ID   CAH1_CHIHA              Reviewed;         259 AA.
AC   P83299;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Carbonic anhydrase 1;
DE            EC=4.2.1.1 {ECO:0000269|PubMed:17510781};
DE   AltName: Full=Carbonate dehydratase I;
DE   AltName: Full=Carbonic anhydrase I;
DE            Short=CA-I;
DE   AltName: Full=Ice-CA;
GN   Name=ca1;
OS   Chionodraco hamatus (Antarctic teleost icefish) (Chaenichthys rhinoceratus
OS   hamatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Channichthyidae; Chionodraco.
OX   NCBI_TaxID=36188;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP   ACETYLATION AT ALA-1.
RC   TISSUE=Gill;
RX   PubMed=17510781; DOI=10.1007/s10930-007-9076-1;
RA   Rizzello A., Ciardiello M.A., Acierno R., Carratore V., Verri T.,
RA   di Prisco G., Storelli C., Maffia M.;
RT   "Biochemical characterization of a S-glutathionylated carbonic anhydrase
RT   isolated from gills of the Antarctic icefish Chionodraco hamatus.";
RL   Protein J. 26:335-348(2007).
CC   -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide.
CC       {ECO:0000269|PubMed:17510781}.
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:0000269|PubMed:17510781};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00921};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17510781}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P83299; -.
DR   SMR; P83299; -.
DR   iPTMnet; P83299; -.
DR   BRENDA; 4.2.1.1; 7095.
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   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   PANTHER; PTHR18952; PTHR18952; 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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Lyase; Metal-binding;
KW   Zinc.
FT   CHAIN           1..259
FT                   /note="Carbonic anhydrase 1"
FT                   /id="PRO_0000289146"
FT   DOMAIN          2..258
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        63
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         197..198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:17510781"
SQ   SEQUENCE   259 AA;  28343 MW;  65CEBB8ECC61AB67 CRC64;
     AHAWGYGPTD GPDKWVSNFP IADGPRQSPI DILPGGASYD SGLKPLSLKY DPSNCLEILN
     NGHSFQVTFA DDSDSSTLKE GPISGVYRLK QFHFHWGASN DKGSEHTVAG TKYPAELHLV
     HWNTKYPSFG EAASKPDGLA VVGVFLKIGD ANASLQKVLD AFNDIRAKGK QTSFADFDPS
     TLLPGCLDYW TYDGSLTTPP LLESVTWIVC KEPISVSCEQ MAKFRSLLFS AEGEPECCMV
     DNYRPPQPLK GRHVRASFQ