ID   CAH2_FLALI              Reviewed;         190 AA.
AC   P46513;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Carbonic anhydrase 2;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase 2;
DE   Flags: Fragment;
OS   Flaveria linearis (Narrowleaf yellowtops).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Tageteae; Flaveria.
OX   NCBI_TaxID=4225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=7579185; DOI=10.1007/bf00043658;
RA   Ludwig M., Burnell J.N.;
RT   "Molecular comparison of carbonic anhydrase from Flaveria species
RT   demonstrating different photosynthetic pathways.";
RL   Plant Mol. Biol. 29:353-365(1995).
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   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: Possesses a transit-like peptide, but it is proposed that this
CC       peptide is not removed and that therefore the enzyme stays in the
CC       cytoplasm instead of going to the chloroplast. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; U19740; AAA86994.1; -; mRNA.
DR   PIR; T10740; T10740.
DR   AlphaFoldDB; P46513; -.
DR   SMR; P46513; -.
DR   GO; GO:0005737; C:cytoplasm; 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   GO; GO:0015976; P:carbon utilization; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Zinc.
FT   CHAIN           <1..190
FT                   /note="Carbonic anhydrase 2"
FT                   /id="PRO_0000077456"
FT   NON_TER         1
SQ   SEQUENCE   190 AA;  20585 MW;  F07686E36A46D782 CRC64;
     NPTLYGELAK GQSPKFLVFA CSDSRVCPSH ILDFQPGEAF VVRNIANMVP PYDTIKHSGA
     GAAIEYAVLH LKVENIVVIG HSCCGGIKGL MSIPDDGTPA SDFIEQWVKL GLPAKSKVKA
     NCNNLEFADL CTKCEKEAVN VSLGNLLTYP FVRDALVNKK LSLKGAHYDF VNGAFDLWNL
     DFGISPSLLQ