CYNT_SYNE7
ID CYNT_SYNE7 Reviewed; 272 AA.
AC P27134; Q31N92;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Carbonic anhydrase {ECO:0000303|PubMed:1584776};
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:Q54735};
DE AltName: Full=Carbonate dehydratase;
GN Name=ccaA {ECO:0000303|PubMed:17675289};
GN Synonyms=icfA {ECO:0000303|PubMed:1584776};
GN OrderedLocusNames=Synpcc7942_1447;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=1584776; DOI=10.1073/pnas.89.10.4437;
RA Fukuzawa H., Suzuki E., Komukai Y., Miyachi S.;
RT "A gene homologous to chloroplast carbonic anhydrase (icfA) is essential to
RT photosynthetic carbon dioxide fixation by Synechococcus PCC7942.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4437-4441(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH CCMM, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=17675289; DOI=10.1074/jbc.m703896200;
RA Long B.M., Badger M.R., Whitney S.M., Price G.D.;
RT "Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple
RT Rubisco complexes with carboxysomal proteins CcmM and CcaA.";
RL J. Biol. Chem. 282:29323-29335(2007).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=20304968; DOI=10.1104/pp.110.154948;
RA Long B.M., Tucker L., Badger M.R., Price G.D.;
RT "Functional cyanobacterial beta-carboxysomes have an absolute requirement
RT for both long and short forms of the CcmM protein.";
RL Plant Physiol. 153:285-293(2010).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=22928045; DOI=10.1371/journal.pone.0043871;
RA Rae B.D., Long B.M., Badger M.R., Price G.D.;
RT "Structural determinants of the outer shell of beta-carboxysomes in
RT Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL.";
RL PLoS ONE 7:e43871-e43871(2012).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=24585024; DOI=10.1007/s11120-014-9986-7;
RA Nishimura T., Yamaguchi O., Takatani N., Maeda S., Omata T.;
RT "In vitro and in vivo analyses of the role of the carboxysomal beta-type
RT carbonic anhydrase of the cyanobacterium Synechococcus elongatus in
RT carboxylation of ribulose-1,5-bisphosphate.";
RL Photosyn. Res. 121:151-157(2014).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=28616951; DOI=10.1039/c7nr02524f;
RA Faulkner M., Rodriguez-Ramos J., Dykes G.F., Owen S.V., Casella S.,
RA Simpson D.M., Beynon R.J., Liu L.N.;
RT "Direct characterization of the native structure and mechanics of
RT cyanobacterial carboxysomes.";
RL Nanoscale 9:10662-10673(2017).
RN [8]
RP BIOTECHNOLOGY.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=29922315; DOI=10.3389/fpls.2018.00739;
RA Fang Y., Huang F., Faulkner M., Jiang Q., Dykes G.F., Yang M., Liu L.N.;
RT "Engineering and Modulating Functional Cyanobacterial CO2-Fixing
RT Organelles.";
RL Front. Plant Sci. 9:739-739(2018).
RN [9]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=31048338; DOI=10.1105/tpc.18.00787;
RA Sun Y., Wollman A.J.M., Huang F., Leake M.C., Liu L.N.;
RT "Single-Organelle Quantification Reveals Stoichiometric and Structural
RT Variability of Carboxysomes Dependent on the Environment.";
RL Plant Cell 31:1648-1664(2019).
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 (Probable). Loss of activity results in limitation of CO(2)
CC availability to RuBisCO located in the cytoplasm (PubMed:24585024).
CC {ECO:0000269|PubMed:24585024, ECO:0000305|PubMed:1584776}.
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:0000250|UniProtKB:Q54735};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q54735};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000250|UniProtKB:Q54735};
CC -!- SUBUNIT: A hexamer formed by a trimer of dimers (By similarity).
CC Purified from carboxysomes with the both RuBisCO subunits and the full-
CC length form of CcmM, probably interacts with the N-terminus of CcmM
CC (PubMed:17675289). {ECO:0000250|UniProtKB:Q54735,
CC ECO:0000269|PubMed:17675289}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:17675289,
CC ECO:0000269|PubMed:20304968, ECO:0000269|PubMed:22928045,
CC ECO:0000269|PubMed:28616951, ECO:0000269|PubMed:31048338}. Note=This
CC cyanobacterium makes beta-type carboxysomes (PubMed:22928045).
CC Associates with the shell portion of carboxysomes (By similarity).
CC {ECO:0000250|UniProtKB:Q54735, ECO:0000269|PubMed:22928045}.
CC -!- INDUCTION: Carboxysome size and components vary with growth conditions.
CC When grown in ambient air at medium light (50 uE meter(-2) second(-1))
CC there are 14 units of this protein per carboxysome, the numbers
CC decrease slightly under low light, and increase under high light and
CC high CO(2) (at protein level). {ECO:0000269|PubMed:31048338}.
CC -!- DISRUPTION PHENOTYPE: Essential for photosynthetic CO(2) fixation,
CC cells do not grow in normal air, but will grow in 5% CO(2), called a
CC high-CO(2) requiring phenotype, HCR (PubMed:1584776). Cells do not grow
CC in 2% CO(2), and grow more slowly than wild-type at 5% CO(2). 70%
CC reduction in the efficiency of RuBisCO carboxylation activity from
CC isolated carboxysomes; there is probably considerable oxygenation of
CC the substrate (PubMed:24585024). {ECO:0000269|PubMed:1584776,
CC ECO:0000269|PubMed:24585024}.
CC -!- BIOTECHNOLOGY: Heterologous expression of 12 carboxysomal genes in
CC E.coli (ccaA, ccmK2, ccmK3, ccmK4, ccmL, ccmM, ccmN, ccmO, ccmP, rbcL,
CC rbcS, rbcX) leads to the formation of bodies that resemble
CC carboxysomes, have densely packed paracrystalline arrays and RuBisCO
CC activity. These structures open the door to generating carboxysomes in
CC plant cells to increase their photosynthesis and productivity, as well
CC as tailoring bacterial microcompartments to specific metabolic needs
CC and molecule delivery. The absence of ccaA, ccmK3, ccmK4, ccmP and rbcX
CC leads to less active RuBisCO. {ECO:0000269|PubMed:29922315}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; M77095; AAA27315.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57477.1; -; Genomic_DNA.
DR PIR; S28795; S28795.
DR RefSeq; WP_011378036.1; NC_007604.1.
DR PDB; 7O54; X-ray; 1.63 A; B=256-272.
DR PDBsum; 7O54; -.
DR AlphaFoldDB; P27134; -.
DR SMR; P27134; -.
DR STRING; 1140.Synpcc7942_1447; -.
DR PRIDE; P27134; -.
DR EnsemblBacteria; ABB57477; ABB57477; Synpcc7942_1447.
DR KEGG; syf:Synpcc7942_1447; -.
DR eggNOG; COG0288; Bacteria.
DR HOGENOM; CLU_053879_5_3_3; -.
DR OMA; PANEIIG; -.
DR OrthoDB; 1841447at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1447-MON; -.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; IMP:UniProtKB.
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; Zinc.
FT CHAIN 1..272
FT /note="Carbonic anhydrase"
FT /id="PRO_0000077463"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q54735"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q54735"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q54735"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:7O54"
SQ SEQUENCE 272 AA; 30185 MW; ACB30A5F16868C93 CRC64;
MRKLIEGLRH FRTSYYPSHR DLFEQFAKGQ HPRVLFITCS DSRIDPNLIT QSGMGELFVI
RNAGNLIPPF GAANGGEGAS IEYAIAALNI EHVVVCGHSH CGAMKGLLKL NQLQEDMPLV
YDWLQHAQAT RRLVLDNYSG YETDDLVEIL VAENVLTQIE NLKTYPIVRS RLFQGKLQIF
GWIYEVESGE VLQISRTSSD DTGIDECPVR LPGSQEKAIL GRCVVPLTEE VAVAPPEPEP
VIAAVAAPPA NYSSRGWLAP EQQQRIYRGN AS
