ID   SCNB_THITI              Reviewed;         157 AA.
AC   O66186;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Thiocyanate hydrolase subunit beta;
DE            EC=3.5.5.8;
GN   Name=scnB;
OS   Thiobacillus thioparus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=THI 115;
RX   PubMed=9573140; DOI=10.1128/jb.180.10.2583-2589.1998;
RA   Katayama Y., Matsushita Y., Kaneko M., Kondo M., Mizuno T., Nyunoya H.;
RT   "Cloning of genes coding for the three subunits of thiocyanate hydrolase of
RT   Thiobacillus thioparus THI 115 and their evolutionary relationships to
RT   nitrile hydratase.";
RL   J. Bacteriol. 180:2583-2589(1998).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=THI 115;
RX   PubMed=1577754; DOI=10.1016/s0021-9258(19)50404-5;
RA   Katayama Y., Narahara Y., Inoue Y., Amano F., Kanagawa T., Kuraishi H.;
RT   "A thiocyanate hydrolase of Thiobacillus thioparus. A novel enzyme
RT   catalyzing the formation of carbonyl sulfide from thiocyanate.";
RL   J. Biol. Chem. 267:9170-9175(1992).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SCNA AND SCNC, AND
RP   SUBUNIT.
RX   PubMed=17222425; DOI=10.1016/j.jmb.2006.12.011;
RA   Arakawa T., Kawano Y., Kataoka S., Katayama Y., Kamiya N., Yohda M.,
RA   Odaka M.;
RT   "Structure of thiocyanate hydrolase: a new nitrile hydratase family protein
RT   with a novel five-coordinate cobalt(III) center.";
RL   J. Mol. Biol. 366:1497-1509(2007).
CC   -!- FUNCTION: Involved in the degradation of thiocyanate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + thiocyanate = carbonyl sulfide + NH4(+);
CC         Xref=Rhea:RHEA:21464, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16573, ChEBI:CHEBI:18022, ChEBI:CHEBI:28938; EC=3.5.5.8;
CC   -!- PATHWAY: Organosulfur degradation; thiocyanate degradation.
CC   -!- SUBUNIT: Heterododecamer consisting of 4 alpha, 4 beta, and 4 gamma
CC       subunits. {ECO:0000269|PubMed:17222425}.
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DR   EMBL; AB007989; BAA28286.1; -; Genomic_DNA.
DR   PDB; 2DD4; X-ray; 2.06 A; B/E/H/K=1-157.
DR   PDB; 2DD5; X-ray; 2.00 A; B/E/H/K=1-157.
DR   PDB; 2DXB; X-ray; 2.25 A; B/E/H/K/N/Q/T/W=1-157.
DR   PDB; 2DXC; X-ray; 1.90 A; B/E/H/K=1-157.
DR   PDB; 2ZZD; X-ray; 1.78 A; B/E/H/K=1-157.
DR   PDB; 3VYG; X-ray; 1.72 A; B/E/H/K=1-157.
DR   PDBsum; 2DD4; -.
DR   PDBsum; 2DD5; -.
DR   PDBsum; 2DXB; -.
DR   PDBsum; 2DXC; -.
DR   PDBsum; 2ZZD; -.
DR   PDBsum; 3VYG; -.
DR   AlphaFoldDB; O66186; -.
DR   SMR; O66186; -.
DR   KEGG; ag:BAA28286; -.
DR   BioCyc; MetaCyc:MON-2146; -.
DR   BRENDA; 3.5.5.8; 6354.
DR   UniPathway; UPA00366; -.
DR   EvolutionaryTrace; O66186; -.
DR   GO; GO:0018822; F:nitrile hydratase activity; IEA:InterPro.
DR   GO; GO:0018760; F:thiocyanate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046265; P:thiocyanate catabolic process; IEA:UniProtKB-UniPathway.
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   Pfam; PF02211; NHase_beta; 1.
DR   SUPFAM; SSF50090; SSF50090; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9573140"
FT   CHAIN           2..157
FT                   /note="Thiocyanate hydrolase subunit beta"
FT                   /id="PRO_0000097631"
FT   HELIX           4..16
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   HELIX           17..19
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   HELIX           37..43
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   HELIX           67..81
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   HELIX           87..95
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   HELIX           100..105
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   HELIX           108..122
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   HELIX           128..143
FT                   /evidence="ECO:0007829|PDB:3VYG"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:3VYG"
SQ   SEQUENCE   157 AA;  18040 MW;  60F183ACAE61A1DA CRC64;
     MSSSIREEVH RHLGTVALMQ PALHQQTHAP APTEITHTLF RAYTRVPHDV GGEADVPIEY
     HEKEEEIWEL NTFATCECLA WRGVWTAEER RRKQNCDVGQ TVYLGMPYYG RWLLTAARIL
     VDKQFVTLTE LHNKIVEMRE RVASGQGLGE YLPPKAK