CAH_NEIGO
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 03-AUG-2022, entry version 125.
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; Neisseriaceae;
OC 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 and
RT some properties of carbonic anhydrase from Neisseria 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 transcribe
RT 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 ION
RP 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 and its
RT complex with the inhibitor acetazolamide.";
RL J. Mol. Biol. 283:301-310(1998).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
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}.
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DR EMBL; Y11152; CAA72038.1; -; Genomic_DNA.
DR EMBL; U11547; AAA75359.1; -; Genomic_DNA.
DR PIR; C56262; C56262.
DR RefSeq; WP_003688976.1; NZ_WHPL01000002.1.
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 AlphaFoldDB; Q50940; -.
DR SMR; Q50940; -.
DR GeneID; 66752914; -.
DR OMA; RMRMENN; -.
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 CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
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
FT /note="Carbonic anhydrase"
FT /id="PRO_0000004266"
FT DOMAIN 31..252
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:9761692"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:9761692"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:9761692"
FT BINDING 203..204
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9761692"
FT DISULFID 54..207
FT /evidence="ECO:0000269|PubMed:9761692"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1KOP"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1KOP"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:1KOP"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1KOP"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 110..122
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:1KOP"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1KOQ"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:1KOP"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:1KOP"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1KOP"
FT HELIX 224..234
FT /evidence="ECO:0007829|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
