CAH_NOSS1
ID CAH_NOSS1 Reviewed; 264 AA.
AC P94170;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Carbonic anhydrase;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase;
DE Flags: Precursor;
GN Name=ecaA; OrderedLocusNames=all2929;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9006032; DOI=10.1128/jb.179.3.769-774.1997;
RA Soltes-Rak E., Mulligan M.E., Coleman J.R.;
RT "Identification and characterization of a gene encoding a vertebrate-type
RT carbonic anhydrase in cyanobacteria.";
RL J. Bacteriol. 179:769-774(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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 -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; U72708; AAC44831.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB74628.1; -; Genomic_DNA.
DR PIR; AB2172; AB2172.
DR RefSeq; WP_010997080.1; NZ_RSCN01000003.1.
DR AlphaFoldDB; P94170; -.
DR SMR; P94170; -.
DR STRING; 103690.17132023; -.
DR EnsemblBacteria; BAB74628; BAB74628; BAB74628.
DR KEGG; ana:all2929; -.
DR eggNOG; COG3338; Bacteria.
DR OMA; RMRMENN; -.
DR OrthoDB; 1572675at2; -.
DR Proteomes; UP000002483; Chromosome.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Lyase; Metal-binding; Reference proteome; Signal; Zinc.
FT SIGNAL 1..33
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 34..264
FT /note="Carbonic anhydrase"
FT /id="PRO_0000004263"
FT DOMAIN 36..264
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 214..215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 264 AA; 29639 MW; 81C10CCD974B4172 CRC64;
MSSTLYRRQL LKLLGMSVLG TSFSSCVTSP ARAKTVNWGY IGKVGPEHWG ELSPDFALCQ
IGRKQTPIDL QIADVKDVHS SSQDLLVTNY QPTALHLINN GKTVQVNYQP GSYLKYAHQK
FELLQFHFHH FSEHRVDGKL YDMELHLVHR SKSGDLAVMG IFLQAGAFNP TLQIIWDATP
QNQGTDKRIE DINIDASQFL PAQHRFFTYS GSLTTPPCSE NVLWCVMATP IEASPAQIAK
FSQMFPQNAR PVQPLNDRLV IEAI
