ID CAH_NEIGO Reviewed; 252 AA. AC Q50940; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 2. DT 28-JUN-2023, entry version 129. DE RecName: Full=Carbonic anhydrase; DE EC=4.2.1.1; DE AltName: Full=Carbonate dehydratase; DE Flags: Precursor; GN Name=cah; OS Neisseria gonorrhoeae. OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=485; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RX PubMed=9108244; DOI=10.1111/j.1432-1033.1997.00755.x; RA Chirica L.C., Elleby B., Jonsson B.-H., Lindskog S.; RT "The complete sequence, expression in Escherichia coli, purification and RT some properties of carbonic anhydrase from Neisseria gonorrhoeae."; RL Eur. J. Biochem. 244:755-760(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-252. RC STRAIN=MS11; RX PubMed=7721686; DOI=10.1128/jb.177.8.1952-1958.1995; RA Black C.G., Fyfe J.A.M., Davies J.K.; RT "A promoter associated with the neisserial repeat can be used to transcribe RT the uvrB gene from Neisseria gonorrhoeae."; RL J. Bacteriol. 177:1952-1958(1995). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-252 IN COMPLEX WITH TINC ION RP AND INHIBITOR ACETAZOLAMIDE, COFACTOR, AND DISULFIDE BOND. RX PubMed=9761692; DOI=10.1006/jmbi.1998.2077; RA Huang S., Xue Y., Sauer-Eriksson E., Chirica L., Lindskog S., RA Jonsson B.-H.; RT "Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its RT complex with the inhibitor acetazolamide."; RL J. Mol. Biol. 283:301-310(1998). 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; CC Evidence={ECO:0000269|PubMed:9761692}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9761692}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family. CC {ECO:0000305}. 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; Y11152; CAA72038.1; -; Genomic_DNA. DR EMBL; U11547; AAA75359.1; -; Genomic_DNA. DR PIR; C56262; C56262. DR RefSeq; WP_003688976.1; NZ_WHPL01000002.1. DR PDB; 1KOP; X-ray; 1.90 A; A/B=30-252. DR PDB; 1KOQ; X-ray; 1.90 A; A/B=30-252. DR PDB; 8DPC; X-ray; 2.41 A; A/C/E/G=27-252. DR PDB; 8DQF; X-ray; 2.80 A; A/C/E/G=27-252. DR PDB; 8DR2; X-ray; 2.81 A; A/C/E/G=27-252. DR PDB; 8DRB; X-ray; 2.59 A; A/C/E/G=27-252. DR PDB; 8DYQ; X-ray; 2.15 A; A/C/E/G=27-252. DR PDBsum; 1KOP; -. DR PDBsum; 1KOQ; -. DR PDBsum; 8DPC; -. DR PDBsum; 8DQF; -. DR PDBsum; 8DR2; -. DR PDBsum; 8DRB; -. DR PDBsum; 8DYQ; -. DR AlphaFoldDB; Q50940; -. DR SMR; Q50940; -. DR GeneID; 66752914; -. DR OMA; RMRMENN; -. DR BRENDA; 4.2.1.1; 3590. DR EvolutionaryTrace; Q50940; -. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. 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; 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 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Lyase; Metal-binding; Periplasm; Signal; KW Zinc. FT SIGNAL 1..26 FT CHAIN 27..252 FT /note="Carbonic anhydrase" FT /id="PRO_0000004266" FT DOMAIN 31..252 FT /note="Alpha-carbonic anhydrase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134" FT ACT_SITE 92 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P00918" FT BINDING 118 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:9761692" FT BINDING 120 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:9761692" FT BINDING 137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:9761692" FT BINDING 203..204 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:9761692" FT DISULFID 54..207 FT /evidence="ECO:0000269|PubMed:9761692" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:1KOP" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:1KOP" FT HELIX 44..47 FT /evidence="ECO:0007829|PDB:1KOP" FT HELIX 49..52 FT /evidence="ECO:0007829|PDB:1KOP" FT HELIX 53..56 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 94..97 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 104..107 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 110..122 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 133..141 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 147..156 FT /evidence="ECO:0007829|PDB:1KOP" FT HELIX 161..163 FT /evidence="ECO:0007829|PDB:1KOQ" FT HELIX 164..167 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 172..178 FT /evidence="ECO:0007829|PDB:1KOP" FT HELIX 185..188 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 195..201 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 209..218 FT /evidence="ECO:0007829|PDB:1KOP" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:1KOP" FT HELIX 224..234 FT /evidence="ECO:0007829|PDB:1KOP" SQ SEQUENCE 252 AA; 28085 MW; E4454A145A0F440F CRC64; MPRFPRTLPR LTAVLLLACT AFSAAAHGNH THWGYTGHDS PESWGNLSEE FRLCSTGKNQ SPVNITETVS GKLPAIKVNY KPSMVDVENN GHTIQVNYPE GGNTLTVNGR TYTLKQFHFH VPSENQIKGR TFPMEAHFVH LDENKQPLVL AVLYEAGKTN GRLSSIWNVM PMTAGKVKLN QPFDASTLLP KRLKYYRFAG SLTTPPCTEG VSWLVLKTYD HIDQAQAEKF TRAVGSENNR PVQPLNARVV IE //