ID A0A401ILZ0_APHSA Unreviewed; 256 AA.
AC A0A401ILZ0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00014628, ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
GN ORFNames=AsFPU1_3671 {ECO:0000313|EMBL:GBF82243.1};
OS Aphanothece sacrum FPU1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=1920663 {ECO:0000313|EMBL:GBF82243.1, ECO:0000313|Proteomes:UP000287247};
RN [1] {ECO:0000313|Proteomes:UP000287247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FPU1 {ECO:0000313|Proteomes:UP000287247};
RA Kanesaki Y., Yoshikawa S., Ohki K.;
RT "Physiological properties and genetic analysis related to exopolysaccharide
RT production of fresh-water unicellular cyanobacterium Aphanothece sacrum,
RT Suizenji Nori, that has been cultured as a food source in Japan.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU367011};
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBF82243.1}.
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DR EMBL; BDQK01000016; GBF82243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401ILZ0; -.
DR OrthoDB; 5327615at2; -.
DR Proteomes; UP000287247; Unassembled WGS sequence.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 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; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF265; CARBONIC ANHYDRASE; 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU367011};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000287247};
KW Signal {ECO:0000256|RuleBase:RU367011};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT CHAIN 29..256
FT /note="Carbonic anhydrase"
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT /id="PRO_5025097451"
FT DOMAIN 36..256
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 256 AA; 29034 MW; 40B301FF812842B9 CRC64;
MKRRTLITSI PIGLAATTFS LSYPSLMAAI AGEKHAEWGY NNSEHWGDLA QDYAACKIGN
EQSPIDLRSA IKSELQPIEI SYQNIPLRLI NNGHTIQVNS NPGNYLILDQ TKFELLQFHF
HHPSEHTITG EKYPMEIHFV HKNEQGLLAV VGVFLKEGAE NKILEPIWKA MPNHKSSEKI
IKEVALSMTE LLPTNSNSYR YFGSLTTPPC SEIVNWVVFQ EPIEISSAQI NQFRQIFPLN
ARPIQPLNRR FLLTSI
//
