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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)DescriptionActionsGraphical viewLength
Metal bindingi128Cobalt1
Metal bindingi131Cobalt1
Metal bindingi132Cobalt; via carbonyl oxygen1
Metal bindingi133Cobalt1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandCobalt, 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 lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesThiobacillaceaeThiobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001868272 – 243Thiocyanate hydrolase subunit gammaAdd BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei131Cysteine sulfinic acid (-SO2H)3 Publications1
Modified residuei133Cysteine sulfenic acid (-SOH)2 Publications1

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1243
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 40Combined sources15
Helixi46 – 58Combined sources13
Helixi62 – 73Combined sources12
Helixi75 – 83Combined sources9
Helixi85 – 89Combined sources5
Helixi90 – 92Combined sources3
Turni96 – 98Combined sources3
Turni107 – 109Combined sources3
Beta strandi113 – 117Combined sources5
Beta strandi122 – 127Combined sources6
Helixi136 – 139Combined sources4
Helixi145 – 147Combined sources3
Helixi149 – 154Combined sources6
Turni155 – 157Combined sources3
Helixi159 – 165Combined sources7
Beta strandi174 – 180Combined sources7
Beta strandi186 – 190Combined sources5
Helixi202 – 207Combined sources6
Helixi211 – 215Combined sources5
Beta strandi236 – 238Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66188.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK20762.

Family and domain databases

Gene3Di3.90.330.10. 1 hit.
InterProiView protein in InterPro
IPR004232. CN_Hdrtase_a/SCN_Hdrlase_g.
IPR023900. CN_Hdrtase_asu/SCN_Hdrlase_gsu.
IPR023901. Thiocyan_Hydrolase_gsu.
PfamiView protein in Pfam
PF02979. NHase_alpha. 1 hit.
PIRSFiPIRSF001426. NHase_alpha. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD007559. CN_Hdrtase_asu/SCN_Hdrlase_gsu. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti13 – 15HDH → KPA AA sequence (PubMed:9573140).Curated3

Sequence databases

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

Genome annotation databases

KEGGiag:BAA28288.

Similar proteinsi

Entry informationi

Entry nameiSCNC_THITI
AccessioniPrimary (citable) accession number: O66188
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 87 of the entry and version 3 of the sequence. See 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