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Carbonic anhydrase (EC 4.2.1.1) (Carbonate dehydratase)

 CAH_NEIGO               Reviewed;         252 AA.
Q50940;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
25-OCT-2017, entry version 105.
RecName: Full=Carbonic anhydrase;
EC=4.2.1.1;
AltName: Full=Carbonate dehydratase;
Flags: Precursor;
Name=cah;
Neisseria gonorrhoeae.
Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
Neisseriaceae; Neisseria.
NCBI_TaxID=485;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
PubMed=9108244; DOI=10.1111/j.1432-1033.1997.00755.x;
Chirica L.C., Elleby B., Jonsson B.-H., Lindskog S.;
"The complete sequence, expression in Escherichia coli, purification
and some properties of carbonic anhydrase from Neisseria
gonorrhoeae.";
Eur. J. Biochem. 244:755-760(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-252.
STRAIN=MS11;
PubMed=7721686; DOI=10.1128/jb.177.8.1952-1958.1995;
Black C.G., Fyfe J.A.M., Davies J.K.;
"A promoter associated with the neisserial repeat can be used to
transcribe the uvrB gene from Neisseria gonorrhoeae.";
J. Bacteriol. 177:1952-1958(1995).
[3]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-252 IN COMPLEX WITH TINC
ION AND INHIBITOR ACETAZOLAMIDE, COFACTOR, AND DISULFIDE BOND.
PubMed=9761692; DOI=10.1006/jmbi.1998.2077;
Huang S., Xue Y., Sauer-Eriksson E., Chirica L., Lindskog S.,
Jonsson B.-H.;
"Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae
and its complex with the inhibitor acetazolamide.";
J. Mol. Biol. 283:301-310(1998).
-!- FUNCTION: Reversible hydration of carbon dioxide.
-!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:9761692};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9761692}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
{ECO:0000305}.
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EMBL; Y11152; CAA72038.1; -; Genomic_DNA.
EMBL; U11547; AAA75359.1; -; Genomic_DNA.
PIR; C56262; C56262.
RefSeq; WP_003688976.1; NZ_NBTV01000001.1.
PDB; 1KOP; X-ray; 1.90 A; A/B=30-252.
PDB; 1KOQ; X-ray; 1.90 A; A/B=30-252.
PDBsum; 1KOP; -.
PDBsum; 1KOQ; -.
ProteinModelPortal; Q50940; -.
SMR; Q50940; -.
eggNOG; COG3338; LUCA.
BRENDA; 4.2.1.1; 3590.
EvolutionaryTrace; Q50940; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
Gene3D; 3.10.200.10; -; 1.
InterPro; IPR001148; Carbonic_anhydrase_a.
InterPro; IPR023561; Carbonic_anhydrase_a-class.
InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
InterPro; IPR036398; Carbonic_anhydrase_a_sf.
PANTHER; PTHR18952; PTHR18952; 1.
Pfam; PF00194; Carb_anhydrase; 1.
SMART; SM01057; Carb_anhydrase; 1.
SUPFAM; SSF51069; SSF51069; 1.
PROSITE; PS00162; ALPHA_CA_1; 1.
PROSITE; PS51144; ALPHA_CA_2; 1.
1: Evidence at protein level;
3D-structure; Disulfide bond; Lyase; Metal-binding; Periplasm; Signal;
Zinc.
SIGNAL 1 26
CHAIN 27 252 Carbonic anhydrase.
/FTId=PRO_0000004266.
DOMAIN 31 252 Alpha-carbonic anhydrase.
{ECO:0000255|PROSITE-ProRule:PRU01134}.
REGION 203 204 Substrate binding.
{ECO:0000269|PubMed:9761692}.
ACT_SITE 92 92 Proton acceptor.
{ECO:0000250|UniProtKB:P00918}.
METAL 118 118 Zinc; catalytic.
{ECO:0000269|PubMed:9761692}.
METAL 120 120 Zinc; catalytic.
{ECO:0000269|PubMed:9761692}.
METAL 137 137 Zinc; catalytic.
{ECO:0000269|PubMed:9761692}.
DISULFID 54 207 {ECO:0000269|PubMed:9761692}.
HELIX 37 39 {ECO:0000244|PDB:1KOP}.
HELIX 41 43 {ECO:0000244|PDB:1KOP}.
HELIX 44 47 {ECO:0000244|PDB:1KOP}.
HELIX 49 52 {ECO:0000244|PDB:1KOP}.
HELIX 53 56 {ECO:0000244|PDB:1KOP}.
STRAND 76 79 {ECO:0000244|PDB:1KOP}.
STRAND 86 89 {ECO:0000244|PDB:1KOP}.
STRAND 94 97 {ECO:0000244|PDB:1KOP}.
STRAND 104 107 {ECO:0000244|PDB:1KOP}.
STRAND 110 122 {ECO:0000244|PDB:1KOP}.
STRAND 124 127 {ECO:0000244|PDB:1KOP}.
STRAND 133 141 {ECO:0000244|PDB:1KOP}.
STRAND 147 156 {ECO:0000244|PDB:1KOP}.
HELIX 161 163 {ECO:0000244|PDB:1KOQ}.
HELIX 164 167 {ECO:0000244|PDB:1KOP}.
STRAND 172 178 {ECO:0000244|PDB:1KOP}.
HELIX 185 188 {ECO:0000244|PDB:1KOP}.
STRAND 195 201 {ECO:0000244|PDB:1KOP}.
STRAND 209 218 {ECO:0000244|PDB:1KOP}.
STRAND 220 222 {ECO:0000244|PDB:1KOP}.
HELIX 224 234 {ECO:0000244|PDB:1KOP}.
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


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