ID   A0A0N4UI07_DRAME        Unreviewed;       299 AA.
AC   A0A0N4UI07;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN   ORFNames=DME_LOCUS1688 {ECO:0000313|EMBL:VDN51715.1};
OS   Dracunculus medinensis (Guinea worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX   NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000721701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:DME_0000721701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN51715.1, ECO:0000313|Proteomes:UP000274756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; UYYG01000028; VDN51715.1; -; Genomic_DNA.
DR   STRING; 318479.A0A0N4UI07; -.
DR   WBParaSite; DME_0000721701-mRNA-1; DME_0000721701-mRNA-1; DME_0000721701.
DR   Proteomes; UP000038040; Unplaced.
DR   Proteomes; UP000274756; 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; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF250; CARBONIC ANHYDRASE 5-RELATED; 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:UP000274756};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT   DOMAIN          80..299
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   299 AA;  33882 MW;  B7C5FD23C8DC1795 CRC64;
     MSYYMQLRTQ DTPHPRQKTI SKSNRANCEL GGNKVASCSI VQDNFKPRDS RLQVALCVYD
     EYERDLLLSS ICNASASYDI NFGYEEDDGP HKWPGVCNTG ARQSPIDISS SAIVVENLPR
     IHFVHYAHAG ELHVENNGLT LIGKGFEQWN QNQPYIYGGD LNGKYFLHQF HLHWGQTNYT
     GSEHTIASLH YPAEMHFVHI KGGKNLSEPF LENDSIAVVA IFVKLGIDEN NFQPLEAYIR
     NITEPESELE VPNFRLIHFL PRDLETFYRY DGSLTTPPCS EAVIWTIMAD PITISASQV
//