ID   CSOCA_HYDCU             Reviewed;         528 AA.
AC   Q31HD6;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Carboxysome shell carbonic anhydrase {ECO:0000303|PubMed:28115547};
DE            Short=CsoSCA {ECO:0000303|PubMed:28115547};
DE            EC=4.2.1.1 {ECO:0000269|PubMed:20400567};
DE   AltName: Full=Carbonic anhydrase {ECO:0000303|PubMed:28115547};
DE            Short=CA {ECO:0000305};
DE   AltName: Full=Carboxysome shell protein CsoS3 {ECO:0000305};
GN   Name=csoS3 {ECO:0000303|PubMed:28115547}; OrderedLocusNames=Tcr_0841;
OS   Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS   crunogena).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Hydrogenovibrio.
OX   NCBI_TaxID=317025;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25203 / XCL-2;
RX   PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA   Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA   Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA   Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA   Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA   Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA   Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA   Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA   Tinkham L.E., Zeruth G.T.;
RT   "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT   XCL-2.";
RL   PLoS Biol. 4:1-17(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=DSM 25203 / XCL-2;
RX   PubMed=20400567; DOI=10.1128/aem.00064-10;
RA   Dobrinski K.P., Boller A.J., Scott K.M.;
RT   "Expression and function of four carbonic anhydrase homologs in the deep-
RT   sea chemolithoautotroph Thiomicrospira crunogena.";
RL   Appl. Environ. Microbiol. 76:3561-3567(2010).
RN   [3]
RP   SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DSM 25203 / XCL-2;
RX   PubMed=28115547; DOI=10.1128/jb.00871-16;
RG   USF MCB4404L;
RA   Mangiapia M., Brown T.W., Chaput D., Haller E., Harmer T.L., Hashemy Z.,
RA   Keeley R., Leonard J., Mancera P., Nicholson D., Stevens S., Wanjugi P.,
RA   Zabinski T., Pan C., Scott K.M.;
RT   "Proteomic and Mutant Analysis of the CO2 Concentrating Mechanism of
RT   Hydrothermal Vent Chemolithoautotroph Thiomicrospira crunogena.";
RL   J. Bacteriol. 199:0-0(2017).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide. This bacteria encodes
CC       at least 3 CA enzymes (PubMed:20400567). Essential for
CC       chemolithotrophic carbon dioxide fixation, supplies CO(2) to RuBisCO
CC       (ribulose bisphosphate carboxylase, cbbL-cbbS) in the carboxysome
CC       (Probable). {ECO:0000269|PubMed:20400567, ECO:0000305|PubMed:20400567}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544; EC=4.2.1.1;
CC         Evidence={ECO:0000269|PubMed:20400567};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O85042};
CC       Note=Binds 1 Zn(2+) per monomer. {ECO:0000250|UniProtKB:O85042};
CC   -!- ACTIVITY REGULATION: Inhibited by ethoxyzolamide and dithiothreitol (in
CC       crude extracts upon expression in E.coli).
CC       {ECO:0000269|PubMed:20400567}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O85042}.
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000305|PubMed:20400567,
CC       ECO:0000305|PubMed:28115547}. Note=This bacterium makes alpha-type
CC       carboxysomes. {ECO:0000305}.
CC   -!- INDUCTION: Induced by growth in low levels of dissolved inorganic
CC       carbon (DIC) (at protein level). {ECO:0000269|PubMed:28115547}.
CC   -!- DISRUPTION PHENOTYPE: Cells do not grow in low DIC levels. Cells lose
CC       carboxysomes when grown under low DIC conditions. Accumulates
CC       intracellular DIC normally, poor CO(2) fixation.
CC       {ECO:0000269|PubMed:28115547}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family. CsoSCA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP000109; ABB41437.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q31HD6; -.
DR   SMR; Q31HD6; -.
DR   STRING; 317025.Tcr_0841; -.
DR   EnsemblBacteria; ABB41437; ABB41437; Tcr_0841.
DR   KEGG; tcx:Tcr_0841; -.
DR   eggNOG; COG0288; Bacteria.
DR   HOGENOM; CLU_535194_0_0_6; -.
DR   OMA; VENSFCC; -.
DR   OrthoDB; 300636at2; -.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1310; -; 1.
DR   Gene3D; 3.30.1330.140; -; 1.
DR   InterPro; IPR014074; Carboxysome_shell_carb_anhy.
DR   InterPro; IPR043066; Carboxysome_shell_carb_anhy_C.
DR   InterPro; IPR043065; Carboxysome_shell_carb_anhy_N.
DR   Pfam; PF08936; CsoSCA; 1.
DR   TIGRFAMs; TIGR02701; shell_carb_anhy; 1.
PE   1: Evidence at protein level;
KW   Bacterial microcompartment; Carbon dioxide fixation; Carboxysome; Lyase;
KW   Metal-binding; Zinc.
FT   CHAIN           1..528
FT                   /note="Carboxysome shell carbonic anhydrase"
FT                   /id="PRO_0000452063"
FT   REGION          17..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O85042"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O85042"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O85042"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O85042"
SQ   SEQUENCE   528 AA;  59254 MW;  BFB6FFBD712B8484 CRC64;
     MNRLKKSHRQ KSLFWRPIAP NPRWQKENPT AHGSTDTGGF GYNGGNEEVK TSSTMMNGIH
     ALVNERQNEW LRGYEVDIKS RFDNIESVLK DILAQQSQLN FVSWANQQLF AKLGVSLTEQ
     DWQSGVQLQS QKGFQFLYGK TLFAQFMRMS EDFFVNDPLS GQRKQEAERM FKEAGFHAVG
     IAPCADGRLA HILSYVLRLP YALARRKAHA GVMFDVSESV RNWVFIEHTR FRDGQPNLAD
     EPTRYLKIAV YHFSKADPTH QGCAAHGSDD HKAAQAALQK LKDFKQAIEN RFGCGSTVQT
     LLLGLNTDDD SMKVHIPNAS GEVCLDRYVE TEQLYQATMN LPDSEAKQAL ENAIVTCNQA
     LGSTAPQPEL VKLLSWLIGN NFSQIAYVNQ YENGCYSDIG HAERFIGIGN GFEEVQLRNL
     SYYSFLDTVE EGVNDVDVGI KIFKGLNVKK GLPIPIIIRC DYDGRVPGSK DRAEAKALRI
     EKALHNRYQE LSAPGLLQTL PTLRDFTSCK PAERLPGLAD LSAKQRTA