NHAB_RHOER
ID NHAB_RHOER Reviewed; 212 AA.
AC P13449; Q59789;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Nitrile hydratase subunit beta;
DE Short=NHase;
DE Short=Nitrilase;
DE EC=4.2.1.84;
GN Name=nthB; Synonyms=nha2;
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 PROTEIN SEQUENCE OF 1-19.
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 [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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).
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 -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC -!- BIOTECHNOLOGY: Industrial production of acrylamide is now being
CC developed using some of these enzymes.
CC -!- SIMILARITY: Belongs to the nitrile hydratase subunit beta family.
CC {ECO:0000305}.
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DR EMBL; X54074; CAA38011.1; -; Genomic_DNA.
DR EMBL; X14668; CAA32798.1; -; Genomic_DNA.
DR EMBL; Z48769; CAA88686.1; -; Genomic_DNA.
DR EMBL; AB016078; BAA36598.1; -; Genomic_DNA.
DR PDB; 1AHJ; X-ray; 2.65 A; B/D/F/H=1-212.
DR PDB; 2AHJ; X-ray; 1.70 A; B/D=1-212.
DR PDB; 2CYZ; X-ray; 1.55 A; B=1-212.
DR PDB; 2CZ0; X-ray; 1.50 A; B=1-212.
DR PDB; 2CZ1; X-ray; 1.39 A; B=1-212.
DR PDB; 2CZ6; X-ray; 1.50 A; B=1-212.
DR PDB; 2CZ7; X-ray; 1.80 A; B=1-212.
DR PDB; 2D0Q; X-ray; 1.65 A; B=1-212.
DR PDB; 2QDY; X-ray; 1.30 A; B=1-212.
DR PDB; 2ZCF; X-ray; 1.43 A; B=1-212.
DR PDB; 2ZPB; X-ray; 1.30 A; B=1-212.
DR PDB; 2ZPE; X-ray; 1.48 A; B=1-212.
DR PDB; 2ZPF; X-ray; 1.48 A; B=1-212.
DR PDB; 2ZPG; X-ray; 1.39 A; B=1-212.
DR PDB; 2ZPH; X-ray; 1.59 A; B=1-212.
DR PDB; 2ZPI; X-ray; 1.49 A; B=1-212.
DR PDB; 3A8G; X-ray; 1.11 A; B=1-212.
DR PDB; 3A8H; X-ray; 1.66 A; B=1-212.
DR PDB; 3A8L; X-ray; 1.63 A; B=1-212.
DR PDB; 3A8M; X-ray; 1.32 A; B=1-212.
DR PDB; 3A8O; X-ray; 1.47 A; B=1-212.
DR PDB; 3WVD; X-ray; 1.18 A; B=1-212.
DR PDB; 3WVE; X-ray; 1.57 A; B=1-212.
DR PDB; 3X20; X-ray; 1.18 A; B=1-212.
DR PDB; 3X24; X-ray; 1.24 A; B=1-212.
DR PDB; 3X25; X-ray; 1.20 A; B=1-212.
DR PDB; 3X26; X-ray; 1.34 A; B=1-212.
DR PDB; 3X28; X-ray; 1.65 A; B=1-212.
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; P13449; -.
DR SMR; P13449; -.
DR DIP; DIP-6076N; -.
DR IntAct; P13449; 1.
DR STRING; 1833.XU06_28850; -.
DR SABIO-RK; P13449; -.
DR EvolutionaryTrace; P13449; -.
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; 1.10.472.20; -; 1.
DR InterPro; IPR042262; CN_hydtase_beta_C.
DR InterPro; IPR024690; CN_hydtase_beta_dom.
DR InterPro; IPR008990; Elect_transpt_acc-like_dom_sf.
DR InterPro; IPR003168; Nitrile_hydratase_bsu.
DR Pfam; PF02211; NHase_beta; 1.
DR PIRSF; PIRSF001427; NHase_beta; 1.
DR SUPFAM; SSF50090; SSF50090; 1.
DR TIGRFAMs; TIGR03888; nitrile_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase.
FT CHAIN 1..212
FT /note="Nitrile hydratase subunit beta"
FT /id="PRO_0000186831"
FT VARIANT 40
FT /note="M -> V (in strain: ACV2)"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:3A8G"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3A8G"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3A8G"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3A8G"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:3A8G"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:3A8G"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3A8G"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3A8G"
SQ SEQUENCE 212 AA; 23487 MW; A0401CA4FC1C2CBE CRC64;
MDGVHDLAGV QGFGKVPHTV NADIGPTFHA EWEHLPYSLM FAGVAELGAF SVDEVRYVVE
RMEPRHYMMT PYYERYVIGV ATLMVEKGIL TQDELESLAG GPFPLSRPSE SEGRPAPVET
TTFEVGQRVR VRDEYVPGHI RMPAYCRGRV GTISHRTTEK WPFPDAIGHG RNDAGEEPTY
HVKFAAEELF GSDTDGGSVV VDLFEGYLEP AA
