CS2H_ACIS1
ID CS2H_ACIS1 Reviewed; 204 AA.
AC G0WXL9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
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};
DE AltName: Full=Carbon disulfide lyase {ECO:0000305};
GN Name=csh {ECO:0000312|EMBL:AEL19654.1};
OS Acidianus sp. (strain A1-3).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus; unclassified Acidianus.
OX NCBI_TaxID=1071056;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS)
RP IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, PATHWAY, AND
RP MUTAGENESIS OF PHE-77; PHE-78; PHE-96 AND 199-GLY--GLU-204.
RC STRAIN=A1-3 {ECO:0000312|EMBL:AEL19654.1};
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).
RN [2]
RP SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=A1-3;
RX PubMed=23771150; DOI=10.1039/c3cc43219j;
RA van Eldijk M.B., van Leeuwen I., Mikhailov V.A., Neijenhuis L.,
RA Harhangi H.R., van Hest J.C., Jetten M.S., Op den Camp H.J., Robinson C.V.,
RA Mecinovic J.;
RT "Evidence that the catenane form of CS2 hydrolase is not an artefact.";
RL Chem. Commun. (Camb.) 49:7770-7772(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 Acidianus sp.
CC A1-3 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: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:0000269|PubMed:22012399};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22012399};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 uM for carbon disulfide {ECO:0000269|PubMed:22012399};
CC KM=22 uM for carbonyl sulfide {ECO:0000269|PubMed:22012399};
CC Vmax=40 nmol/min/ug enzyme towards hydrogen sulfide formation from
CC carbon disulfide {ECO:0000269|PubMed:22012399};
CC Vmax=74 nmol/min/ug enzyme towards hydrogen sulfide formation from
CC carbonyl sulfide {ECO:0000269|PubMed:22012399};
CC Note=kcat is 952 sec(-1) with carbon disulfide as substrate. kcat is
CC 1800 sec(-1) with the intermediate carbonyl sulfide as substrate.
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. Exists as both
CC octamers and hexadecamers in solution. {ECO:0000269|PubMed:22012399,
CC ECO:0000269|PubMed:23771150}.
CC -!- INTERACTION:
CC G0WXL9; G0WXL9: csh; NbExp=8; IntAct=EBI-15949148, EBI-15949148;
CC -!- MASS SPECTROMETRY: Mass=23575.7; Method=Electrospray; Note=Monomeric
CC form obtained under denaturing conditions.;
CC Evidence={ECO:0000269|PubMed:23771150};
CC -!- MASS SPECTROMETRY: Mass=188945; Method=Electrospray; Note=Octameric
CC ring form.; Evidence={ECO:0000269|PubMed:23771150};
CC -!- MASS SPECTROMETRY: Mass=378535; Method=Electrospray; Note=Hexadecameric
CC catenane form.; Evidence={ECO:0000269|PubMed:23771150};
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; HM805096; AEL19654.1; -; Genomic_DNA.
DR PDB; 3TEN; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-204.
DR PDB; 3TEO; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-204.
DR PDBsum; 3TEN; -.
DR PDBsum; 3TEO; -.
DR AlphaFoldDB; G0WXL9; -.
DR SMR; G0WXL9; -.
DR DIP; DIP-59165N; -.
DR KEGG; ag:AEL19654; -.
DR BioCyc; MetaCyc:MON-18114; -.
DR SABIO-RK; G0WXL9; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..204
FT /note="Carbon disulfide hydrolase"
FT /id="PRO_0000430808"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22012399,
FT ECO:0000312|PDB:3TEN"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22012399,
FT ECO:0000312|PDB:3TEN"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22012399,
FT ECO:0000312|PDB:3TEN"
FT MUTAGEN 77
FT /note="F->A: Increases catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:22012399"
FT MUTAGEN 78
FT /note="F->Y,A,W: Nearly abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:22012399"
FT MUTAGEN 96
FT /note="F->S: Increases catalytic activity."
FT /evidence="ECO:0000269|PubMed:22012399"
FT MUTAGEN 199..204
FT /note="Missing: Increases catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:22012399"
FT HELIX 3..17
FT /evidence="ECO:0007829|PDB:3TEO"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:3TEO"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3TEO"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:3TEO"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:3TEO"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:3TEO"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:3TEO"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:3TEO"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:3TEO"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3TEO"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3TEO"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:3TEO"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:3TEO"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:3TEO"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:3TEO"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3TEO"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3TEN"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:3TEO"
SQ SEQUENCE 204 AA; 23576 MW; F7BE1AB7A0F79469 CRC64;
MVSEYIDSEL KRLEDYALRR VKGIPNNRRL WVLTCMDERV HIEQSLGIQP DDAHIYRNAG
GIVTDDAIRS ASLTTNFFGT KEIIVVTHTD CGMLRFTGEE VAKYFISKGI KPTEVQLDPL
LPAFRISSEE DFIKWFKFYE DLGVKSPDEM ALKGVEILRN HPLIPKDVRI TGYVYEVETH
RLRKPNQIIY NETSKFEHGT IVKE
