ID   CAH1_FLALI              Reviewed;         330 AA.
AC   P46512;
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 1;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase 1;
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; U19738; AAA86993.1; -; mRNA.
DR   PIR; S61883; S61883.
DR   AlphaFoldDB; P46512; -.
DR   SMR; P46512; -.
DR   PRIDE; P46512; -.
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 1"
FT                   /id="PRO_0000077455"
FT   REGION          1..109
FT                   /note="Chloroplast transit peptide-like"
SQ   SEQUENCE   330 AA;  35574 MW;  2B71061E73C7E7CD CRC64;
     MSTASAFAIN APSFVNASSL KKSSTSSARS GVLSARFTCN SSSSSSSATP PSLIRNEPVF
     AAPAPIITPN WTEDGNESYE EAIDALKKML IEKGELEPVA AARIDQITAQ AAAPDTKAPF
     DPVERIKSGF VKFKTEKFVT NPALYDELAK GQSPKFMVFA CSDSRVCPSH VLDFQPGEAF
     VVRNVANMVP PFDKTKYSGV GAAVEYAVLH LKVQEIFVIG HSRCGGIKGL MTFPDEGPHS
     TDFIEDWVKV CLPAKSKVVA EHNGTHLDDQ CVQCEKEAVN VSLGNLLTYP FVRDGLRNNT
     LALKGGHYDF VNGTFELWAL DFGLSSPTSV