CAH_KLEPN
ID CAH_KLEPN Reviewed; 246 AA.
AC O52535;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Carbonic anhydrase;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase;
DE Flags: Precursor;
GN Name=cah;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9811652; DOI=10.1128/jb.180.22.5932-5946.1998;
RA Beach M.B., Osuna R.;
RT "Identification and characterization of the fis operon in enteric
RT bacteria.";
RL J. Bacteriol. 180:5932-5946(1998).
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AF040380; AAC77887.1; -; Genomic_DNA.
DR AlphaFoldDB; O52535; -.
DR SMR; O52535; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; 1.
DR Gene3D; 3.10.200.10; -; 1.
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; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Lyase; Metal-binding; Periplasm; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..246
FT /note="Carbonic anhydrase"
FT /id="PRO_0000004265"
FT DOMAIN 23..246
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 84
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 197..198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 46..201
FT /evidence="ECO:0000250"
SQ SEQUENCE 246 AA; 27145 MW; A337BC0020A7427A CRC64;
MKTSLGKAAL LALSMMPVTV FASHWSYEGE GSPEHWGALN EEYKTCQNGM NQSPINIDAT
FKTHLSPLDT HYIDGPITLI NNGHTIQAAL KTTTADTITI DGTPFILQQF HFHAPSENTV
HGKHYAMEMH LVHKNAKGAV AVVAVMFEQG AENTELNKLW ATMPEQAEQT AKIVTQMDLN
ALLPIDKTYW RFSGSLTTPP CSEGVTRIVL KHPLTLSSAQ LAKFSHAMHH DNNRPVQPLN
GRVVIE
