CSOCA_PROMP
ID CSOCA_PROMP Reviewed; 509 AA.
AC Q7V2C7;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Carboxysome shell carbonic anhydrase {ECO:0000303|PubMed:14729686};
DE Short=CsoSCA {ECO:0000303|PubMed:22155772};
DE EC=4.2.1.1 {ECO:0000269|PubMed:14729686};
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=PMM0553;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
RN [2]
RP FUNCTION AS A CARBONIC ANHYDRASE, AND CATALYTIC ACTIVITY.
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTEIN
RP ABUNDANCE, AND SUBCELLULAR LOCATION.
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=22155772; DOI=10.1128/jb.06444-11;
RA Roberts E.W., Cai F., Kerfeld C.A., Cannon G.C., Heinhorst S.;
RT "Isolation and characterization of the Prochlorococcus carboxysome reveal
RT the presence of the novel shell protein CsoS1D.";
RL J. Bacteriol. 194:787-795(2012).
CC -!- FUNCTION: Reversible hydration of carbon dioxide (PubMed:14729686).
CC Essential for photosynthetic carbon dioxide fixation, supplies CO(2) to
CC RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) in the
CC carboxysome (Probable). There are estimated to be 29 CsoSCA oligomers
CC per carboxysome (PubMed:22155772). {ECO:0000269|PubMed:14729686,
CC ECO:0000269|PubMed:22155772, ECO:0000305|PubMed:14729686}.
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:14729686};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 8700 sec(-1) at pH 8.5, from purified carboxysomes.
CC {ECO:0000269|PubMed:22155772};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O85042}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:22155772}.
CC Note=While the protein is very difficult to identify due to its low
CC abundance, the enzyme activity fractionates with the carboxysome. This
CC cyanobacterium makes alpha-type carboxysomes.
CC {ECO:0000269|PubMed:22155772}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family. CsoSCA
CC subfamily. {ECO:0000305|PubMed:14729686}.
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DR EMBL; BX548174; CAE19012.1; -; Genomic_DNA.
DR RefSeq; WP_011132187.1; NC_005072.1.
DR AlphaFoldDB; Q7V2C7; -.
DR SMR; Q7V2C7; -.
DR STRING; 59919.PMM0553; -.
DR EnsemblBacteria; CAE19012; CAE19012; PMM0553.
DR KEGG; pmm:PMM0553; -.
DR eggNOG; ENOG502Z9V7; Bacteria.
DR HOGENOM; CLU_535194_0_0_3; -.
DR OMA; VENSFCC; -.
DR OrthoDB; 300636at2; -.
DR Proteomes; UP000001026; 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..509
FT /note="Carboxysome shell carbonic anhydrase"
FT /id="PRO_0000452065"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O85042"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O85042"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O85042"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O85042"
SQ SEQUENCE 509 AA; 57306 MW; 74BD99B57056CE56 CRC64;
MPLRGLAKAK NFTLGPTAPM KTFTENVHSQ NNEINNLKKI DKTHNLTNNS QNEKLYKYES
QIKSSFDRIV PTLKEIARIQ HHEDFINTAQ SISKQNLGIN LPTHILDKSW VKPLDMRALY
AWCAFKQHEK LSDNFFENDP LEGSFGSPNA NNFETALLDC GIHLLDITPC SDGRLAHSVA
YVMRIPFSAV RRRSHAGALF DIENTVNRWV KTEHKRYREN NPNEAHEDTR YLKIVTYHFS
SVDPLHQGCA AHGSDDKLAA KEGSEKLLAF KEAVENSFCC GASVDLMLIG LDTDTDSLKI
HLSSSDGKID LENTISSLDI YNSTINFSKD EAEKEICQII SGNSNKVQLK GLDKFVYKLI
VNNISQIDYV KKFHKGSYED IGHAERFIGV GIGFKEVHLR NLTYFAHLDT VEEGAPDLDV
GVKIFTGLNV SQDLPIPIVI RFDYSGKVPG AKERAAKDCY RVNNAISIRY KSLVDKGLLH
TCLTIRDRDN IHSAQIIGMS LDQKTKEAH
