ID A0A0V0V572_9BILA Unreviewed; 363 AA.
AC A0A0V0V572;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
DE Flags: Fragment;
GN ORFNames=T09_11309 {ECO:0000313|EMBL:KRX58131.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX58131.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX58131.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX58131.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX58131.1}.
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DR EMBL; JYDN01000090; KRX58131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0V572; -.
DR STRING; 181606.A0A0V0V572; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd00326; alpha_CA; 1.
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:SF268; AGAP002359-PA; 1.
DR PANTHER; PTHR18952; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT DOMAIN 61..328
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX58131.1"
SQ SEQUENCE 363 AA; 41762 MW; 8D4E80FD8D0EF6CF CRC64;
LFVNCIVQLR CNFESAEFFS SPQTTLPSIF ILALLIAPGY LMDLKLIIFY SLIFQFYVQS
LEWDYDGIHT GPANWSRIAS PLCAGKQQSP IQIWPNDMKI ALVPRDLSPF DFHNLDNLIT
DAVIENNGHS VQVSIPEKFN ITVKGGPLEY EYQLRQFHFH WAAVNDLGSE HTIGSSHYPL
EAHFVHTCEV PINGSSSFAS RIAVLAVFFE LVSDPSVPQT TPLSSFASYI KQCTFKNDRH
ILKEDFEIQN FYPADPNSYM FYKGSLTTPP CTEDVSWVLF THPMPVTIDE LNSFRELHAN
RRREGEKWLQ RNFRPTQPLY GRQVLFVQQD LHSYKKSNDA TTYDKRFLNI SIIFALLATY
FNF
//
