ID   NHB2_RHORH              Reviewed;         226 AA.
AC   P29379;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Low-molecular weight cobalt-containing nitrile hydratase subunit beta;
DE            Short=L-NHase;
DE            Short=L-nitrilase;
DE            EC=4.2.1.84;
OS   Rhodococcus rhodochrous.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=J1;
RX   PubMed=1840499; DOI=10.1016/0167-4781(91)90208-4;
RA   Kobayashi M., Nishiyama M., Nagasawa T., Horinouchi S., Beppu T.,
RA   Yamada H.;
RT   "Cloning, nucleotide sequence and expression in Escherichia coli of two
RT   cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous
RT   J1.";
RL   Biochim. Biophys. Acta 1129:23-33(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   -!- INTERACTION:
CC       P29379; P29378; NbExp=2; IntAct=EBI-15729954, EBI-15729943;
CC   -!- INDUCTION: By cobalt and urea or cyclohexanecarboxamide.
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; X64360; CAA45711.1; -; Genomic_DNA.
DR   PIR; S19715; S19715.
DR   AlphaFoldDB; P29379; -.
DR   SMR; P29379; -.
DR   DIP; DIP-46300N; -.
DR   IntAct; P29379; 1.
DR   BRENDA; 4.2.1.84; 5395.
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   Direct protein sequencing; Lyase.
FT   CHAIN           1..226
FT                   /note="Low-molecular weight cobalt-containing nitrile
FT                   hydratase subunit beta"
FT                   /id="PRO_0000186833"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   226 AA;  25201 MW;  A790BCC67B319654 CRC64;
     MDGIHDLGGR AGLGPIKPES DEPVFHSDWE RSVLTMFPAM ALAGAFNLDQ FRGAMEQIPP
     HDYLTSQYYE HWMHAMIHHG IEAGIFDSDE LDRRTQYYMD HPDDTTPTRQ DPQLVETISQ
     LITHGADYRR PTDTEAAFAV GDKVIVRSDA SPNTHTRRAG YVRGRVGEVV ATHGAYVFPD
     TNALGAGESP EHLYTVRFSA TELWGEPAAP NVVNHIDVFE PYLLPA