ID   CAHX_FLAPR              Reviewed;         329 AA.
AC   P46281;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   05-FEB-2025, entry version 88.
DE   RecName: Full=Carbonic anhydrase;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase;
OS   Flaveria pringlei.
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=4226;
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=hydrogencarbonate + H(+) = 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; U19737; AAA86992.1; -; mRNA.
DR   PIR; S61884; S61884.
DR   AlphaFoldDB; P46281; -.
DR   SMR; P46281; -.
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   FunFam; 3.40.1050.10:FF:000002; Carbonic anhydrase; 1.
DR   Gene3D; 3.40.1050.10; Carbonic anhydrase; 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:SF56; BETA CARBONIC ANHYDRASE 2, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 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..329
FT                   /note="Carbonic anhydrase"
FT                   /id="PRO_0000077457"
FT   REGION          1..108
FT                   /note="Chloroplast transit peptide-like"
SQ   SEQUENCE   329 AA;  35486 MW;  B18E656B1E84C34B CRC64;
     MSTASAFAIN APSFVNASSL KKSSSSARSG VLSARFTCNS SSSSSSATPP SLIRNEPVFA
     APAPIITPNW TEDGNESYEE AIDALKKMLI EKGELEPVAA ARIDQITAQA AAPDTKAPFD
     PVERIKSGFV KFKTEKFVTN PVLYDELAKG QSPKFMVFAC SDSRVCPSHV LDFQPGEAFV
     VRNVANMVPP FDKTKYSGVG AAVEYAVLHL KVQEIFVIGH SRCGGIKGLM TFPDEGPHST
     DFIEDWVKVC LPAKSKVVAE HNGTHLDDQC VLCEKEAVNV SLGNLLTYPF VRDGLRNNTL
     ALKGGHYDFV NGTFELWALD FGLSSPTSV
//