CSOCA_HALNC
ID CSOCA_HALNC Reviewed; 514 AA.
AC O85042; D0KZ89;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Carboxysome shell carbonic anhydrase {ECO:0000303|PubMed:16407248};
DE Short=CsoSCA {ECO:0000303|PubMed:16407248};
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:10816046};
GN Name=csoS3 {ECO:0000303|PubMed:10816046};
GN Synonyms=ORF1 {ECO:0000303|PubMed:9696760}; OrderedLocusNames=Hneap_0919;
OS Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS neapolitanus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Halothiobacillaceae; Halothiobacillus.
OX NCBI_TaxID=555778;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2;
RX PubMed=9696760; DOI=10.1128/jb.180.16.4133-4139.1998;
RA Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.;
RT "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate
RT carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in
RT expression of form II RuBisCO, loss of carboxysomes, and an increased CO2
RT requirement for growth.";
RL J. Bacteriol. 180:4133-4139(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23641 / c2;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Kerfeld C., Cannon G., Heinhort S.;
RT "Complete sequence of Halothiobacillus neapolitanus c2.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=10816046; DOI=10.1007/s002030000141;
RA Baker S.H., Williams D.S., Aldrich H.C., Gambrell A.C., Shively J.M.;
RT "Identification and localization of the carboxysome peptide Csos3 and its
RT corresponding gene in Thiobacillus neapolitanus.";
RL Arch. Microbiol. 173:278-283(2000).
RN [4]
RP FUNCTION AS A CARBONIC ANHYDRASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND SIMILARITY.
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 [5]
RP FUNCTION, PROTEIN ABUNDANCE, AND SUBCELLULAR LOCATION.
RX DOI=10.1007/7171_023;
RA Heinhorst S., Cannon G.C., Shively J.M.;
RT "Carboxysomes and Carboxysome-like Inclusions.";
RL (In) Shively J.M. (eds.);
RL Microbiology Monographs, pp.2:141-164, Springer-Verlag, Berlin (2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND SIMILARITY.
RX PubMed=17012396; DOI=10.1128/jb.00990-06;
RA Heinhorst S., Williams E.B., Cai F., Murin C.D., Shively J.M., Cannon G.C.;
RT "Characterization of the carboxysomal carbonic anhydrase CsoSCA from
RT Halothiobacillus neapolitanus.";
RL J. Bacteriol. 188:8087-8094(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=18258595; DOI=10.1074/jbc.m709285200;
RA Dou Z., Heinhorst S., Williams E.B., Murin C.D., Shively J.M., Cannon G.C.;
RT "CO2 fixation kinetics of Halothiobacillus neapolitanus mutant carboxysomes
RT lacking carbonic anhydrase suggest the shell acts as a diffusional barrier
RT for CO2.";
RL J. Biol. Chem. 283:10377-10384(2008).
RN [8]
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=22184212; DOI=10.1073/pnas.1108557109;
RA Bonacci W., Teng P.K., Afonso B., Niederholtmeyer H., Grob P., Silver P.A.,
RA Savage D.F.;
RT "Modularity of a carbon-fixing protein organelle.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:478-483(2012).
RN [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23641 / c2;
RX PubMed=31406332; DOI=10.1038/s41564-019-0520-8;
RA Desmarais J.J., Flamholz A.I., Blikstad C., Dugan E.J., Laughlin T.G.,
RA Oltrogge L.M., Chen A.W., Wetmore K., Diamond S., Wang J.Y., Savage D.F.;
RT "DABs are inorganic carbon pumps found throughout prokaryotic phyla.";
RL Nat. Microbiol. 4:2204-2215(2019).
RN [10]
RP CARBOXYSOME ASSEMBLY, BIOTECHNOLOGY, AND DISRUPTION PHENOTYPE.
RX PubMed=33116131; DOI=10.1038/s41467-020-19280-0;
RA Li T., Jiang Q., Huang J., Aitchison C.M., Huang F., Yang M., Dykes G.F.,
RA He H.L., Wang Q., Sprick R.S., Cooper A.I., Liu L.N.;
RT "Reprogramming bacterial protein organelles as a nanoreactor for hydrogen
RT production.";
RL Nat. Commun. 11:5448-5448(2020).
RN [11] {ECO:0007744|PDB:2FGY}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ZINC, POSSIBLE
RP REACTION MECHANISM, POSSIBLE ACTIVE SITE, COFACTOR, SUBUNIT, AND
RP SIMILARITY.
RX PubMed=16407248; DOI=10.1074/jbc.m510464200;
RA Sawaya M.R., Cannon G.C., Heinhorst S., Tanaka S., Williams E.B.,
RA Yeates T.O., Kerfeld C.A.;
RT "The structure of beta-carbonic anhydrase from the carboxysomal shell
RT reveals a distinct subclass with one active site for the price of two.";
RL J. Biol. Chem. 281:7546-7555(2006).
CC -!- FUNCTION: Reversible hydration of carbon dioxide (PubMed:14729686,
CC PubMed:17012396, PubMed:18258595). Essential for chemolithotrophic
CC carbon dioxide fixation, supplies CO(2) to RuBisCO (ribulose
CC bisphosphate carboxylase, cbbL-cbbS) in the carboxysome (Probable)
CC (PubMed:18258595). There are estimated to be 40 CsoSCA dimers per
CC carboxysome (Ref.5). {ECO:0000269|PubMed:14729686,
CC ECO:0000269|PubMed:17012396, ECO:0000269|PubMed:18258595,
CC ECO:0000269|Ref.5, ECO:0000305|PubMed:14729686}.
CC -!- FUNCTION: Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form
CC without cargo protein. CsoS2 is essential for Cb formation and is also
CC capable of targeting foreign proteins to the Cb. The Cb shell assembles
CC with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of
CC the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms
CC pseudohexamers that probably control metabolite flux into and out of
CC the shell. {ECO:0000269|PubMed:33116131}.
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|PubMed:17012396};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16407248, ECO:0000269|PubMed:17012396,
CC ECO:0007744|PDB:2FGY};
CC Note=The fourth ligand is a water molecule. Binds 1 Zn(2+) per monomer,
CC in PDB:2FGY a second Zn(2+) is seen, but one of its ligands is an
CC accidentally introduced mutation. {ECO:0000269|PubMed:16407248,
CC ECO:0007744|PDB:2FGY};
CC -!- ACTIVITY REGULATION: Carbonic anhydrase activity is inhibited by
CC ethoxyzolamide, dithiothreitol, cyanide, and divalent metal chelators
CC dipicolinic acid and nitrilotriacetic acid.
CC {ECO:0000269|PubMed:14729686, ECO:0000269|PubMed:17012396}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 mM for CO(2) {ECO:0000269|PubMed:17012396};
CC KM=9.3 mM for hydrogencarbonate {ECO:0000269|PubMed:17012396};
CC Note=kcat is 8.9 x 10(4) sec(-1) for CO(2) hydration at pH 8.0, and
CC 4.6 x 10(4) sec(-1) for hydrogencarbonate dehydration at pH 7.0.
CC {ECO:0000269|PubMed:17012396};
CC pH dependence:
CC Optimum pH is 8.0-8.5 for CO(2) hydration, and pH 6.0 for
CC hydrogencarbonate dehydration. {ECO:0000269|PubMed:17012396};
CC -!- SUBUNIT: Homodimer, may form filaments. {ECO:0000269|PubMed:16407248}.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:10816046,
CC ECO:0000269|PubMed:14729686, ECO:0000269|PubMed:17012396,
CC ECO:0000269|PubMed:18258595}. Note=Coomassie staining of gels and
CC immunogold staining shows this is a minor shell protein
CC (PubMed:10816046, PubMed:14729686). The protein is probably found
CC inside the carboxysome, as its addition to mutant organelles does not
CC complement the deletion (PubMed:18258595). This cyanobacterium makes
CC alpha-type carboxysomes (Ref.5, PubMed:18258595).
CC {ECO:0000269|PubMed:10816046, ECO:0000269|PubMed:14729686,
CC ECO:0000269|PubMed:18258595, ECO:0000269|Ref.5}.
CC -!- DOMAIN: The N-terminal domain is physically isolated from the rest of
CC the protein and may serve to anchor the protein to the carboxysome
CC shell or to RuBisCO; in PDB:2FGY the N-terminal domain binds Zn(2+)
CC which is thought to be non-physiological. The central domain bears the
CC catalytic Zn(2+), while the C-terminal domain is structurally similar
CC to the central catalytic domain but cannot bind Zn(2+).
CC {ECO:0000269|PubMed:16407248}.
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. Loss of CA
CC activity, requires 3.5 X more inorganic carbon for half-maximal CO(2)
CC fixation. Carboxysomes are approximately normal except that ratio of
CC CsoS2A:CsoS2B shifts from 1:1 to 2:1. Required for growth in ambient
CC air (PubMed:31406332). {ECO:0000269|PubMed:18258595,
CC ECO:0000269|PubMed:31406332, ECO:0000269|PubMed:33116131}.
CC -!- BIOTECHNOLOGY: Expression of 10 genes for alpha-carboxysome (Cb)
CC proteins (cbbL-cbbS-csoS2-csoS3-csoS4A-csoS4B-csoS1C-csoS1A-csoS1B-
CC csoS1D) in E.coli generates compartments that resemble Cb, contain
CC RuBisCO and have its catalytic activity, showing it is possible to make
CC artificial, functional Cb using these 10 genes. Cargo proteins can be
CC targeted to these organelles (PubMed:22184212). Artificial Cb assembly
CC in E.coli requires csoS2-csoS4A-csoS4B-csoS1C-csoS1A-csoS1B-csoS1D (but
CC not the gene for carbonic anhydrase, csoS3). Targeting proteins to the
CC organelle requires at least one of the CsoS2 C-repeats; 3 repeats gives
CC the best localization. A nanoreactor of the Cb shell proteins has been
CC engineered which generates H(2) using a ferredoxin-hydrogenase fusion
CC (AC P07839-Q9FYU1) and a flavodoxin/ferredoxin--NADP reductase (AC
CC A0A0K3QZA5) targeted separately to the Cb; the hydrogenase has first to
CC be matured and activated by HydGXEF (AC Q8EAH9, Q8EAH8, Q8EAH7 and
CC Q8EAH6 respectively). Encapsulation increases H(2) production about 20%
CC during anaerobic growth, and over 4-fold more during aerobic growth
CC (PubMed:33116131). {ECO:0000269|PubMed:22184212,
CC ECO:0000269|PubMed:33116131}.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family. CsoSCA
CC subfamily. {ECO:0000305|PubMed:14729686, ECO:0000305|PubMed:16407248,
CC ECO:0000305|PubMed:17012396}.
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DR EMBL; AF038430; AAC32552.1; -; Genomic_DNA.
DR EMBL; CP001801; ACX95762.1; -; Genomic_DNA.
DR RefSeq; WP_012823798.1; NC_013422.1.
DR PDB; 2FGY; X-ray; 2.20 A; A/B=1-514.
DR PDBsum; 2FGY; -.
DR AlphaFoldDB; O85042; -.
DR SMR; O85042; -.
DR STRING; 555778.Hneap_0919; -.
DR EnsemblBacteria; ACX95762; ACX95762; Hneap_0919.
DR KEGG; hna:Hneap_0919; -.
DR eggNOG; ENOG502Z9V7; Bacteria.
DR HOGENOM; CLU_535194_0_0_6; -.
DR OMA; VENSFCC; -.
DR OrthoDB; 300636at2; -.
DR EvolutionaryTrace; O85042; -.
DR Proteomes; UP000009102; 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 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 3D-structure; Bacterial microcompartment; Carbon dioxide fixation;
KW Carboxysome; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..514
FT /note="Carboxysome shell carbonic anhydrase"
FT /id="PRO_0000452062"
FT REGION 1..144
FT /note="N-terminal domain"
FT /evidence="ECO:0000305|PubMed:16407248,
FT ECO:0007744|PDB:2FGY"
FT REGION 151..397
FT /note="Catalytic domain"
FT /evidence="ECO:0000305|PubMed:16407248,
FT ECO:0007744|PDB:2FGY"
FT REGION 398..514
FT /note="C-terminal domain"
FT /evidence="ECO:0000305|PubMed:16407248,
FT ECO:0007744|PDB:2FGY"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:16407248"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16407248,
FT ECO:0007744|PDB:2FGY"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16407248,
FT ECO:0007744|PDB:2FGY"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16407248,
FT ECO:0007744|PDB:2FGY"
FT CONFLICT 14
FT /note="F -> C (in Ref. 1; AAC32552)"
FT CONFLICT 34
FT /note="A -> V (in Ref. 1; AAC32552)"
FT CONFLICT 437
FT /note="K -> T (in Ref. 1; AAC32552)"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 56..74
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2FGY"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 206..223
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 234..243
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2FGY"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 260..281
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:2FGY"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 333..348
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 362..386
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:2FGY"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 429..442
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 450..458
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 465..483
FT /evidence="ECO:0007829|PDB:2FGY"
FT HELIX 485..489
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 493..503
FT /evidence="ECO:0007829|PDB:2FGY"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:2FGY"
SQ SEQUENCE 514 AA; 57336 MW; F2927DB52C5115F0 CRC64;
MNTRNTRSKQ RAPFGVSSSV KPRLDLIEQA PNPAYDRHPA CITLPERTCR HPLTDLEANE
QLGRCEDSVK NRFDRVIPFL QVVAGIPLGL DYVTRVQELA QSSLGHTLPE ELLKDNWISG
HNLKGIFGYA TAKALTAATE QFSRKIMSEK DDSASAIGFF LDCGFHAVDI SPCADGRLKG
LLPYILRLPL TAFTYRKAYA GSMFDIEDDL AQWEKNELRR YREGVPNTAD QPTRYLKIAV
YHFSTSDPTH SGCAAHGSND RAALEAALTQ LMKFREAVEN AHCCGASIDI LLIGVDTDTD
AIRVHIPDSK GFLNPYRYVD NTVTYAQTLH LAPDEARVII HEAILNANRS DGWAKGNGVA
SEGMRRFIGQ LLINNLSQID YVVNRHGGRY PPNDIGHAER YISVGDGFDE VQIRNLAYYA
HLDTVEENAI DVDVGIKIFT KLNLSRGLPI PIAIHYRYDP NVPGSRERTV VKARRIYNAI
KERFSSLDEQ NLLQFRLSVQ AQDIGSPIEE VASA
