ID E9GSS6_DAPPU Unreviewed; 339 AA.
AC E9GSS6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN Name=CAA7Q {ECO:0000313|EMBL:EFX77528.1};
GN ORFNames=DAPPUDRAFT_442495 {ECO:0000313|EMBL:EFX77528.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX77528.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX77528.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
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; GL732562; EFX77528.1; -; Genomic_DNA.
DR AlphaFoldDB; E9GSS6; -.
DR STRING; 6669.E9GSS6; -.
DR EnsemblMetazoa; EFX77528; EFX77528; DAPPUDRAFT_442495.
DR KEGG; dpx:DAPPUDRAFT_442495; -.
DR eggNOG; KOG0382; Eukaryota.
DR HOGENOM; CLU_039326_2_0_1; -.
DR InParanoid; E9GSS6; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
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:SF259; CARBONIC ANHYDRASE 4; 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, ECO:0000313|EMBL:EFX77528.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT DOMAIN 20..276
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 339 AA; 39452 MW; 40F43AD3628AE5EE CRC64;
MVEKCSLTCQ VYMLSVNFFR IWRPLIASFL SWNEQRSHCG GQHQSPINIE SNKGFLANYP
EFIFHQYDRV FPEILKNDGH TVELKIEEQG EELPFITGGG LGDRYNFVQL HFRWGESVRG
SEHIINGKQY PAEMHIVHYN SKYGNFNDAL TQADGLSVLG VLIELQPWDN IAFRHLEQFD
NIVNPSTTNT DALQFSVPLS ELLPDNTSSF FRYNGQLTTG NCNEDVTWTI FDTPFAISER
QLAKFRLLLI DDNGNRLRQK VRPTQLLHER VVMYPLPRYC PLLPRYDRFI RTEFQSNKSI
CLYSQRFQMY FNQIKQSCKS VDCTVLTPIR LSAPQLLFL
//
