ID   NHAB_RHOSO              Reviewed;         235 AA.
AC   Q53117;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Nitrile hydratase subunit beta;
DE            Short=NHase;
DE            Short=Nitrilase;
DE            EC=4.2.1.84;
GN   Name=nthB;
OS   Rhodococcus sp.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1938876; DOI=10.1128/jb.173.21.6694-6704.1991;
RA   Mayaux J.-F., Cerbelaud E., Soubrier F., Yeh P., Blanche F., Petre D.;
RT   "Purification, cloning, and primary structure of a new enantiomer-selective
RT   amidase from a Rhodococcus strain: structural evidence for a conserved
RT   genetic coupling with nitrile hydratase.";
RL   J. Bacteriol. 173:6694-6704(1991).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M74531; AAA26184.1; -; Genomic_DNA.
DR   PIR; B41326; B41326.
DR   AlphaFoldDB; Q53117; -.
DR   SMR; Q53117; -.
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   Lyase.
FT   CHAIN           1..235
FT                   /note="Nitrile hydratase subunit beta"
FT                   /id="PRO_0000186834"
SQ   SEQUENCE   235 AA;  26078 MW;  DA3FCA0AE485C177 CRC64;
     MNGVFDLGGT DGIGPVDPPA EEPVFRADWE KAAFTMFSAL FRAGWFGIDE FRHGVEKMDP
     ALYLKSPYYK HWIASFEYHG KRTGKLDLAE LDRRTQYYLA NPDAPLPEHG PNQELIDFAN
     AVVPSGAPAI RPTDKEPRFK IGDVVRMSSD VPFGHTRIAG YVRGKVGRVI SHHGSFVYPD
     SAGNGRGDDP QHLYTLQFDA TELWGEQYAE PNVTTTFDAW DPYLTLVTAP EGAAA