(data stored in SCRATCH zone)

SWISSPROT: Q13DV6_RHOPS

ID   Q13DV6_RHOPS            Unreviewed;       214 AA.
AC   Q13DV6;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
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   OrderedLocusNames=RPD_0495 {ECO:0000313|EMBL:ABE37733.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37733.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37733.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37733.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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;
CC         Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1;
CC         Evidence={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; CP000283; ABE37733.1; -; Genomic_DNA.
DR   RefSeq; WP_011500921.1; NC_007958.1.
DR   STRING; 316057.RPD_0495; -.
DR   EnsemblBacteria; ABE37733; ABE37733; RPD_0495.
DR   KEGG; rpd:RPD_0495; -.
DR   eggNOG; ENOG4107B2H; Bacteria.
DR   eggNOG; COG0288; LUCA.
DR   HOGENOM; HOG000125183; -.
DR   KO; K01673; -.
DR   OMA; KINHVIV; -.
DR   OrthoDB; 1841447at2; -.
DR   BioCyc; RPAL316057:RPD_RS02545-MONOMER; -.
DR   Proteomes; UP000001818; 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; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13DV6.
DR   SWISS-2DPAGE; Q13DV6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Lyase {ECO:0000256|RuleBase:RU003956, ECO:0000313|EMBL:ABE37733.1};
KW   Zinc {ECO:0000256|RuleBase:RU003956}.
SQ   SEQUENCE   214 AA;  23794 MW;  11C947E663155F49 CRC64;
     MTSFPKTLIE GYQAFRTQRL PTEQSRYRDL SERGQSPEVM LIGCCDSRVS PEVIFDAGPG
     ELFVVRNVAN LVPVYEPDGG AHGVSAALEF AVQVLKVKHI VVLGHAQCGG IKAFTDKTPP
     LTDSDFIGRW MSMFIKPGEV VEQRDHESVQ DFRTRIEKAA VFRSIENLMT FPCIKILVER
     GRLQLHGAYF GVAAGELFVL DPQTKEFRPA APRG
//

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