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Database: UniProt
Entry: A0A095CAC3_PISSA
LinkDB: A0A095CAC3_PISSA
Original site: A0A095CAC3_PISSA 
ID   A0A095CAC3_PISSA        Unreviewed;       220 AA.
AC   A0A095CAC3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   31-JAN-2018, entry version 22.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU003956};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU003956};
DE   AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN   ORFNames=KU39_1167 {ECO:0000313|EMBL:ALB22350.1}, KW89_1902
GN   {ECO:0000313|EMBL:ALA25368.1};
OS   Piscirickettsia salmonis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Piscirickettsia.
OX   NCBI_TaxID=1238 {ECO:0000313|EMBL:ALA25368.1, ECO:0000313|Proteomes:UP000029541};
RN   [1] {ECO:0000313|EMBL:ALB22350.1, ECO:0000313|Proteomes:UP000029558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1-32597 {ECO:0000313|Proteomes:UP000029558}, and PM32597B1
RC   {ECO:0000313|EMBL:ALB22350.1};
RX   PubMed=25523762;
RA   Bohle H., Henriquez P., Grothusen H., Navas E., Sandoval A.,
RA   Bustamante F., Bustos P., Mancilla M.;
RT   "Comparative Genome Analysis of Two Isolates of the Fish Pathogen
RT   Piscirickettsia salmonis from Different Hosts Reveals Major
RT   Differences in Virulence-Associated Secretion Systems.";
RL   Genome Announc. 2:0-0(2014).
RN   [2] {ECO:0000313|EMBL:ALB22350.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PM32597B1 {ECO:0000313|EMBL:ALB22350.1};
RA   Bohle H., Henriquez P., Navas E., Grothusen H., Bustamante F.,
RA   Bustos P., Bustos P., Mancilla M.;
RT   "Complete genome sequence of Piscirickettsia salmonis strain
RT   PM32597B1.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ALA25368.1, ECO:0000313|Proteomes:UP000029541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1-15972 {ECO:0000313|Proteomes:UP000029541}, and PM15972A1
RC   {ECO:0000313|EMBL:ALA25368.1};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M.,
RA   Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J.,
RA   Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L.,
RA   Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J.,
RA   Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L.,
RA   Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z.,
RA   Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J.,
RA   Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA   Hatfull G.F.;
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|RuleBase:RU003956}.
CC   -!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
CC       {ECO:0000256|RuleBase:RU003956}.
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000256|RuleBase:RU003956}.
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DR   EMBL; CP012413; ALA25368.1; -; Genomic_DNA.
DR   EMBL; CP012508; ALB22350.1; -; Genomic_DNA.
DR   RefSeq; WP_016209947.1; NZ_PDFD01000169.1.
DR   EnsemblBacteria; ALA25368; ALA25368; KW89_1902.
DR   EnsemblBacteria; ALB22350; ALB22350; KU39_1167.
DR   GeneID; 29880450; -.
DR   PATRIC; fig|1227812.109.peg.2033; -.
DR   Proteomes; UP000029541; Chromosome.
DR   Proteomes; UP000029558; 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   Gene3D; 3.40.1050.10; -; 1.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR015892; Carbonic_anhydrase_CS.
DR   InterPro; IPR036874; Carbonic_anhydrase_sf.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; SSF53056; 1.
DR   PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
DR   PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000029541,
KW   ECO:0000313|Proteomes:UP000029558};
KW   Lyase {ECO:0000256|RuleBase:RU003956, ECO:0000313|EMBL:ALA25368.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029541};
KW   Zinc {ECO:0000256|RuleBase:RU003956}.
SQ   SEQUENCE   220 AA;  24837 MW;  374798EC1B522E00 CRC64;
     MKEKSGKNPI VQLILGHKDF KEEYLSEENE RYRKEAAQGQ HPKVLIISCS DSRVNPVIVN
     HINLGQVFSI QNVANTVPPY QPGKLGADSH HGTSAAIEFA VLGLNVEHII VYGHSGCGGI
     RSLVEGELPF KPTFVDQWVR ILDAAKQNVQ RDFPDATVDE QCHHCEREGV KVSLKNLLTF
     PWVKERVDNH TLQLHGWHFD IPTGDITRFD EKKNSFLKLD
//
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