ID A0A2B4RAU6_STYPI Unreviewed; 358 AA.
AC A0A2B4RAU6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN Name=cahz {ECO:0000313|EMBL:PFX13487.1};
GN ORFNames=AWC38_SpisGene22426 {ECO:0000313|EMBL:PFX13487.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX13487.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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|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:PFX13487.1}.
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DR EMBL; LSMT01000965; PFX13487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4RAU6; -.
DR STRING; 50429.A0A2B4RAU6; -.
DR EnsemblMetazoa; XM_022953268.1; XP_022809003.1; LOC111345980.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd00326; alpha_CA; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
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:SF266; CARBONIC ANHYDRASE 2, ISOFORM A; 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|RuleBase:RU367011}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT TRANSMEM 48..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..322
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 358 AA; 38971 MW; 145C41D25D8DFE77 CRC64;
MHLIHELIGM TNHFQDIYLI GFIDSSGSFI NVTDVLKRGK NKQNQQTMAK FLFLAFIGLT
GISIGLGTDS WSYCSNCADG PLRWTGDCAS GKSQSPIDIS LANATYKSFS AWNWKNYGST
LSTKFTQQNT GSALQVNLPD KKFFVSGGGL VGNYTTAQFH LHWGPDNGQG SEHTLNGEQF
AAEIHFVSYN VKYPNLTYAA AQPDGLAVLG VFIEVGSANS AYDKFLKYTS KVVNGNTTAS
IAPFPLSPLF PSNTSKFYRY QGSLTTPGCL ESVTWTVFHD SVKISASQVA AMRSLMMNDT
DYIGLNYRPT QALNTRTVYA SFDVSPTTET PTVDDSAAGV KMTTSLLLLM LIGALFLN
//
