ID A0A496KSY9_9NEIS Unreviewed; 212 AA. AC A0A496KSY9; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 10-FEB-2021, entry version 8. DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011}; DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011}; DE Flags: Fragment; GN ORFNames=D8H97_11445 {ECO:0000313|EMBL:RKV81747.1}; OS Neisseria sp. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria; unclassified Neisseria. OX NCBI_TaxID=192066 {ECO:0000313|EMBL:RKV81747.1, ECO:0000313|Proteomes:UP000279304}; RN [1] {ECO:0000313|Proteomes:UP000279304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Espinoza J., Harkins D., Torralba M., Gomez A., Highlander S., Jones M., RA Leong P., Saffery R., Bockmann M., Kuelbs C., Inman J., Hughes T., RA Craig J.M., Nelson K.E., Dupont C.; RT "Supragingival plaque microbiome ecology and functional potential in the RT context of health and disease."; RL bioRxivorg 0:0-0(2018). CC -!- FUNCTION: Reversible hydration of carbon dioxide. CC {ECO:0000256|ARBA:ARBA00002904, 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|ARBA:ARBA00000943, CC 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|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:RKV81747.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; RBKF01000528; RKV81747.1; -; Genomic_DNA. DR Proteomes; UP000279304; 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; -; 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 Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU367011}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU367011}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}. FT DOMAIN 1..212 FT /note="Alpha-carbonic anhydrase" FT /evidence="ECO:0000259|PROSITE:PS51144" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:RKV81747.1" SQ SEQUENCE 212 AA; 23765 MW; 0D49B5F17CD113B6 CRC64; PESWGNLSEE FRLCSTGKNQ SPVNITETVS GKLPAIKVNY KPSTVDVENN GHTIQVNYPE GGNTLTVNGR TYTLKQFHFH VPSENQIKGR TFPMEAHFVH LDENKQPLVL AVLYEAGKTN DRLAPIWNVM PMKEGKVNLD KAFDAGTLLP KRLKYYRFAG SLTTPPCTEG VSWLVLKTYD HIDQAQAEKF TRAVGSENNR PVQPLNARVV IE //