ID A0A3B4CWX5_PYGNA Unreviewed; 379 AA.
AC A0A3B4CWX5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000015039.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000015039.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000256|RuleBase:RU367011}.
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:0000256|RuleBase:RU367011};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU367011};
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR RefSeq; XP_017552723.1; XM_017697234.1.
DR AlphaFoldDB; A0A3B4CWX5; -.
DR STRING; 42514.ENSPNAP00000015039; -.
DR Ensembl; ENSPNAT00000023125.1; ENSPNAP00000015039.1; ENSPNAG00000021022.1.
DR GeneID; 108427237; -.
DR CTD; 768; -.
DR GeneTree; ENSGT00940000156893; -.
DR OMA; MNFRATQ; -.
DR OrthoDB; 49814at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 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; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF282; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU367011}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011}; Signal {ECO:0000256|RuleBase:RU367011};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT CHAIN 18..379
FT /note="Carbonic anhydrase"
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT /id="PRO_5025096503"
FT TRANSMEM 331..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..297
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT REGION 18..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 42563 MW; 0C58E356D550FE31 CRC64;
MLLKLIILLL IQNQVQAGKV PSSSSEEDGS SEHDDEEHDR SSSHEHHWGY HDQEAWMSSF
QDCSGKSQSP IDIETSKAIY DPNLNLIELE GYDLTGGPHL TLLNNGHTLL LALPNTMRIV
RGFDEVYLAA QLHFHWGTIE VPGSEHTIDK VHFPAEIHMV HYNSKYANMS EAANKPDGLA
VLGGFIGIGL HENENYEKIL SALTDVSIEE SNTQIPSFNV RHLLPNNLER FYRYNGSLTT
PPCFQTVNWT MFNDTITVSR KQLAALENTL KAGQNQHLSK NFRAPQLLHG RRVLSSFSSS
PSVDNRNVDV PLETEPFKRS GALGELSRGD ILAIAFGVLF AVTLLVFSMY AYQQRKKHSK
LKKDSRQNVI YKPGTKEEV
//
