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 08-MAR-2011, entry version 72. 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; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=485; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RX MEDLINE=97261830; PubMed=9108244; RX 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 RT and some properties of carbonic anhydrase from Neisseria RT gonorrhoeae."; RL Eur. J. Biochem. 244:755-760(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-252. RC STRAIN=MS11; RX MEDLINE=95238263; PubMed=7721686; RA Black C.G., Fyfe J.A.M., 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) OF 30-252 IN COMPLEX WITH TINC RP ION AND INHIBITOR ACETAZOLAMIDE. RX MEDLINE=98437389; 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 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: Periplasm (Potential). CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase 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; -; Genomic_DNA. DR EMBL; U11547; AAA75359.1; -; Genomic_DNA. DR PIR; C56262; C56262. 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 PDBsum; 1KOP; -. DR PDBsum; 1KOQ; -. DR ProteinModelPortal; Q50940; -. DR SMR; Q50940; 30-252. DR BRENDA; 4.2.1.1; 588. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro. DR InterPro; IPR001148; Carbonic_anhydrase_a-class_cat. DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS. DR Gene3D; G3DSA:3.10.200.10; Euk_COanhd; 1. DR Pfam; PF00194; Carb_anhydrase; 1. DR SUPFAM; SSF51069; Euk_COanhd; 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 Carbonic anhydrase. FT /FTId=PRO_0000004266. FT REGION 203 204 Substrate binding. FT ACT_SITE 92 92 Proton acceptor (By similarity). FT METAL 118 118 Zinc; catalytic. FT METAL 120 120 Zinc; catalytic. FT METAL 137 137 Zinc; catalytic. FT DISULFID 54 207 FT HELIX 37 39 FT HELIX 41 43 FT HELIX 44 47 FT HELIX 49 52 FT HELIX 53 56 FT STRAND 76 79 FT STRAND 86 89 FT STRAND 94 97 FT STRAND 104 107 FT STRAND 110 122 FT STRAND 124 127 FT STRAND 133 141 FT STRAND 147 156 FT HELIX 164 167 FT STRAND 172 178 FT HELIX 185 188 FT STRAND 195 201 FT STRAND 209 218 FT STRAND 220 222 FT HELIX 224 234 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 //