NHAA_RHOER
ID NHAA_RHOER Reviewed; 207 AA.
AC P13448;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Nitrile hydratase subunit alpha;
DE Short=NHase;
DE Short=Nitrilase;
DE EC=4.2.1.84;
GN Name=nthA;
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=N-774;
RX PubMed=2659343; DOI=10.1111/j.1432-1033.1989.tb14761.x;
RA Ikehata O., Nishiyama M., Horinouchi S., Beppu T.;
RT "Primary structure of nitrile hydratase deduced from the nucleotide
RT sequence of a Rhodococcus species and its expression in Escherichia coli.";
RL Eur. J. Biochem. 181:563-570(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=N-774;
RX PubMed=2001397; DOI=10.1016/0167-4781(91)90058-t;
RA Hashimoto Y., Nishiyama M., Ikehata O., Horinouchi S., Beppu T.;
RT "Cloning and characterization of an amidase gene from Rhodococcus species
RT N-774 and its expression in Escherichia coli.";
RL Biochim. Biophys. Acta 1088:225-233(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ACV2;
RA Bigey F., Chebrou H., Arnaud A., Galzy P.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=N-771;
RX PubMed=10101282; DOI=10.1093/oxfordjournals.jbchem.a022339;
RA Nojiri M., Yohda M., Odaka M., Matsushita Y., Tsujimura M., Yoshida T.,
RA Dohmae N., Takio K., Endo I.;
RT "Functional expression of nitrile hydratase in Escherichia coli:
RT requirement of a nitrile hydratase activator and post-translational
RT modification of a ligand cysteine.";
RL J. Biochem. 125:696-704(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
RC STRAIN=Brevibacterium sp. R312;
RX PubMed=2254253; DOI=10.1128/jb.172.12.6764-6773.1990;
RA Mayaux J.-F., Cerbelaud E., Soubrier F., Faucher D., Petre D.;
RT "Purification, cloning, and primary structure of an enantiomer-selective
RT amidase from Brevibacterium sp. strain R312: structural evidence for
RT genetic coupling with nitrile hydratase.";
RL J. Bacteriol. 172:6764-6773(1990).
RN [6]
RP PROTEIN SEQUENCE OF 2-20.
RC STRAIN=N-774;
RX PubMed=2920826; DOI=10.1016/0014-5793(89)81218-9;
RA Endo T., Watanabe I.;
RT "Nitrile hydratase of Rhodococcus sp. N-774. Purification and amino acid
RT sequences.";
RL FEBS Lett. 243:61-64(1989).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
RC STRAIN=Brevibacterium sp. R312;
RX PubMed=9195885; DOI=10.1016/s0969-2126(97)00223-2;
RA Huang W., Jia J., Cummings J., Nelson M., Schneider G., Lindqvist Y.;
RT "Crystal structure of nitrile hydratase reveals a novel iron centre in a
RT novel fold.";
RL Structure 5:691-699(1997).
RN [8] {ECO:0007744|PDB:2AHJ}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH IRON, COFACTOR,
RP IDENTIFICATION BY MASS SPECTROMETRY, OXIDATION AT CYS-113 AND CYS-115, AND
RP LIGAND-BINDING.
RX PubMed=9586994; DOI=10.1038/nsb0598-347;
RA Nagashima S., Nakasako M., Dohmae N., Tsujimura M., Takio K., Odaka M.,
RA Yohda M., Kamiya N., Endo I.;
RT "Novel non-heme iron center of nitrile hydratase with a claw setting of
RT oxygen atoms.";
RL Nat. Struct. Biol. 5:347-351(1998).
RN [9]
RP EPR SPECTROSCOPY OF 106-129, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP OXIDATION AT CYS-113.
RC STRAIN=N-771;
RX PubMed=9368004; DOI=10.1074/jbc.272.47.29454;
RA Tsujimura M., Dohmae N., Odaka M., Chijimatsu M., Takio K., Yohda M.,
RA Hoshino M., Nagashima S., Endo I.;
RT "Structure of the photoreactive iron center of the nitrile hydratase from
RT Rhodococcus sp. N-771. Evidence of a novel post-translational modification
RT in the cysteine ligand.";
RL J. Biol. Chem. 272:29454-29459(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=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:9586994};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:9586994};
CC -!- ACTIVITY REGULATION: Inactivated by nitrosylation of the iron center in
CC the dark and activated by photo-induced nitric oxide (NO) release.
CC Inactivated by oxidation of Cys-115 to a sulfenic acid.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- PTM: Oxidation on Cys-113 is essential for the activity.
CC {ECO:0000269|PubMed:9368004, ECO:0000269|PubMed:9586994}.
CC -!- PTM: Oxidation on Cys-115 stabilizes the Fe-NO ligand coordinated in
CC the inactive form. {ECO:0000269|PubMed:9586994}.
CC -!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; X14668; CAA32797.1; -; Genomic_DNA.
DR EMBL; X54074; CAA38010.1; -; Genomic_DNA.
DR EMBL; Z48769; CAA88685.1; -; Genomic_DNA.
DR EMBL; AB016078; BAA36597.1; -; Genomic_DNA.
DR EMBL; M60264; AAA62722.1; -; Genomic_DNA.
DR PIR; B37806; B37806.
DR PDB; 1AHJ; X-ray; 2.65 A; A/C/E/G=1-207.
DR PDB; 2AHJ; X-ray; 1.70 A; A/C=2-207.
DR PDB; 2CYZ; X-ray; 1.55 A; A=2-207.
DR PDB; 2CZ0; X-ray; 1.50 A; A=2-207.
DR PDB; 2CZ1; X-ray; 1.39 A; A=2-207.
DR PDB; 2CZ6; X-ray; 1.50 A; A=2-207.
DR PDB; 2CZ7; X-ray; 1.80 A; A=2-207.
DR PDB; 2D0Q; X-ray; 1.65 A; A=2-207.
DR PDB; 2QDY; X-ray; 1.30 A; A=1-207.
DR PDB; 2ZCF; X-ray; 1.43 A; A=2-207.
DR PDB; 2ZPB; X-ray; 1.30 A; A=2-207.
DR PDB; 2ZPE; X-ray; 1.48 A; A=2-207.
DR PDB; 2ZPF; X-ray; 1.48 A; A=2-207.
DR PDB; 2ZPG; X-ray; 1.39 A; A=2-207.
DR PDB; 2ZPH; X-ray; 1.59 A; A=2-207.
DR PDB; 2ZPI; X-ray; 1.49 A; A=2-207.
DR PDB; 3A8G; X-ray; 1.11 A; A=1-207.
DR PDB; 3A8H; X-ray; 1.66 A; A=1-207.
DR PDB; 3A8L; X-ray; 1.63 A; A=1-207.
DR PDB; 3A8M; X-ray; 1.32 A; A=1-207.
DR PDB; 3A8O; X-ray; 1.47 A; A=1-207.
DR PDB; 3WVD; X-ray; 1.18 A; A=1-207.
DR PDB; 3WVE; X-ray; 1.57 A; A=1-207.
DR PDB; 3X20; X-ray; 1.18 A; A=1-207.
DR PDB; 3X24; X-ray; 1.24 A; A=1-207.
DR PDB; 3X25; X-ray; 1.20 A; A=1-207.
DR PDB; 3X26; X-ray; 1.34 A; A=1-207.
DR PDB; 3X28; X-ray; 1.65 A; A=1-207.
DR PDBsum; 1AHJ; -.
DR PDBsum; 2AHJ; -.
DR PDBsum; 2CYZ; -.
DR PDBsum; 2CZ0; -.
DR PDBsum; 2CZ1; -.
DR PDBsum; 2CZ6; -.
DR PDBsum; 2CZ7; -.
DR PDBsum; 2D0Q; -.
DR PDBsum; 2QDY; -.
DR PDBsum; 2ZCF; -.
DR PDBsum; 2ZPB; -.
DR PDBsum; 2ZPE; -.
DR PDBsum; 2ZPF; -.
DR PDBsum; 2ZPG; -.
DR PDBsum; 2ZPH; -.
DR PDBsum; 2ZPI; -.
DR PDBsum; 3A8G; -.
DR PDBsum; 3A8H; -.
DR PDBsum; 3A8L; -.
DR PDBsum; 3A8M; -.
DR PDBsum; 3A8O; -.
DR PDBsum; 3WVD; -.
DR PDBsum; 3WVE; -.
DR PDBsum; 3X20; -.
DR PDBsum; 3X24; -.
DR PDBsum; 3X25; -.
DR PDBsum; 3X26; -.
DR PDBsum; 3X28; -.
DR AlphaFoldDB; P13448; -.
DR SMR; P13448; -.
DR DIP; DIP-6075N; -.
DR IntAct; P13448; 1.
DR STRING; 1833.XU06_28845; -.
DR BRENDA; 4.2.1.84; 5389.
DR SABIO-RK; P13448; -.
DR EvolutionaryTrace; P13448; -.
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 3D-structure; Direct protein sequencing; Iron; Lyase; Metal-binding;
KW Oxidation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2920826"
FT CHAIN 2..207
FT /note="Nitrile hydratase subunit alpha"
FT /id="PRO_0000186823"
FT BINDING 110
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:9586994,
FT ECO:0007744|PDB:2AHJ"
FT BINDING 113
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:9586994,
FT ECO:0007744|PDB:2AHJ"
FT BINDING 114
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:9586994,
FT ECO:0007744|PDB:2AHJ"
FT BINDING 115
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000269|PubMed:9586994,
FT ECO:0007744|PDB:2AHJ"
FT MOD_RES 113
FT /note="Cysteine sulfinic acid (-SO2H)"
FT /evidence="ECO:0000269|PubMed:9368004,
FT ECO:0000269|PubMed:9586994"
FT MOD_RES 115
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000269|PubMed:9586994"
FT CONFLICT 18
FT /note="P -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="S -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:3A8G"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:3A8G"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:3A8G"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:3A8G"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:3A8G"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:3A8G"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:3A8G"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3A8G"
SQ 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
