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Database: UniProt
Entry: E9FX47_DAPPU
LinkDB: E9FX47_DAPPU
Original site: E9FX47_DAPPU 
ID   E9FX47_DAPPU            Unreviewed;       370 AA.
AC   E9FX47;
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=CAA6B {ECO:0000313|EMBL:EFX88008.1};
GN   ORFNames=DAPPUDRAFT_442471 {ECO:0000313|EMBL:EFX88008.1};
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:EFX88008.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX88008.1, 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; GL732526; EFX88008.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9FX47; -.
DR   STRING; 6669.E9FX47; -.
DR   EnsemblMetazoa; EFX88008; EFX88008; DAPPUDRAFT_442471.
DR   KEGG; dpx:DAPPUDRAFT_442471; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   HOGENOM; CLU_039326_2_0_1; -.
DR   InParanoid; E9FX47; -.
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:EFX88008.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW   Signal {ECO:0000256|RuleBase:RU367011};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT   CHAIN           21..370
FT                   /note="Carbonic anhydrase"
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT                   /id="PRO_5025077709"
FT   DOMAIN          53..312
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   REGION          41..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   370 AA;  42427 MW;  CB062589701EF074 CRC64;
     MPRPSVILIV FLVCFRFVTP SSTDDTLEAL PTTAETVKRK YNNYKKPESK PKPSWSHKDP
     DAWPVKYPTC GGKQQSPINI HSNSTVRTTY PNFKFHNYGY IDRMALINNG HSAAYNLPAY
     YPKKKTPHIT GGGMDGIYQF AQIHLHWGSD STKGSEHLVN SKSYPVELHL VHWNVKYGSF
     AEASKYSYDG LAVLTVFAKV VPEDNKYFHP LVEQLGEIVN NGDETIVKKP ISLYDLLPRR
     ISSFYRYFGS VTTPACQELV IWTIFDNPIE ISEKQASRVN KFRSLKDEVG DRMVNNFRPP
     QPVNDRTIFY RSFSVPDIPL SHPPSVNSYS PFSEAYKWSK ATFKNYATRF LGIFDHPYPH
     RYNSCRSRPC
//
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