CAH_DUNSA
ID CAH_DUNSA Reviewed; 589 AA.
AC P54212;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Carbonic anhydrase;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase;
GN Name=DCA;
OS Dunaliella salina (Green alga) (Protococcus salinus).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Dunaliellaceae; Dunaliella.
OX NCBI_TaxID=3046;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8663366; DOI=10.1074/jbc.271.30.17718;
RA Fisher M., Gokhman I., Pick U., Zamir A.;
RT "A salt-resistant plasma membrane carbonic anhydrase is induced by salt in
RT Dunaliella salina.";
RL J. Biol. Chem. 271:17718-17723(1996).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- INDUCTION: By salt stress.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U53811; AAC49378.1; -; mRNA.
DR PIR; T08466; T08466.
DR AlphaFoldDB; P54212; -.
DR SMR; P54212; -.
DR BRENDA; 4.2.1.1; 2018.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd03124; alpha_CA_prokaryotic_like; 2.
DR Gene3D; 3.10.200.10; -; 2.
DR InterPro; IPR041891; Alpha_CA_prokaryot-like.
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; PTHR18952; 2.
DR Pfam; PF00194; Carb_anhydrase; 2.
DR SMART; SM01057; Carb_anhydrase; 2.
DR SUPFAM; SSF51069; SSF51069; 2.
DR PROSITE; PS00162; ALPHA_CA_1; 2.
DR PROSITE; PS51144; ALPHA_CA_2; 2.
PE 2: Evidence at transcript level;
KW Lyase; Metal-binding; Stress response; Zinc.
FT CHAIN 1..589
FT /note="Carbonic anhydrase"
FT /id="PRO_0000077445"
FT DOMAIN 59..316
FT /note="Alpha-carbonic anhydrase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT DOMAIN 321..585
FT /note="Alpha-carbonic anhydrase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 390..589
FT /note="Catalytic"
FT BINDING 258..259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
SQ SEQUENCE 589 AA; 64258 MW; 0CC2A6F42C121171 CRC64;
MGSRRITLLG ALFAVLAVAI EGRTLLTHNL KAEAAETVDA VSSVVAGSAG RQLLVSEPHD
YNYEKVGFDW TGGVCVNTGT SKQSPINIET DSLAEESERL GTADDTSRLA LKGLLSSSYQ
LTSEVAINLE QDMQFSFNAP DEDLPQLTIG GVVHTFKPVQ IHFHHFASEH AIDGQLYPLE
AHMVMASQND GSDQLAVIGI MYKYGEEDPF LKRLQETAQS NGEAGDKNVE LNSFSINVAR
DLLPESDLTY YGYDGSLTTP GCDERVKWHV FKEARTVSVA QLKVFSEVTL AAHPEATVTN
NRVIQPLNGR KVYEYKGEPN DKYNYVQHGF DWRDNGLDSC AGDVQSPIDI VTSTLQAGSS
RSDVSSVNLM TLNTDAFTLT GNTVNIGQGM QINFGDPPAG DLPVIRIGTR DVTFRPLQVH
WHFFLSEHTV DGVHYPLEAH IVMKDNDNLG DSAGQLAVIG IMYKYGDADP FITDMQKRVS
DKIASGAITY GQSGVSLNNP DDPFNVNIKN NFLPSELGYA GYDGSLTTPP CSEIVKWHVF
LEPRTVSVEQ MEVFADVTLN SNPGATVTTN RMIQPLEGRT VYGYNGAAA
