COSH_THITI
ID COSH_THITI Reviewed; 219 AA.
AC H1AAP2;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Carbonyl sulfide hydrolase {ECO:0000303|PubMed:23406161};
DE Short=COSase {ECO:0000303|PubMed:23406161};
DE EC=3.13.1.7 {ECO:0000269|PubMed:23406161, ECO:0000269|PubMed:29199215};
GN Name=cos {ECO:0000312|EMBL:BAL45931.1};
OS Thiobacillus thioparus.
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=931;
RN [1] {ECO:0007744|PDB:3VQJ, ECO:0007744|PDB:3VRK}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND X-RAY
RP CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEXES WITH ZINC AND THIOCYANATE.
RC STRAIN=THI 115;
RX PubMed=23406161; DOI=10.1021/ja307735e;
RA Ogawa T., Noguchi K., Saito M., Nagahata Y., Kato H., Ohtaki A.,
RA Nakayama H., Dohmae N., Matsushita Y., Odaka M., Yohda M., Nyunoya H.,
RA Katayama Y.;
RT "Carbonyl sulfide hydrolase from Thiobacillus thioparus strain THI115 is
RT one of the beta-carbonic anhydrase family enzymes.";
RL J. Am. Chem. Soc. 135:3818-3825(2013).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=THI 115;
RX PubMed=29199215; DOI=10.1264/jsme2.me17130;
RA Ogawa T., Hattori S., Kamezaki K., Kato H., Yoshida N., Katayama Y.;
RT "Isotopic fractionation of sulfur in carbonyl sulfide by carbonyl sulfide
RT hydrolase of Thiobacillus thioparus THI115.";
RL Microbes Environ. 32:367-375(2017).
CC -!- FUNCTION: Catalyzes the degradation of carbonyl sulfide (COS) to
CC hydrogen sulfide and CO(2) (PubMed:23406161, PubMed:29199215). May
CC function as one of the microbial sinks for ambient COS, which is an
CC atmospheric trace gas leading to sulfate aerosol formation, thereby
CC participating in the global radiation balance and ozone chemistry
CC (PubMed:23406161). Shows little CO(2) hydration activity and poor
CC carbon disulfide (CS(2)) hydrolysis activity (PubMed:23406161).
CC {ECO:0000269|PubMed:23406161, ECO:0000269|PubMed:29199215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbonyl sulfide + H2O = CO2 + H(+) + hydrogen sulfide;
CC Xref=Rhea:RHEA:38151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16573, ChEBI:CHEBI:29919; EC=3.13.1.7;
CC Evidence={ECO:0000269|PubMed:23406161, ECO:0000269|PubMed:29199215};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38152;
CC Evidence={ECO:0000269|PubMed:23406161, ECO:0000269|PubMed:29199215};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23406161};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23406161};
CC -!- ACTIVITY REGULATION: Weakly inhibited by thiocyanate (SCN(-)).
CC {ECO:0000269|PubMed:23406161}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for carbonyl sulfide {ECO:0000269|PubMed:23406161};
CC Note=kcat is 58 sec(-1). {ECO:0000269|PubMed:23406161};
CC -!- SUBUNIT: Homotetramer. Two pairs of subunits form tightly associated
CC dimers. {ECO:0000269|PubMed:23406161}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AB583934; BAL45931.1; -; Genomic_DNA.
DR PDB; 3VQJ; X-ray; 1.20 A; A=1-219.
DR PDB; 3VRK; X-ray; 1.33 A; A=1-219.
DR PDBsum; 3VQJ; -.
DR PDBsum; 3VRK; -.
DR AlphaFoldDB; H1AAP2; -.
DR SMR; H1AAP2; -.
DR KEGG; ag:BAL45931; -.
DR BioCyc; MetaCyc:MON-20302; -.
DR BRENDA; 3.13.1.7; 6354.
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 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 3D-structure; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..219
FT /note="Carbonyl sulfide hydrolase"
FT /id="PRO_0000451598"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:23406161,
FT ECO:0007744|PDB:3VQJ, ECO:0007744|PDB:3VRK"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:23406161,
FT ECO:0007744|PDB:3VQJ, ECO:0007744|PDB:3VRK"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:23406161,
FT ECO:0007744|PDB:3VQJ, ECO:0007744|PDB:3VRK"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:3VQJ"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3VQJ"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3VQJ"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:3VQJ"
FT HELIX 74..85
FT /evidence="ECO:0007829|PDB:3VQJ"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3VQJ"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3VQJ"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:3VQJ"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:3VQJ"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3VQJ"
FT HELIX 161..180
FT /evidence="ECO:0007829|PDB:3VQJ"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:3VQJ"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:3VQJ"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:3VQJ"
SQ SEQUENCE 219 AA; 23353 MW; EE23464D99549096 CRC64;
MEKSNTDALL ENNRLYAGGQ ATHRPGHPGM QPIQPSRRVA VVACMDARLD VEDLLGLQTG
EAHIIRNAGG VINEDAIRCL IISHHLLNTH EIILVHHTRC GMLAFTDDLL RAGLEGDAAA
EKLIGQATGR AFVSAGKASA SPAAFQAFRG PPEPLDAPRS DASTERIAAD VRRGLSIILN
HPWLPTAGPD AITVRGFIYD VDTGRLEEVS YPGPMGGFG
