CS2H_SACS2
ID CS2H_SACS2 Reviewed; 204 AA.
AC Q97YU3;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Carbon disulfide hydrolase {ECO:0000303|PubMed:22012399};
DE Short=CS(2) hydrolase {ECO:0000303|PubMed:22012399};
DE EC=3.13.1.5 {ECO:0000269|PubMed:22012399};
GN OrderedLocusNames=SSO1214 {ECO:0000312|EMBL:AAK41461.1};
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=22012399; DOI=10.1038/nature10464;
RA Smeulders M.J., Barends T.R., Pol A., Scherer A., Zandvoort M.H.,
RA Udvarhelyi A., Khadem A.F., Menzel A., Hermans J., Shoeman R.L.,
RA Wessels H.J., van den Heuvel L.P., Russ L., Schlichting I., Jetten M.S.,
RA Op den Camp H.J.;
RT "Evolution of a new enzyme for carbon disulphide conversion by an
RT acidothermophilic archaeon.";
RL Nature 478:412-416(2011).
CC -!- FUNCTION: Catalyzes the conversion of carbon disulfide into hydrogen
CC sulfide and carbon dioxide, with carbonyl sulfide as an intermediate.
CC Likely plays a key role in sulfur metabolism in S.solfataricus. Does
CC not show carbonic anhydrase activity (hydration of CO(2) to carbonate).
CC {ECO:0000269|PubMed:22012399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbon disulfide + 2 H2O = CO2 + 2 H(+) + 2 hydrogen sulfide;
CC Xref=Rhea:RHEA:38143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:23012, ChEBI:CHEBI:29919; EC=3.13.1.5;
CC Evidence={ECO:0000269|PubMed:22012399};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:G0WXL9};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:G0WXL9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=86 uM for carbon disulfide {ECO:0000269|PubMed:22012399};
CC Vmax=96 nmol/min/ug enzyme towards hydrogen sulfide formation
CC {ECO:0000269|PubMed:22012399};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis.
CC {ECO:0000269|PubMed:22012399}.
CC -!- SUBUNIT: Forms a hexadecameric catenane homooligomer, through
CC interactions of two interlocked octameric rings.
CC {ECO:0000250|UniProtKB:G0WXL9}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AE006641; AAK41461.1; -; Genomic_DNA.
DR PIR; F90275; F90275.
DR RefSeq; WP_010923252.1; NC_002754.1.
DR AlphaFoldDB; Q97YU3; -.
DR SMR; Q97YU3; -.
DR STRING; 273057.SSO1214; -.
DR EnsemblBacteria; AAK41461; AAK41461; SSO1214.
DR GeneID; 27427583; -.
DR KEGG; sso:SSO1214; -.
DR PATRIC; fig|273057.12.peg.1214; -.
DR eggNOG; arCOG02860; Archaea.
DR HOGENOM; CLU_084253_1_1_2; -.
DR InParanoid; Q97YU3; -.
DR OMA; AIFTCMD; -.
DR PhylomeDB; Q97YU3; -.
DR SABIO-RK; Q97YU3; -.
DR UniPathway; UPA00140; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1050.10; -; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR43175; PTHR43175; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; SSF53056; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..204
FT /note="Carbon disulfide hydrolase"
FT /id="PRO_0000444998"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:G0WXL9"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:G0WXL9"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:G0WXL9"
SQ SEQUENCE 204 AA; 23678 MW; AA05BEF5269714B4 CRC64;
MISEYVDEEI KRREDYSLRR LKGIPNDRRL WILTCMDERV HVEEALGIRP EDAHIYRNAG
GIVTDDAIRS ASLTTNFFGT KEIIVITHTD CGMIRFTGDE VAKYFLDKGV KVNELQIDPL
LPSLRLQSTE DFTKWFKFFR DLGANSPDDI ALKNAEILKN HPLIPKNVTI SAYVYEVETH
KLRKPHQRLY ELTSRFEHGT VVKE
