CS2H1_ACITH
ID CS2H1_ACITH Reviewed; 217 AA.
AC S5FT07;
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:AGQ48123.1};
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=S1p;
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 S1p 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=93 uM for carbon disulfide {ECO:0000269|PubMed:23836868};
CC KM=74 uM for carbonyl sulfide {ECO:0000269|PubMed:23836868};
CC Vmax=32 nmol/min/ug enzyme towards hydrogen sulfide formation from
CC carbon disulfide {ECO:0000269|PubMed:23836868};
CC Vmax=34 nmol/min/ug enzyme towards hydrogen sulfide formation from
CC carbonyl sulfide {ECO:0000269|PubMed:23836868};
CC Note=kcat is 780 sec(-1) with carbon disulfide as substrate. kcat is
CC 814 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: Forms only homooctamers in solution.
CC {ECO:0000269|PubMed:23836868}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; KC902815; AGQ48123.1; -; Genomic_DNA.
DR AlphaFoldDB; S5FT07; -.
DR SMR; S5FT07; -.
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..217
FT /note="Carbon disulfide hydrolase"
FT /id="PRO_0000444999"
FT REGION 192..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:G0WXL9"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:G0WXL9"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:G0WXL9"
SQ SEQUENCE 217 AA; 24317 MW; 1A3DDD03E979FD68 CRC64;
MSTLKEQLTA HVASYDHWAQ RRRYGPDGHN NRSLWVLACM DERLPVDEAL GIHVDTPAGG
GDAHCFRNAG GIVTDDAIRS AMLTCNFFGT KEIVIVQHTQ CGMLSGNANE MEKVLREKGM
DTDNITLDPT LPELQLAKGA FAKWIGMMDD VDETCMKTIN AFKNHPLIPK DIVVSGWVWE
VENRRLRAPT LDKEKRARTD CTPTPYGVKG NQPPRWK
