UniProt: A0A377PWA0

Database: UniProt
Entry: A0A377PWA0_9HELI

LinkDB:  A0A377PWA0_9HELI 
Original site:  A0A377PWA0_9HELI

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   A0A377PWA0_9HELI        Unreviewed;       254 AA.
AC   A0A377PWA0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00014628, ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
GN   Name=cah_2 {ECO:0000313|EMBL:STQ85903.1};
GN   ORFNames=LS73_007240 {ECO:0000313|EMBL:TLD99564.1}, NCTC12714_00692
GN   {ECO:0000313|EMBL:STQ85903.1};
OS   Helicobacter muridarum.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=216 {ECO:0000313|EMBL:STQ85903.1, ECO:0000313|Proteomes:UP000255139};
RN   [1] {ECO:0000313|EMBL:TLD99564.1, ECO:0000313|Proteomes:UP000029922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST1 {ECO:0000313|EMBL:TLD99564.1,
RC   ECO:0000313|Proteomes:UP000029922};
RX   PubMed=25428971;
RA   Sheh A., Shen Z., Fox J.G.;
RT   "Draft genome sequences of eight enterohepatic helicobacter species
RT   isolated from both laboratory and wild rodents.";
RL   Genome Announc. 2:e01218-e01214(2014).
RN   [2] {ECO:0000313|EMBL:STQ85903.1, ECO:0000313|Proteomes:UP000255139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12714 {ECO:0000313|EMBL:STQ85903.1,
RC   ECO:0000313|Proteomes:UP000255139};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|RuleBase:RU367011}.
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|RuleBase:RU367011};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU367011};
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR   EMBL; UGJE01000002; STQ85903.1; -; Genomic_DNA.
DR   EMBL; JRPD02000017; TLD99564.1; -; Genomic_DNA.
DR   RefSeq; WP_052089829.1; NZ_UGJE01000002.1.
DR   AlphaFoldDB; A0A377PWA0; -.
DR   STRING; 216.LS73_07525; -.
DR   OrthoDB; 5327615at2; -.
DR   Proteomes; UP000029922; Unassembled WGS sequence.
DR   Proteomes; UP000255139; Unassembled WGS sequence.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 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; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF265; CARBONIC ANHYDRASE; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU367011};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000255139};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT   DOMAIN          30..254
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   254 AA;  28111 MW;  8347426514AF56A5 CRC64;
     MKLKLSLLLK KGFFATLLLG FCYGASDHHA HWSYSGESGP KMWGELDPSY SACKMEKFQS
     PINILDSKTT KSSANFILKN AYTVNSKDIV NNGHTIQVNF NPGNSLVFDG VSYDLVQLHF
     HTPSENQLNN RSFPAEVHMV HKDSSGNLLV VGVFIKQGNT NLALQSILKA APNKPNTKID
     FKDISLSSLL PQNIAYYQFQ GSLTTPPCSG NVTWVVMRDS IDASKSQIHA LNEIMKDNAR
     DVQPLNGRTI SISY
//

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