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 25-OCT-2017, entry version 105. 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 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 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 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 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, 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 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: 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_NBTV01000001.1. 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 PDBsum; 1KOP; -. DR PDBsum; 1KOQ; -. DR ProteinModelPortal; Q50940; -. DR SMR; Q50940; -. DR eggNOG; COG3338; LUCA. 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 GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro. DR Gene3D; 3.10.200.10; -; 1. DR InterPro; IPR001148; Carbonic_anhydrase_a. DR InterPro; IPR023561; Carbonic_anhydrase_a-class. DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS. DR InterPro; IPR036398; Carbonic_anhydrase_a_sf. 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 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 DOMAIN 31 252 Alpha-carbonic anhydrase. FT {ECO:0000255|PROSITE-ProRule:PRU01134}. FT REGION 203 204 Substrate binding. FT {ECO:0000269|PubMed:9761692}. FT ACT_SITE 92 92 Proton acceptor. FT {ECO:0000250|UniProtKB:P00918}. FT METAL 118 118 Zinc; catalytic. FT {ECO:0000269|PubMed:9761692}. FT METAL 120 120 Zinc; catalytic. FT {ECO:0000269|PubMed:9761692}. FT METAL 137 137 Zinc; catalytic. FT {ECO:0000269|PubMed:9761692}. FT DISULFID 54 207 {ECO:0000269|PubMed:9761692}. FT HELIX 37 39 {ECO:0000244|PDB:1KOP}. FT HELIX 41 43 {ECO:0000244|PDB:1KOP}. FT HELIX 44 47 {ECO:0000244|PDB:1KOP}. FT HELIX 49 52 {ECO:0000244|PDB:1KOP}. FT HELIX 53 56 {ECO:0000244|PDB:1KOP}. FT STRAND 76 79 {ECO:0000244|PDB:1KOP}. FT STRAND 86 89 {ECO:0000244|PDB:1KOP}. FT STRAND 94 97 {ECO:0000244|PDB:1KOP}. FT STRAND 104 107 {ECO:0000244|PDB:1KOP}. FT STRAND 110 122 {ECO:0000244|PDB:1KOP}. FT STRAND 124 127 {ECO:0000244|PDB:1KOP}. FT STRAND 133 141 {ECO:0000244|PDB:1KOP}. FT STRAND 147 156 {ECO:0000244|PDB:1KOP}. FT HELIX 161 163 {ECO:0000244|PDB:1KOQ}. FT HELIX 164 167 {ECO:0000244|PDB:1KOP}. FT STRAND 172 178 {ECO:0000244|PDB:1KOP}. FT HELIX 185 188 {ECO:0000244|PDB:1KOP}. FT STRAND 195 201 {ECO:0000244|PDB:1KOP}. FT STRAND 209 218 {ECO:0000244|PDB:1KOP}. FT STRAND 220 222 {ECO:0000244|PDB:1KOP}. FT HELIX 224 234 {ECO:0000244|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 //