CYNT_HELPJ
ID CYNT_HELPJ Reviewed; 221 AA.
AC Q9ZN54;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Carbonic anhydrase;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase;
GN Name=cynT; OrderedLocusNames=jhp_0004;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AE001439; AAD05588.1; -; Genomic_DNA.
DR PIR; F71985; F71985.
DR RefSeq; WP_000387094.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZN54; -.
DR SMR; Q9ZN54; -.
DR STRING; 85963.jhp_0004; -.
DR EnsemblBacteria; AAD05588; AAD05588; jhp_0004.
DR KEGG; hpj:jhp_0004; -.
DR PATRIC; fig|85963.30.peg.1041; -.
DR eggNOG; COG0288; Bacteria.
DR OMA; WHYIIET; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd00884; beta_CA_cladeB; 1.
DR Gene3D; 3.40.1050.10; -; 1.
DR InterPro; IPR045066; Beta_CA_cladeB.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR11002; PTHR11002; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; SSF53056; 1.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 3: Inferred from homology;
KW Lyase; Metal-binding; Zinc.
FT CHAIN 1..221
FT /note="Carbonic anhydrase"
FT /id="PRO_0000077462"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 221 AA; 25741 MW; 48ABBA5DD912D1CF CRC64;
MEAFLGALEF QENEYEEFKE LYESLKTKQK PHTLFISCVD SRVVPNLITG TQPGELYVIR
NMGNVIPPKT SYKESLSTIA SVEYAIAHVG VQNLIICGHS DCGACGSIHL IHDETTKAKT
PYIANWIQFL EPIKEELKNH PQFSNHFAKR SWLTERLNAR LQLNNLLSYD FIQERVINNE
LKIFGWHYII ETGRIYNYNF ESHFFEPIEE TIKQRISHEN F
