ID   CAH1_MONDO              Reviewed;         262 AA.
AC   Q8HY33;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Carbonic anhydrase 1;
DE            EC=4.2.1.1 {ECO:0000250|UniProtKB:P00915};
DE   AltName: Full=Carbonate dehydratase I;
DE   AltName: Full=Carbonic anhydrase I;
DE            Short=CA-I;
GN   Name=CA1;
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Barome P.O.;
RT   "Characterisation of opossum (Monodelphis domestica) carbonic anhydrase I
RT   and alpha globin coding sequences.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide.
CC       {ECO:0000250|UniProtKB:P00915}.
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         Evidence={ECO:0000250|UniProtKB:P00915};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00915};
CC   -!- ACTIVITY REGULATION: Inhibited by acetazolamide. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNN3}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ417908; CAD10681.1; -; mRNA.
DR   RefSeq; NP_001028142.1; NM_001032970.1.
DR   AlphaFoldDB; Q8HY33; -.
DR   SMR; Q8HY33; -.
DR   STRING; 13616.ENSMODP00000007216; -.
DR   Ensembl; ENSMODT00000007364; ENSMODP00000007216; ENSMODG00000005833.
DR   GeneID; 497246; -.
DR   KEGG; mdo:497246; -.
DR   CTD; 759; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000161270; -.
DR   HOGENOM; CLU_039326_2_1_1; -.
DR   InParanoid; Q8HY33; -.
DR   OMA; DYGSEHT; -.
DR   OrthoDB; 1377476at2759; -.
DR   TreeFam; TF316425; -.
DR   Proteomes; UP000002280; Chromosome 3.
DR   Bgee; ENSMODG00000005833; Expressed in blood and 16 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004064; F:arylesterase activity; IEA:Ensembl.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR   Gene3D; 3.10.200.10; -; 1.
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   InterPro; IPR018442; Carbonic_anhydrase_CA1.
DR   PANTHER; PTHR18952; PTHR18952; 1.
DR   PANTHER; PTHR18952:SF82; PTHR18952:SF82; 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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Lyase; Metal-binding; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
FT   CHAIN           2..262
FT                   /note="Carbonic anhydrase 1"
FT                   /id="PRO_0000077412"
FT   DOMAIN          4..261
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        65
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
FT   BINDING         200..201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
SQ   SEQUENCE   262 AA;  29175 MW;  38A217356BCD5C9A CRC64;
     MANLNWSYEG ENGPEHWSKL YPIANGDNQS PIDIKTKEVK HDASLKPISV SYNPATAKEI
     VNVSHNFQVN FEDKDNQSVL KGGPFTGSFR LRQFHFHWGT ADDHGSEHTV DGVKYSSELH
     IVHWNSEKYS SFSEAAEKPD GLAIIAVFIK AGQANPGLQK VIDALSSIKT KGKKAPFANF
     DPSLLIPQSS DYWSYHGSLT HPPLHESVTW IIYREPISAS SEQLAKFRSL LSTAEGEKAS
     SILHNHRLPQ PLKGRQVKAS FK