ID   CSOCA_PARMW             Reviewed;         579 AA.
AC   Q7TTT8;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Carboxysome shell carbonic anhydrase {ECO:0000303|PubMed:14729686};
DE            Short=CsoSCA {ECO:0000305};
DE            EC=4.2.1.1 {ECO:0000269|PubMed:14729686, ECO:0000269|Ref.3};
DE   AltName: Full=Carbonic anhydrase {ECO:0000303|PubMed:14729686};
DE            Short=CA {ECO:0000303|PubMed:14729686};
DE   AltName: Full=Carboxysome shell protein CsoS3 {ECO:0000303|PubMed:14729686};
GN   Name=csoS3 {ECO:0000303|PubMed:14729686}; OrderedLocusNames=SYNW1715;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
RN   [2]
RP   FUNCTION AS A CARBONIC ANHYDRASE, AND CATALYTIC ACTIVITY.
RC   STRAIN=WH8102;
RX   PubMed=14729686; DOI=10.1128/jb.186.3.623-630.2004;
RA   So A.K., Espie G.S., Williams E.B., Shively J.M., Heinhorst S.,
RA   Cannon G.C.;
RT   "A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a
RT   component of the carboxysome shell.";
RL   J. Bacteriol. 186:623-630(2004).
RN   [3]
RP   FUNCTION AS A CARBONIC ANHYDRASE, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RX   DOI=10.1139/b05-057;
RA   So A.K., Espie G.S.;
RT   "Cyanobacterial carbonic anhydrases.";
RL   Can. J. Bot. 83:721-734(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC   STRAIN=WH8102;
RX   PubMed=31507578; DOI=10.3389/fmicb.2019.01976;
RA   Li Y.Y., Chen X.H., Xue C., Zhang H., Sun G., Xie Z.X., Lin L., Wang D.Z.;
RT   "Proteomic Response to Rising Temperature in the Marine Cyanobacterium
RT   Synechococcus Grown in Different Nitrogen Sources.";
RL   Front. Microbiol. 10:1976-1976(2019).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide (PubMed:14729686,
CC       Ref.3). Essential for photosynthetic carbon dioxide fixation, supplies
CC       CO(2) to RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) in the
CC       carboxysome (Probable). {ECO:0000269|PubMed:14729686,
CC       ECO:0000269|Ref.3, ECO:0000305|PubMed:14729686, ECO:0000305|Ref.3}.
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; Evidence={ECO:0000269|PubMed:14729686,
CC         ECO:0000269|Ref.3};
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 dithiothreitol, partially inhibited
CC       by acetatzolamide and cyanide. {ECO:0000269|Ref.3}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O85042}.
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000303|Ref.3}. Note=This
CC       cyanobacterium makes alpha-type carboxysomes. {ECO:0000305}.
CC   -!- INDUCTION: Carbonic anhydrase activity of nitrate- and urea-grown cells
CC       decreases with rising temperature (from 25 to 28 degrees Celsius,
CC       present versus predicted future ocean temperatures); there is probably
CC       more than one carbonic anhydrase in this cyanobacteria.
CC       {ECO:0000269|PubMed:31507578}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family. CsoSCA
CC       subfamily. {ECO:0000305|PubMed:14729686}.
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DR   EMBL; BX569693; CAE08230.1; -; Genomic_DNA.
DR   RefSeq; WP_011128577.1; NC_005070.1.
DR   AlphaFoldDB; Q7TTT8; -.
DR   SMR; Q7TTT8; -.
DR   STRING; 84588.SYNW1715; -.
DR   EnsemblBacteria; CAE08230; CAE08230; SYNW1715.
DR   KEGG; syw:SYNW1715; -.
DR   eggNOG; ENOG502Z9V7; Bacteria.
DR   HOGENOM; CLU_535194_0_0_3; -.
DR   OMA; VENSFCC; -.
DR   OrthoDB; 300636at2; -.
DR   Proteomes; UP000001422; Chromosome.
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   GO; GO:0015979; P:photosynthesis; 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; Photosynthesis; Zinc.
FT   CHAIN           1..579
FT                   /note="Carboxysome shell carbonic anhydrase"
FT                   /id="PRO_0000452066"
FT   REGION          72..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        242
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O85042"
FT   BINDING         240
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O85042"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O85042"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O85042"
SQ   SEQUENCE   579 AA;  63865 MW;  251CCFB9AD3B5B29 CRC64;
     MVRSMPLRGG RPQAPTAPTR WQLQNTVFAA ESQNQPSASE AVVSSTRDAA LQRRRALTTD
     GKAATLVQGS VGGGRVRSAR DQRQPGWVRR DKGATSGVPF NLSRSSLPIT NRQHPLTDTA
     ANARLRAYEQ EVKGRFDRIV PLLQRVSALQ HEPDFIEQAQ RLTRAELGFD LPQHILERAW
     VRPLDMRALF AWCVFESHRL FSDRFFQDDP LDGAAGSVAA RDFEQFLLDC GIHLLDVSPC
     ADGRLAHTVA YALRIPFSAV RRRSHAGAMF DVENTVNRWV KTEHRRHREG MPNPSTEPTR
     YLKVVTYHFS SLDPQHQGCA AHGSNDELAA AAGHQRLLDF REAVENSFCC GASVDLLLIG
     LDTDTDAIRV HPPSRDSEMV LDQWLCAREL HAATASMTAD QAMAQIAEAI EAGASGPMEP
     GMVAFLTRLI ANNCSQIDYV QDLHGAPYPD AGHAERFIGV GIGFKEVHLR NLTYFAHLDT
     VEEGAPDLDV GVKIFKGLNV SRDLPIPVVV RFDYSGRVPG ARERAIADCQ RVNQAIADRY
     GELVNQGLLH TCLTVRDRNQ TAPAEVVGST LAPPLQEAH