ID   CAHX_FLABI              Reviewed;         330 AA.
AC   P46510;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Carbonic anhydrase;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase;
OS   Flaveria bidentis (Coastal plain yellowtops) (Ethulia bidentis).
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=4224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=8070567; DOI=10.1016/0014-5793(94)00767-5;
RA   Cavallaro A., Ludwig M., Burnell J.N.;
RT   "The nucleotide sequence of a complementary DNA encoding Flaveria bidentis
RT   carbonic anhydrase.";
RL   FEBS Lett. 350:216-218(1994).
RN   [2]
RP   SEQUENCE REVISION.
RA   Burnell J.N.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- 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.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U08398; AAA86939.2; -; mRNA.
DR   PIR; S48675; S48675.
DR   AlphaFoldDB; P46510; -.
DR   SMR; P46510; -.
DR   BindingDB; P46510; -.
DR   ChEMBL; CHEMBL2401609; -.
DR   DrugCentral; P46510; -.
DR   PRIDE; P46510; -.
DR   BRENDA; 4.2.1.1; 2264.
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..330
FT                   /note="Carbonic anhydrase"
FT                   /id="PRO_0000077453"
FT   REGION          1..109
FT                   /note="Chloroplast transit peptide-like"
SQ   SEQUENCE   330 AA;  35545 MW;  53989F16CE4DF26C CRC64;
     MSAASAFAMN APSFVNASSL KKASTSARSG VLSARFTCNS SSSSSSSATP PSLIRNEPVF
     AAPAPIITPN WTEDGNESYE EAIDALKKTL IEKGELEPVA ATRIDQITAQ AAAPDTKAPF
     DPVERIKSGF VKFKTEKFVT NPALYDELAK GQSPKFMVFA CSDSRVCPSH VLDFQPGEAF
     VVRNVANMVP PFDKTKYSGV GAAVEYAVLH LKVQEIFVIG HSRCGGIKGL MTFPDEGPHS
     TDFIEDWVKV CLPAKSKVVA EHNGTHLDDQ CVLCEKEAVN VSLGNLLTYP FVRDGLRNKT
     LALKGGHYDF VNGTFELWAL DFGLSSPTSV