CAH2_CHLRE
ID CAH2_CHLRE Reviewed; 380 AA.
AC P24258;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Carbonic anhydrase 2;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase 2;
DE Short=CA2;
DE Contains:
DE RecName: Full=Carbonic anhydrase 2 large chain;
DE Contains:
DE RecName: Full=Carbonic anhydrase 2 small chain;
DE Flags: Precursor;
GN Name=CAH2;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IAM C-9;
RX PubMed=2243800; DOI=10.1093/nar/18.21.6441;
RA Fukuzawa H., Fujiwara S., Tachiki A., Miyachi S.;
RT "Nucleotide sequences of two genes CAH1 and CAH2 which encode carbonic
RT anhydrase polypeptides in Chlamydomonas reinhardtii.";
RL Nucleic Acids Res. 18:6441-6442(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=2124702; DOI=10.1073/pnas.87.24.9779;
RA Fujiwara S., Fukuzawa H., Tachiki A., Miyachi S.;
RT "Structure and differential expression of two genes encoding carbonic
RT anhydrase in Chlamydomonas reinhardtii.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9779-9783(1990).
RN [3]
RP PROTEIN SEQUENCE OF 21-41 AND 344-363.
RX PubMed=1903396; DOI=10.1016/s0021-9258(18)92880-2;
RA Rawat M., Moroney J.V.;
RT "Partial characterization of a new isoenzyme of carbonic anhydrase isolated
RT from Chlamydomonas reinhardtii.";
RL J. Biol. Chem. 266:9719-9723(1991).
RN [4]
RP PROTEIN SEQUENCE OF 21-41 AND 344-364, AND CHARACTERIZATION.
RX PubMed=1368343; DOI=10.1271/bbb.56.794;
RA Tachiki A., Fukuzawa H., Miyachi S.;
RT "Characterization of carbonic anhydrase isozyme CA2, which is the CAH2 gene
RT product, in Chlamydomonas reinhardtii.";
RL Biosci. Biotechnol. Biochem. 56:794-798(1992).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC -!- SUBUNIT: Tetramer of two large and two small subunits linked by two
CC disulfide bonds.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: Expressed under high-CO2 condition.
CC {ECO:0000269|PubMed:2124702}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; X54488; CAA38360.1; -; Genomic_DNA.
DR PIR; S14188; S14188.
DR RefSeq; XP_001692290.1; XM_001692238.1.
DR AlphaFoldDB; P24258; -.
DR SMR; P24258; -.
DR STRING; 3055.EDP04240; -.
DR EnsemblPlants; PNW84146; PNW84146; CHLRE_04g223050v5.
DR GeneID; 5717780; -.
DR Gramene; PNW84146; PNW84146; CHLRE_04g223050v5.
DR KEGG; cre:CHLRE_04g223050v5; -.
DR eggNOG; KOG0382; Eukaryota.
DR HOGENOM; CLU_728358_0_0_1; -.
DR OMA; CNSTETD; -.
DR OrthoDB; 1377476at2759; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Lyase;
KW Metal-binding; Periplasm; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1368343,
FT ECO:0000269|PubMed:1903396"
FT CHAIN 21..380
FT /note="Carbonic anhydrase 2"
FT /id="PRO_0000004260"
FT CHAIN 21..?343
FT /note="Carbonic anhydrase 2 large chain"
FT /id="PRO_0000004261"
FT CHAIN 344..380
FT /note="Carbonic anhydrase 2 small chain"
FT /id="PRO_0000004262"
FT DOMAIN 38..322
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 112
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 260..261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 61..264
FT /evidence="ECO:0000250"
FT DISULFID 194..198
FT /evidence="ECO:0000250"
FT DISULFID 296..354
FT /note="Interchain (between large and small chains)"
FT /evidence="ECO:0000250"
FT CONFLICT 220..225
FT /note="Missing (in Ref. 1; CAA38360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42172 MW; 5ABC3823A1DD7862 CRC64;
MARTGALLLA ALALAGCAQA CIYKFGTSPD SKATHTGDHW DHSLNGENWE GKDGAGNPWV
CKTGRKQSPI NVPQYHVLDG KGSKIATGLQ TQWSYPDLMS NGSSVQVINN GHTIQVQWTY
DYAGHATIAI PAMRNQSNRI VDVLEMRPND ASDRVTAVPT QFHFHSTSEH LLAGKIFPLE
LHIVHKVTDK LEACKGGCFS VTGILFQLDN GPDNELLEPI FANMPTREGT FTNLPAGTTI
KLGELLPSDR DYVTYEGSLT TPPCSEGLLW HVMTQPQRIS FGQWNRYRLA VGEKECNSTE
TDAAHADAGH HHHHHRRLLH NHAHLEEVPA ATSEPKHYFR RVMEETENPD AYTCTTVAFG
QNFRNAQYAN GRTIKLARYE
