ID A0A1J1LV16_9CYAN Unreviewed; 234 AA.
AC A0A1J1LV16;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 02-APR-2025, entry version 24.
DE RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN ORFNames=PL921480172 {ECO:0000313|EMBL:CUR36062.1};
OS Planktothrix tepida PCC 9214.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=671072 {ECO:0000313|EMBL:CUR36062.1, ECO:0000313|Proteomes:UP000184315};
RN [1] {ECO:0000313|Proteomes:UP000184315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Regsiter A., william w.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogencarbonate + H(+) = 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|ARBA:ARBA00048348};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601765-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601765-1};
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217}.
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DR EMBL; CZDF01000188; CUR36062.1; -; Genomic_DNA.
DR RefSeq; WP_072717182.1; NZ_LN889764.1.
DR AlphaFoldDB; A0A1J1LV16; -.
DR STRING; 671072.PL921480172; -.
DR OrthoDB; 9797527at2; -.
DR Proteomes; UP000184315; Unassembled WGS sequence.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd03378; beta_CA_cladeC; 1.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR11002:SF76; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601765-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184315};
KW Zinc {ECO:0000256|PIRSR:PIRSR601765-1}.
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR601765-1"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR601765-1"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR601765-1"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR601765-1"
SQ SEQUENCE 234 AA; 24752 MW; 578FEAD91BA49CBB CRC64;
MSGIQNNLNV SRRNLLKFGA AAAGTAALTV GLGTKANWLK QKPAIAGNNI TPDEALNQLL
DGNKRFVENK RKNPNQSMAR IQEVAQGQTP FAAILSCADS RVPSEIIFDQ GFGDLFVVRN
AGNIATPEEI GSLEFGTLVL GAKVLMVIGH KNCGAVKATI DGKAVPGQIG SIIDVIKPAI
KMNQTLEENI ISNVKSGMGR LKASPVISQL IKEGKLKIVG GYYDLDTGMV KVVA
//