SCNC_THITI
ID SCNC_THITI Reviewed; 243 AA.
AC O66188;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Thiocyanate hydrolase subunit gamma;
DE EC=3.5.5.8;
GN Name=scnC;
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 2-22.
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 COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, OXIDATION AT CYS-131 AND
RP CYS-133, AND SUBUNIT.
RX PubMed=16879822; DOI=10.1016/j.febslet.2006.07.051;
RA Kataoka S., Arakawa T., Hori S., Katayama Y., Hara Y., Matsushita Y.,
RA Nakayama H., Yohda M., Nyunoya H., Dohmae N., Maeda M., Odaka M.;
RT "Functional expression of thiocyanate hydrolase is promoted by its
RT activator protein, P15K.";
RL FEBS Lett. 580:4667-4672(2006).
RN [4]
RP COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, AND OXIDATION AT CYS-131.
RX PubMed=16417356; DOI=10.1021/ja057010q;
RA Katayama Y., Hashimoto K., Nakayama H., Mino H., Nojiri M., Ono T.A.,
RA Nyunoya H., Yohda M., Takio K., Odaka M.;
RT "Thiocyanate hydrolase is a cobalt-containing metalloenzyme with a
RT cysteine-sulfinic acid ligand.";
RL J. Am. Chem. Soc. 128:728-729(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH COBALT IONS; SCNA AND
RP SCNB, OXIDATION AT CYS-131 AND CYS-133, AND 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 -!- COFACTOR:
CC Name=Co(3+); Xref=ChEBI:CHEBI:49415;
CC Evidence={ECO:0000269|PubMed:16417356, ECO:0000269|PubMed:16879822};
CC Note=Binds 1 Co(3+) ion per subunit. {ECO:0000269|PubMed:16417356,
CC ECO:0000269|PubMed:16879822};
CC -!- PATHWAY: Organosulfur degradation; thiocyanate degradation.
CC -!- SUBUNIT: Heterododecamer consisting of 4 alpha, 4 beta, and 4 gamma
CC subunits. {ECO:0000269|PubMed:16879822, ECO:0000269|PubMed:17222425}.
CC -!- SIMILARITY: Belongs to the nitrile hydratase subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; AB007989; BAA28288.1; -; Genomic_DNA.
DR PDB; 2DD4; X-ray; 2.06 A; C/F/I/L=1-243.
DR PDB; 2DD5; X-ray; 2.00 A; C/F/I/L=1-243.
DR PDB; 2DXB; X-ray; 2.25 A; C/F/I/L/O/R/U/X=1-243.
DR PDB; 2DXC; X-ray; 1.90 A; C/F/I/L=1-243.
DR PDB; 2ZZD; X-ray; 1.78 A; C/F/I/L=1-243.
DR PDB; 3VYG; X-ray; 1.72 A; C/F/I/L=1-243.
DR PDBsum; 2DD4; -.
DR PDBsum; 2DD5; -.
DR PDBsum; 2DXB; -.
DR PDBsum; 2DXC; -.
DR PDBsum; 2ZZD; -.
DR PDBsum; 3VYG; -.
DR AlphaFoldDB; O66188; -.
DR SMR; O66188; -.
DR KEGG; ag:BAA28288; -.
DR BioCyc; MetaCyc:MON-2147; -.
DR BRENDA; 3.5.5.8; 6354.
DR UniPathway; UPA00366; -.
DR EvolutionaryTrace; O66188; -.
DR GO; GO:0018760; F:thiocyanate hydrolase 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 GO; GO:0046265; P:thiocyanate catabolic process; IEA:UniProtKB-UniPathway.
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; IPR023901; Thiocyan_Hydrolase_gsu.
DR Pfam; PF02979; NHase_alpha; 1.
DR PIRSF; PIRSF001426; NHase_alpha; 1.
DR SUPFAM; SSF56209; SSF56209; 1.
DR TIGRFAMs; TIGR03887; thiocyan_alph; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalt; Direct protein sequencing; Hydrolase; Metal-binding;
KW Oxidation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9573140"
FT CHAIN 2..243
FT /note="Thiocyanate hydrolase subunit gamma"
FT /id="PRO_0000186827"
FT BINDING 128
FT /ligand="Co(3+)"
FT /ligand_id="ChEBI:CHEBI:49415"
FT /evidence="ECO:0007744|PDB:2DD5"
FT BINDING 131
FT /ligand="Co(3+)"
FT /ligand_id="ChEBI:CHEBI:49415"
FT /evidence="ECO:0007744|PDB:2DD5"
FT BINDING 132
FT /ligand="Co(3+)"
FT /ligand_id="ChEBI:CHEBI:49415"
FT /evidence="ECO:0007744|PDB:2DD5"
FT BINDING 133
FT /ligand="Co(3+)"
FT /ligand_id="ChEBI:CHEBI:49415"
FT /evidence="ECO:0007744|PDB:2DD5"
FT MOD_RES 131
FT /note="Cysteine sulfinic acid (-SO2H)"
FT /evidence="ECO:0000269|PubMed:16417356,
FT ECO:0000269|PubMed:16879822, ECO:0000269|PubMed:17222425"
FT MOD_RES 133
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000269|PubMed:16879822,
FT ECO:0000269|PubMed:17222425"
FT CONFLICT 13..15
FT /note="HDH -> KPA (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 26..40
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3VYG"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3VYG"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3VYG"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3VYG"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:3VYG"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:3VYG"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:3VYG"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:3VYG"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:3VYG"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3VYG"
SQ SEQUENCE 243 AA; 27530 MW; 3A9D391B38220C50 CRC64;
MSADHDHDHD HDHDHKPAPM VEEVSDFEIL EMAVRELAIE KGLFSAEDHR VWKDYVHTLG
PLPAARLVAK AWLDPEYKKL CIEDGVEASK AVGVNWVTSP PTQFGTPSDY CNLRVLADSP
TLKHVVVCTL CSCYPRPILG QSPEWYRSPN YRRRLVRWPR QVLAEFGLQL PSEVQIRVAD
SNQKTRYIVM PVRPEGTDGW TEDQLAEIVT RDCLIGVAVP KPGITVNAKR PVLKANRPVH
HDH
