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 01-MAR-2002 (Rel. 41, Last annotation update) DE Carbonic anhydrase precursor (EC 4.2.1.1) (Carbonate dehydratase). GN CAH. OS Neisseria gonorrhoeae. OC Bacteria; Proteobacteria; beta subdivision; 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 HYDRATATION 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 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 //