ID A0A1I8G5K4_9PLAT Unreviewed; 336 AA.
AC A0A1I8G5K4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0000818-snap-gene-0.5-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0000818-snap-gene-0.5-mRNA-1, ECO:0000313|WBParaSite:maker-uti_cns_0046045-snap-gene-0.2-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 AlphaFoldDB; A0A1I8G5K4; -.
DR WBParaSite; maker-uti_cns_0000818-snap-gene-0.5-mRNA-1; maker-uti_cns_0000818-snap-gene-0.5-mRNA-1; maker-uti_cns_0000818-snap-gene-0.5.
DR WBParaSite; maker-uti_cns_0046045-snap-gene-0.2-mRNA-1; maker-uti_cns_0046045-snap-gene-0.2-mRNA-1; maker-uti_cns_0046045-snap-gene-0.2.
DR WBParaSite; maker-uti_cns_0046046-snap-gene-0.3-mRNA-1; maker-uti_cns_0046046-snap-gene-0.3-mRNA-1; maker-uti_cns_0046046-snap-gene-0.3.
DR Proteomes; UP000095280; 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 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:SF266; CARBONIC ANHYDRASE 2, ISOFORM A; 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..31
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT CHAIN 32..336
FT /note="Carbonic anhydrase"
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT /id="PRO_5009845611"
FT TRANSMEM 310..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..303
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 336 AA; 36724 MW; C7B027B96A382CE6 CRC64;
TYLQTMASAG SKSWVTMLSL LVAAQLQASL AAGGWDYGKN GPNRWAELFP EFCAGDKQSP
IDLSTQTALQ SSLIRKYVFH QSSIAAGVKF TLKNDGHKIE LNWSPELSIT MGQTAADQMY
TAAQLHWHWG SSDQQGSEHT LDKKSYAAEG HLVFYNSKDY ANISMAASRP NGLAVLGVFY
EVSATDNPLF KDLEKALAND TLINMGGAAE VAARTDFNMF STFLPSNQDE FFRYDGSLTT
PVCYESVLWT VYRQAVPISA RQLQMLRRLH YSDNSSMVNN FRPPLPLNPG NRPGTPRTLY
RTFSAGAAGL APSALSTVGL ILAALLAGRL FVAVEL
//
