CS2H2_ACITH
ID CS2H2_ACITH Reviewed; 199 AA.
AC S5FU55;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Carbon disulfide hydrolase {ECO:0000303|PubMed:23836868};
DE Short=CS(2) hydrolase {ECO:0000303|PubMed:23836868};
DE EC=3.13.1.5 {ECO:0000269|PubMed:23836868};
GN Name=csh {ECO:0000312|EMBL:AGQ48122.1};
OS Acidithiobacillus thiooxidans (Thiobacillus thiooxidans).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=930;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, 3D-STRUCTURE MODELING,
RP AND PATHWAY.
RC STRAIN=G8;
RX PubMed=23836868; DOI=10.1128/jb.00627-13;
RA Smeulders M.J., Pol A., Venselaar H., Barends T.R., Hermans J.,
RA Jetten M.S., Op den Camp H.J.;
RT "Bacterial CS2 hydrolases from Acidithiobacillus thiooxidans strains are
RT homologous to the archaeal catenane CS2 hydrolase.";
RL J. Bacteriol. 195:4046-4056(2013).
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 that allows A.thiooxidans
CC G8 to grow on carbon disulfide as the main carbon and energy source.
CC Does not show carbonic anhydrase activity (hydration of CO(2) to
CC carbonate). {ECO:0000269|PubMed:23836868}.
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:23836868};
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=46 uM for carbon disulfide {ECO:0000269|PubMed:23836868};
CC KM=14 uM for carbonyl sulfide {ECO:0000269|PubMed:23836868};
CC Vmax=131 nmol/min/ug enzyme towards hydrogen sulfide formation from
CC carbon disulfide {ECO:0000269|PubMed:23836868};
CC Vmax=97 nmol/min/ug enzyme towards hydrogen sulfide formation from
CC carbonyl sulfide {ECO:0000269|PubMed:23836868};
CC Note=kcat is 3000 sec(-1) with carbon disulfide as substrate. kcat is
CC 22400 sec(-1) with the intermediate carbonyl sulfide as substrate.
CC {ECO:0000269|PubMed:23836868};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis.
CC {ECO:0000269|PubMed:23836868}.
CC -!- SUBUNIT: Exists as both octamers and hexadecamers in solution. The
CC hexadecameric homooligomer may form a catenane, through interactions of
CC two interlocked octameric rings. {ECO:0000269|PubMed:23836868}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; KC902814; AGQ48122.1; -; Genomic_DNA.
DR AlphaFoldDB; S5FU55; -.
DR SMR; S5FU55; -.
DR BRENDA; 3.13.1.5; 92.
DR UniPathway; UPA00140; -.
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; Zinc.
FT CHAIN 1..199
FT /note="Carbon disulfide hydrolase"
FT /id="PRO_0000445000"
FT BINDING 36
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"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:G0WXL9"
SQ SEQUENCE 199 AA; 22632 MW; 129306B930DDD317 CRC64;
MSLKQQLESD FEGHKRWALR RQMGIPNNRR LWVCACMDER LPVDDALGIR GDRGDAHVFR
NAGGLITDDA IRSAMLTCNF FGTEEIVIIN HTECGMMSAQ TDTIVKALKD KGIDLDNLQL
DPDLPELTLK AGMFGKWVKM YQDVDETCAR QVEYMRNHPL IPKHVTISGW IWEVETGHLR
PPHFRIGEKV NTNKAMGAK
