ID E1Q3H1_HELPP Unreviewed; 221 AA.
AC E1Q3H1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN OrderedLocusNames=HPPC_00020 {ECO:0000313|EMBL:ADO06269.1};
OS Helicobacter pylori (strain PeCan4).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=765963 {ECO:0000313|EMBL:ADO06269.1, ECO:0000313|Proteomes:UP000006863};
RN [1] {ECO:0000313|Proteomes:UP000006863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PeCan4 {ECO:0000313|Proteomes:UP000006863};
RA Kersulyte D., Vasquez J., Gilman R.H., Berg D.E.;
RT "Complete genome sequence of Helicobacter pylori strain PeCan4.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000256|RuleBase:RU003956}.
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 Evidence={ECO:0000256|ARBA:ARBA00000943,
CC ECO:0000256|RuleBase:RU003956};
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006217, ECO:0000256|RuleBase:RU003956}.
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DR EMBL; CP002074; ADO06269.1; -; Genomic_DNA.
DR RefSeq; WP_000643021.1; NC_014555.1.
DR AlphaFoldDB; E1Q3H1; -.
DR KEGG; hpc:HPPC_00020; -.
DR HOGENOM; CLU_053879_5_3_7; -.
DR Proteomes; UP000006863; Chromosome.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd00884; beta_CA_cladeB; 1.
DR Gene3D; 3.40.1050.10; Carbonic anhydrase; 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; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR11002:SF83; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003956};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
FT COILED 1..28
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 221 AA; 25746 MW; 054D25965A1B35FF CRC64;
MKAFLGALEF QENEYEELKE LYESLKTKQK PHTLFISCVD SRVVPNLITG TKPGELYVIR
NMGNVIPPKT SYKESLSTMA SIEYAIVHVG VQNLIICGHS DCGACGSIHL INDETTKAKT
PYIADWIQFL EPIKEELKNH PQFSSHFAKR SWLTERLNVR LQLNNLLSYD FIQERVVNNE
LKIFGWHYII ETGRIYNYNF ESHFFEPIEE TIKQRKSHEN F
//