.48 A; A=2-207.
PDB; 2ZPF; X-ray; 1.48 A; A=2-207.
PDB; 2ZPG; X-ray; 1.39 A; A=2-207.
PDB; 2ZPH; X-ray; 1.59 A; A=2-207.
PDB; 2ZPI; X-ray; 1.49 A; A=2-207.
PDB; 3A8G; X-ray; 1.11 A; A=1-207.
PDB; 3A8H; X-ray; 1.66 A; A=1-207.
PDB; 3A8L; X-ray; 1.63 A; A=1-207.
PDB; 3A8M; X-ray; 1.32 A; A=1-207.
PDB; 3A8O; X-ray; 1.47 A; A=1-207.
PDB; 3WVD; X-ray; 1.18 A; A=1-207.
PDB; 3WVE; X-ray; 1.57 A; A=1-207.
PDB; 3X20; X-ray; 1.18 A; A=1-207.
PDB; 3X24; X-ray; 1.24 A; A=1-207.
PDB; 3X25; X-ray; 1.20 A; A=1-207.
PDB; 3X26; X-ray; 1.34 A; A=1-207.
PDB; 3X28; X-ray; 1.65 A; A=1-207.
PDBsum; 1AHJ; -.
PDBsum; 2AHJ; -.
PDBsum; 2CYZ; -.
PDBsum; 2CZ0; -.
PDBsum; 2CZ1; -.
PDBsum; 2CZ6; -.
PDBsum; 2CZ7; -.
PDBsum; 2D0Q; -.
PDBsum; 2QDY; -.
PDBsum; 2ZCF; -.
PDBsum; 2ZPB; -.
PDBsum; 2ZPE; -.
PDBsum; 2ZPF; -.
PDBsum; 2ZPG; -.
PDBsum; 2ZPH; -.
PDBsum; 2ZPI; -.
PDBsum; 3A8G; -.
PDBsum; 3A8H; -.
PDBsum; 3A8L; -.
PDBsum; 3A8M; -.
PDBsum; 3A8O; -.
PDBsum; 3WVD; -.
PDBsum; 3WVE; -.
PDBsum; 3X20; -.
PDBsum; 3X24; -.
PDBsum; 3X25; -.
PDBsum; 3X26; -.
PDBsum; 3X28; -.
ProteinModelPortal; P13448; -.
SMR; P13448; -.
DIP; DIP-6075N; -.
IntAct; P13448; 1.
eggNOG; ENOG4105EKJ; Bacteria.
eggNOG; ENOG410XR8T; LUCA.
SABIO-RK; P13448; -.
EvolutionaryTrace; P13448; -.
GO; GO:0080109; F:indole-3-acetonitrile nitrile hydratase activity; IEA:UniProtKB-EC.
GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
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; Direct protein sequencing; Iron; Lyase; Metal-binding;
Oxidation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2920826}.
CHAIN 2 207 Nitrile hydratase subunit alpha.
/FTId=PRO_0000186823.
METAL 110 110 Iron.
METAL 113 113 Iron.
METAL 114 114 Iron.
METAL 115 115 Iron.
MOD_RES 113 113 Cysteine sulfinic acid (-SO2H).
{ECO:0000269|PubMed:9368004,
ECO:0000269|PubMed:9586994}.
MOD_RES 115 115 Cysteine sulfenic acid (-SOH).
{ECO:0000269|PubMed:9586994}.
CONFLICT 18 18 P -> A (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 20 20 S -> T (in Ref. 6; AA sequence).
{ECO:0000305}.
HELIX 19 31 {ECO:0000244|PDB:3A8G}.
TURN 32 34 {ECO:0000244|PDB:3A8G}.
HELIX 40 50 {ECO:0000244|PDB:3A8G}.
HELIX 54 66 {ECO:0000244|PDB:3A8G}.
HELIX 68 76 {ECO:0000244|PDB:3A8G}.
HELIX 78 84 {ECO:0000244|PDB:3A8G}.
STRAND 92 99 {ECO:0000244|PDB:3A8G}.
STRAND 104 109 {ECO:0000244|PDB:3A8G}.
HELIX 118 121 {ECO:0000244|PDB:3A8G}.
HELIX 126 129 {ECO:0000244|PDB:3A8G}.
HELIX 131 136 {ECO:0000244|PDB:3A8G}.
TURN 137 139 {ECO:0000244|PDB:3A8G}.
HELIX 141 148 {ECO:0000244|PDB:3A8G}.
STRAND 156 162 {ECO:0000244|PDB:3A8G}.
STRAND 165 172 {ECO:0000244|PDB:3A8G}.
HELIX 184 190 {ECO:0000244|PDB:3A8G}.
HELIX 193 197 {ECO:0000244|PDB:3A8G}.
STRAND 198 200 {ECO:0000244|PDB:3A8G}.
SEQUENCE 207 AA; 22996 MW; 22DD21260A2D70E5 CRC64;
MSVTIDHTTE NAAPAQAPVS DRAWALFRAL DGKGLVPDGY VEGWKKTFEE DFSPRRGAEL
VARAWTDPEF RQLLLTDGTA AVAQYGYLGP QGEYIVAVED TPTLKNVIVC SLCSCTAWPI
LGLPPTWYKS FEYRARVVRE PRKVLSEMGT EIASDIEIRV YDTTAETRYM VLPQRPAGTE
GWSQEQLQEI VTKDCLIGVA IPQVPTV


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