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Protein

Thiocyanate hydrolase subunit gamma

Gene

scnC

Organism
Thiobacillus thioparus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of thiocyanate.

Catalytic activityi

Thiocyanate + 2 H2O = carbonyl sulfide + NH3 + HO-.

Cofactori

Co3+2 PublicationsNote: Binds 1 Co3+ ion per subunit.2 Publications

Pathwayi: thiocyanate degradation

This protein is involved in the pathway thiocyanate degradation, which is part of Organosulfur degradation.
View all proteins of this organism that are known to be involved in the pathway thiocyanate degradation and in Organosulfur degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi128 – 1281Cobalt
Metal bindingi131 – 1311Cobalt
Metal bindingi132 – 1321Cobalt; via carbonyl oxygen
Metal bindingi133 – 1331Cobalt

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Cobalt, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2147.
BRENDAi3.5.5.8. 6354.
UniPathwayiUPA00366.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiocyanate hydrolase subunit gamma (EC:3.5.5.8)
Gene namesi
Name:scnC
OrganismiThiobacillus thioparus
Taxonomic identifieri931 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 243242Thiocyanate hydrolase subunit gammaPRO_0000186827Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei131 – 1311Cysteine sulfinic acid (-SO2H)3 Publications
Modified residuei133 – 1331Cysteine sulfenic acid (-SOH)2 Publications

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Heterododecamer consisting of 4 alpha, 4 beta, and 4 gamma subunits.2 Publications

Structurei

Secondary structure

1
243
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 4015Combined sources
Helixi46 – 5813Combined sources
Helixi62 – 7312Combined sources
Helixi75 – 839Combined sources
Helixi85 – 895Combined sources
Helixi90 – 923Combined sources
Turni96 – 983Combined sources
Turni107 – 1093Combined sources
Beta strandi113 – 1175Combined sources
Beta strandi122 – 1276Combined sources
Helixi136 – 1394Combined sources
Helixi145 – 1473Combined sources
Helixi149 – 1546Combined sources
Turni155 – 1573Combined sources
Helixi159 – 1657Combined sources
Beta strandi174 – 1807Combined sources
Beta strandi186 – 1905Combined sources
Helixi202 – 2076Combined sources
Helixi211 – 2155Combined sources
Beta strandi236 – 2383Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DD4X-ray2.06C/F/I/L1-243[»]
2DD5X-ray2.00C/F/I/L1-243[»]
2DXBX-ray2.25C/F/I/L/O/R/U/X1-243[»]
2DXCX-ray1.90C/F/I/L1-243[»]
2ZZDX-ray1.78C/F/I/L1-243[»]
3VYGX-ray1.72C/F/I/L1-243[»]
ProteinModelPortaliO66188.
SMRiO66188. Positions 23-239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66188.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.90.330.10. 1 hit.
InterProiIPR004232. CN_Hdrtase_a/SCN_Hdrlase_g.
IPR023900. CN_Hdrtase_asu/SCN_Hdrlase_gsu.
IPR023901. Thiocyan_Hydrolase_gsu.
[Graphical view]
PfamiPF02979. NHase_alpha. 1 hit.
[Graphical view]
PIRSFiPIRSF001426. NHase_alpha. 1 hit.
ProDomiPD007559. CN_Hdrtase_asu/SCN_Hdrlase_gsu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56209. SSF56209. 1 hit.
TIGRFAMsiTIGR03887. thiocyan_alph. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O66188-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSADHDHDHD HDHDHKPAPM VEEVSDFEIL EMAVRELAIE KGLFSAEDHR
60 70 80 90 100
VWKDYVHTLG PLPAARLVAK AWLDPEYKKL CIEDGVEASK AVGVNWVTSP
110 120 130 140 150
PTQFGTPSDY CNLRVLADSP TLKHVVVCTL CSCYPRPILG QSPEWYRSPN
160 170 180 190 200
YRRRLVRWPR QVLAEFGLQL PSEVQIRVAD SNQKTRYIVM PVRPEGTDGW
210 220 230 240
TEDQLAEIVT RDCLIGVAVP KPGITVNAKR PVLKANRPVH HDH
Length:243
Mass (Da):27,530
Last modified:January 23, 2007 - v3
Checksum:i3A9D391B38220C50
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 153HDH → KPA AA sequence (PubMed:9573140).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007989 Genomic DNA. Translation: BAA28288.1.

Genome annotation databases

KEGGiag:BAA28288.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007989 Genomic DNA. Translation: BAA28288.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DD4X-ray2.06C/F/I/L1-243[»]
2DD5X-ray2.00C/F/I/L1-243[»]
2DXBX-ray2.25C/F/I/L/O/R/U/X1-243[»]
2DXCX-ray1.90C/F/I/L1-243[»]
2ZZDX-ray1.78C/F/I/L1-243[»]
3VYGX-ray1.72C/F/I/L1-243[»]
ProteinModelPortaliO66188.
SMRiO66188. Positions 23-239.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA28288.

Enzyme and pathway databases

UniPathwayiUPA00366.
BioCyciMetaCyc:MONOMER-2147.
BRENDAi3.5.5.8. 6354.

Miscellaneous databases

EvolutionaryTraceiO66188.

Family and domain databases

Gene3Di3.90.330.10. 1 hit.
InterProiIPR004232. CN_Hdrtase_a/SCN_Hdrlase_g.
IPR023900. CN_Hdrtase_asu/SCN_Hdrlase_gsu.
IPR023901. Thiocyan_Hydrolase_gsu.
[Graphical view]
PfamiPF02979. NHase_alpha. 1 hit.
[Graphical view]
PIRSFiPIRSF001426. NHase_alpha. 1 hit.
ProDomiPD007559. CN_Hdrtase_asu/SCN_Hdrlase_gsu. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56209. SSF56209. 1 hit.
TIGRFAMsiTIGR03887. thiocyan_alph. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI 115 and their evolutionary relationships to nitrile hydratase."
    Katayama Y., Matsushita Y., Kaneko M., Kondo M., Mizuno T., Nyunoya H.
    J. Bacteriol. 180:2583-2589(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22.
    Strain: THI 115.
  2. "A thiocyanate hydrolase of Thiobacillus thioparus. A novel enzyme catalyzing the formation of carbonyl sulfide from thiocyanate."
    Katayama Y., Narahara Y., Inoue Y., Amano F., Kanagawa T., Kuraishi H.
    J. Biol. Chem. 267:9170-9175(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: THI 115.
  3. "Functional expression of thiocyanate hydrolase is promoted by its activator protein, P15K."
    Kataoka S., Arakawa T., Hori S., Katayama Y., Hara Y., Matsushita Y., Nakayama H., Yohda M., Nyunoya H., Dohmae N., Maeda M., Odaka M.
    FEBS Lett. 580:4667-4672(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, OXIDATION AT CYS-131 AND CYS-133, SUBUNIT.
  4. "Thiocyanate hydrolase is a cobalt-containing metalloenzyme with a cysteine-sulfinic acid ligand."
    Katayama Y., Hashimoto K., Nakayama H., Mino H., Nojiri M., Ono T.A., Nyunoya H., Yohda M., Takio K., Odaka M.
    J. Am. Chem. Soc. 128:728-729(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, OXIDATION AT CYS-131.
  5. "Structure of thiocyanate hydrolase: a new nitrile hydratase family protein with a novel five-coordinate cobalt(III) center."
    Arakawa T., Kawano Y., Kataoka S., Katayama Y., Kamiya N., Yohda M., Odaka M.
    J. Mol. Biol. 366:1497-1509(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH COBALT IONS; SCNA AND SCNB, OXIDATION AT CYS-131 AND CYS-133, SUBUNIT.

Entry informationi

Entry nameiSCNC_THITI
AccessioniPrimary (citable) accession number: O66188
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.