ID CAH_NEIGO STANDARD; PRT; 252 AA. AC Q50940; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Carbonic anhydrase precursor (EC 4.2.1.1) (Carbonate dehydratase). GN CAH. OS Neisseria gonorrhoeae. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=485; RN [1] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=97261830; PubMed=9108244; RA Chirica L.C., Elleby B., Jonsson B.-H., Lindskog S.; RT "The complete sequence, expression in Escherichia coli, purification RT and some properties of carbonic anhydrase from Neisseria RT gonorrhoeae."; RL Eur. J. Biochem. 244:755-760(1997). RN [2] RP SEQUENCE OF 50-252 FROM N.A. RC STRAIN=MS11; RX MEDLINE=95238263; PubMed=7721686; RA Black C.G., Fyfe J.A., Davies J.K.; RT "A promoter associated with the neisserial repeat can be used to RT transcribe the uvrB gene from Neisseria gonorrhoeae."; RL J. Bacteriol. 177:1952-1958(1995). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX MEDLINE=98437389; PubMed=9761692; 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 RT and its complex with the inhibitor acetazolamide."; RL J. Mol. Biol. 283:301-310(1998). CC -!- FUNCTION: Reversible hydration of carbon dioxide. CC -!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O. CC -!- COFACTOR: Zinc. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Periplasmic (Potential). CC -!- SIMILARITY: Belongs to the eukaryotic-type carbonic anhydrase CC family. 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; -. DR EMBL; U11547; AAA75359.1; -. DR PDB; 1KOP; 13-JAN-99. DR PDB; 1KOQ; 13-JAN-99. DR InterPro; IPR001148; Euk_COanhd. DR Pfam; PF00194; carb_anhydrase; 1. DR ProDom; PD000865; Euk_COanhd; 1. DR PROSITE; PS00162; EUK_CO2_ANHYDRASE; 1. KW Lyase; Zinc; Periplasmic; Signal; 3D-structure. FT SIGNAL 1 26 FT CHAIN 27 252 Carbonic anhydrase. FT METAL 118 118 Zinc (catalytic) (By similarity). FT METAL 120 120 Zinc (catalytic) (By similarity). FT METAL 137 137 Zinc (catalytic) (By similarity). FT DISULFID 54 207 FT HELIX 37 39 FT HELIX 41 43 FT HELIX 44 47 FT HELIX 49 51 FT TURN 52 52 FT HELIX 53 56 FT STRAND 64 65 FT STRAND 69 69 FT STRAND 76 79 FT STRAND 83 83 FT STRAND 86 89 FT STRAND 94 97 FT STRAND 104 107 FT TURN 108 109 FT STRAND 110 120 FT STRAND 126 127 FT TURN 128 129 FT STRAND 130 130 FT STRAND 134 141 FT TURN 143 144 FT STRAND 147 156 FT HELIX 161 163 FT HELIX 164 167 FT TURN 168 169 FT STRAND 175 178 FT STRAND 183 183 FT HELIX 185 188 FT STRAND 195 201 FT TURN 205 206 FT STRAND 209 216 FT STRAND 220 222 FT HELIX 224 234 FT TURN 246 247 FT STRAND 251 252 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 //