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Protein

Thiocyanate hydrolase subunit alpha

Gene

scnA

Organism
Thiobacillus thioparus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of thiocyanate.

Catalytic activityi

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

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2145.
BRENDAi3.5.5.8. 6354.
UniPathwayiUPA00366.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 126125Thiocyanate hydrolase subunit alphaPRO_0000097630Add
BLAST

Interactioni

Subunit structurei

Heterododecamer consisting of 4 alpha, 4 beta, and 4 gamma subunits.1 Publication

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 196Combined sources
Turni20 – 223Combined sources
Helixi26 – 283Combined sources
Turni29 – 324Combined sources
Beta strandi42 – 454Combined sources
Helixi58 – 603Combined sources
Beta strandi64 – 7411Combined sources
Helixi77 – 804Combined sources
Turni81 – 833Combined sources
Beta strandi89 – 979Combined sources
Helixi98 – 1014Combined sources
Helixi107 – 1093Combined sources
Beta strandi113 – 1197Combined sources
Helixi120 – 1223Combined sources
Beta strandi123 – 1253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DD4X-ray2.06A/D/G/J1-126[»]
2DD5X-ray2.00A/D/G/J1-126[»]
2DXBX-ray2.25A/D/G/J/M/P/S/V1-126[»]
2DXCX-ray1.90A/D/G/J1-126[»]
2ZZDX-ray1.78A/D/G/J1-126[»]
3VYGX-ray1.72A/D/G/J1-126[»]
ProteinModelPortaliO66187.
SMRiO66187. Positions 7-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66187.

Family & Domainsi

Family and domain databases

InterProiIPR024690. CN_hydtase_beta_dom.
IPR008990. Elect_transpt_acc-like_dom.
[Graphical view]
PfamiPF02211. NHase_beta. 1 hit.
[Graphical view]
SUPFAMiSSF50090. SSF50090. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O66187-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSHHKPVW DRTHHAKMAT GIGDPQCFKG MAGKSKFNVG DRVRIKDLPD
60 70 80 90 100
LFYTRTMTYT RGATGTIVRL VYESPAAEDE AFGNEENVEW FYSIVFAQKD
110 120
LWPEYSDTFA NDTLETEIPE RYLEKA
Length:126
Mass (Da):14,488
Last modified:January 23, 2007 - v3
Checksum:iF0416CE49201E9E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007989 Genomic DNA. Translation: BAA28287.1.

Genome annotation databases

KEGGiag:BAA28287.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007989 Genomic DNA. Translation: BAA28287.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DD4X-ray2.06A/D/G/J1-126[»]
2DD5X-ray2.00A/D/G/J1-126[»]
2DXBX-ray2.25A/D/G/J/M/P/S/V1-126[»]
2DXCX-ray1.90A/D/G/J1-126[»]
2ZZDX-ray1.78A/D/G/J1-126[»]
3VYGX-ray1.72A/D/G/J1-126[»]
ProteinModelPortaliO66187.
SMRiO66187. Positions 7-126.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA28287.

Enzyme and pathway databases

UniPathwayiUPA00366.
BioCyciMetaCyc:MONOMER-2145.
BRENDAi3.5.5.8. 6354.

Miscellaneous databases

EvolutionaryTraceiO66187.

Family and domain databases

InterProiIPR024690. CN_hydtase_beta_dom.
IPR008990. Elect_transpt_acc-like_dom.
[Graphical view]
PfamiPF02211. NHase_beta. 1 hit.
[Graphical view]
SUPFAMiSSF50090. SSF50090. 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 2-13.
    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. "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 SCNB AND SCNC, SUBUNIT.

Entry informationi

Entry nameiSCNA_THITI
AccessioniPrimary (citable) accession number: O66187
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 64 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

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.