CSOCA_PROMM
ID CSOCA_PROMM Reviewed; 514 AA.
AC Q7V6G1;
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};
DE AltName: Full=Carbonic anhydrase {ECO:0000303|PubMed:14729686};
DE Short=CA {ECO:0000303|PubMed:14729686};
DE AltName: Full=Carboxysome shell protein CsoS3;
GN Name=csoS3 {ECO:0000303|PubMed:14729686}; OrderedLocusNames=PMT_1202;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
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=MIT 9313;
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).
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). {ECO:0000269|PubMed:14729686,
CC 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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O85042}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000305|PubMed:14729686}.
CC Note=This cyanobacterium makes alpha-type carboxysomes. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family. CsoSCA
CC subfamily. {ECO:0000305|PubMed:14729686}.
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DR EMBL; BX548175; CAE21377.1; -; Genomic_DNA.
DR RefSeq; WP_011130573.1; NC_005071.1.
DR AlphaFoldDB; Q7V6G1; -.
DR SMR; Q7V6G1; -.
DR STRING; 74547.PMT_1202; -.
DR EnsemblBacteria; CAE21377; CAE21377; PMT_1202.
DR KEGG; pmt:PMT_1202; -.
DR eggNOG; ENOG502Z9V7; Bacteria.
DR HOGENOM; CLU_535194_0_0_3; -.
DR OMA; VENSFCC; -.
DR OrthoDB; 300636at2; -.
DR Proteomes; UP000001423; 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; Reference proteome; Zinc.
FT CHAIN 1..514
FT /note="Carboxysome shell carbonic anhydrase"
FT /id="PRO_0000452064"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O85042"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O85042"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O85042"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O85042"
SQ SEQUENCE 514 AA; 57266 MW; C30AA06C1D55D55F CRC64;
MAYRNRNLAS QTQRPLAPTA PRRRPVVTPQ ISDRSRLRGF ANVGSGPCHP LTDRAANQHL
QTYEANVKGS FELIVPFLKR ISALQHDQDF VSKCQSLARS ELGFDLPSHL LEQAWVRALD
MRALFAWCVF QSHQHVSDHF FQEDPLQGGE GSIQAKHFQS FLVDCGFHLL DVSPCADGRL
AHTIAYALRI PFSSVRRRSH AGALFDVEKT VNRWIKTEHR RYREGVPNSA DSPTRYLKVV
TYHFSSLDPS HQGCAAHGSD DALAASAGQQ RLLDFRESVE NSFCCGASVD LLLIGLDTDT
DAIRVHVPAA DGSIVLDEWL SAEDLYHETL SLTSDEAMQH IAERVEAIAP KKPDEGMVAF
IVKLIANNFS QIDYVKQSHA GPYPDAGHAE RFIGVGIGFK EVHLRNLTYF AHLDTVEVGA
PDLDVGVKIF KGLNVSRDLP IPVVVRFDYS GQVPGARDRA VTDCYRVNQA IAERYSELFD
QGLLHTFLTI RDRDKKDTSE VVGSSLEPVH QEAH
