CYNT_SYNY3
ID CYNT_SYNY3 Reviewed; 274 AA.
AC Q54735; P74088;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Carbonic anhydrase;
DE EC=4.2.1.1 {ECO:0000269|PubMed:9617794};
DE AltName: Full=Carbonate dehydratase;
GN Name=ccaA {ECO:0000303|PubMed:9617794};
GN Synonyms=icfA {ECO:0000303|PubMed:9617794}; OrderedLocusNames=slr1347;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=9617794; DOI=10.1023/a:1005959200390;
RA So A.K.C., Espie G.S.;
RT "Cloning, characterization and expression of carbonic anhydrase from the
RT cyanobacterium Synechocystis PCC6803.";
RL Plant Mol. Biol. 37:205-215(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=11859847; DOI=10.1007/s004250100638;
RA So A.K., John-McKay M., Espie G.S.;
RT "Characterization of a mutant lacking carboxysomal carbonic anhydrase from
RT the cyanobacterium Synechocystis PCC6803.";
RL Planta 214:456-467(2002).
RN [4]
RP FUNCTION.
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CCMM, SUBCELLULAR LOCATION,
RP DOMAIN, AND MUTAGENESIS OF 215-GLN--ARG-274 AND 215-ASP--ARG-274.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=17993516; DOI=10.1128/jb.01283-07;
RA Cot S.S., So A.K., Espie G.S.;
RT "A multiprotein bicarbonate dehydration complex essential to carboxysome
RT function in cyanobacteria.";
RL J. Bacteriol. 190:936-945(2008).
RN [6] {ECO:0007744|PDB:5SWC}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-220 IN COMPLEX WITH ZINC,
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION
RP WITH CCMM, DOMAIN, AND MUTAGENESIS OF 221-PRO--ARG-274.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=27729545; DOI=10.1042/bcj20160773;
RA McGurn L.D., Moazami-Goudarzi M., White S.A., Suwal T., Brar B., Tang J.Q.,
RA Espie G.S., Kimber M.S.;
RT "The structure, kinetics and interactions of the beta-carboxysomal beta-
RT carbonic anhydrase, CcaA.";
RL Biochem. J. 473:4559-4572(2016).
CC -!- FUNCTION: Reversible hydration of carbon dioxide. Essential to
CC photosynthetic carbon dioxide fixation, supplies CO(2) to RuBisCO
CC (ribulose bisphosphate carboxylase, rbcL-rbcS) in the carboxysome.
CC {ECO:0000269|PubMed:11859847, ECO:0000269|PubMed:17993516,
CC ECO:0000269|PubMed:9617794, ECO:0000269|Ref.4}.
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:17993516,
CC ECO:0000269|PubMed:9617794};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:27729545, ECO:0007744|PDB:5SWC};
CC Note=Binds 1 zinc ion per monomer, a water molecule forms the fourth
CC ligand. {ECO:0000269|PubMed:27729545};
CC -!- ACTIVITY REGULATION: Inhibited by ethoxyzolamide.
CC {ECO:0000269|PubMed:9617794}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 3340 sec(-1) for full length enzyme at pH 7.5.
CC {ECO:0000269|PubMed:27729545};
CC -!- SUBUNIT: A hexamer formed by a trimer of dimers. Interacts with the
CC first 260 residues of CcmM; both the N-terminal 206 residues and the C-
CC terminal tail contribute to CcmM binding (PubMed:27729545). Interacts
CC with full-length and the N-terminal 249 residues of CcmM. A probable
CC CcmM-CcaA-CcmN complex as well as a CcaA-RuBisCO-CcmM complex can also
CC be isolated (PubMed:17993516). {ECO:0000269|PubMed:17993516,
CC ECO:0000269|PubMed:27729545}.
CC -!- INTERACTION:
CC Q54735; Q54735: ccaA; NbExp=2; IntAct=EBI-1622341, EBI-1622341;
CC Q54735; P72758: ccmM; NbExp=6; IntAct=EBI-1622341, EBI-862848;
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:11859847,
CC ECO:0000269|PubMed:17993516, ECO:0000269|PubMed:9617794}. Note=This
CC cyanobacterium makes beta-type carboxysomes. Associates with the shell
CC portion of carboxysomes. {ECO:0000269|PubMed:17993516}.
CC -!- DOMAIN: Dimerization, activity and interactions with CcmM requires all
CC but the last 60 amino acids of the protein (PubMed:17993516). The C-
CC terminal tail (about 55 residues) inhibits CA activity about 10-fold;
CC it might attenuate activity before encapsulation in the carboxysome
CC (PubMed:27729545). {ECO:0000269|PubMed:17993516,
CC ECO:0000269|PubMed:27729545}.
CC -!- DISRUPTION PHENOTYPE: Cells do not grow in normal air but do grow on 5%
CC CO(2), called a high-CO(2) requiring phenotype, HCR; even at high CO(2)
CC levels photosynthesis is less effective. Carboxyomes appear wild-type
CC and contain RuBisCO but no longer have a HCO(3)- to CO(2)
CC interconversion activity. Light-dependent CO(2) transport into the cell
CC is unchanged. {ECO:0000269|PubMed:11859847}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305|PubMed:9617794}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA18166.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U45962; AAC46375.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18166.1; ALT_INIT; Genomic_DNA.
DR PIR; S75605; S75605.
DR PDB; 5SWC; X-ray; 1.45 A; A/B/C/D/E/F=1-218.
DR PDBsum; 5SWC; -.
DR AlphaFoldDB; Q54735; -.
DR SMR; Q54735; -.
DR DIP; DIP-40255N; -.
DR IntAct; Q54735; 5.
DR STRING; 1148.1653251; -.
DR PaxDb; Q54735; -.
DR EnsemblBacteria; BAA18166; BAA18166; BAA18166.
DR KEGG; syn:slr1347; -.
DR eggNOG; COG0288; Bacteria.
DR InParanoid; Q54735; -.
DR OMA; PANEIIG; -.
DR PhylomeDB; Q54735; -.
DR BRENDA; 4.2.1.1; 16015.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR CDD; cd00884; beta_CA_cladeB; 1.
DR Gene3D; 3.40.1050.10; -; 1.
DR InterPro; IPR045066; Beta_CA_cladeB.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR11002; PTHR11002; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; SSF53056; 1.
DR PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW Carboxysome; Lyase; Metal-binding; Photosynthesis; Reference proteome;
KW Zinc.
FT CHAIN 1..274
FT /note="Carbonic anhydrase"
FT /id="PRO_0000077464"
FT REGION 214..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27729545,
FT ECO:0007744|PDB:5SWC"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27729545,
FT ECO:0007744|PDB:5SWC"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:27729545,
FT ECO:0007744|PDB:5SWC"
FT MUTAGEN 205..274
FT /note="Missing: Protein has no CA activity, does not
FT dimerize, does not interact with CcmM."
FT /evidence="ECO:0000269|PubMed:17993516"
FT MUTAGEN 215..274
FT /note="Missing: Protein has CA activity, dimerizes and
FT interacts with CcmM."
FT /evidence="ECO:0000269|PubMed:17993516"
FT MUTAGEN 221..274
FT /note="Missing: 10-fold increase in kcat, enzyme loses
FT activity over 20 minutes."
FT /evidence="ECO:0000269|PubMed:27729545"
FT CONFLICT 219
FT /note="P -> L (in Ref. 2; BAA18166)"
FT /evidence="ECO:0000305"
FT HELIX 1..13
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:5SWC"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:5SWC"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:5SWC"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:5SWC"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 143..162
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:5SWC"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:5SWC"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:5SWC"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:5SWC"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:5SWC"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:5SWC"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5SWC"
SQ SEQUENCE 274 AA; 30761 MW; 2F4F634246C0D5A9 CRC64;
MQRLIEGLQK FREGYFSSHR DLFEQLSHGQ HPRILFICCS DSRVDPNLIT QSEVGDLFVI
RNAGNIIPPY GAANGGEGAA MEYALVALEI NQIIVCGHSH CGAMKGLLKL NSLQEKLPLV
YDWLKHTEAT RRLVLDNYSH LEGEDLIEVA VAENILTQLK NLQTYPAIHS RLHRGDLSLH
GWIYRIEEGE VLAYDGVLHD FVAPQSRINA LEPEDEYAPH PNSPLISYDA FKVPGKERPG
REKATESPAP QLSPLPGFGH LPREQAERIY RGSR
