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Database: UniProt
Entry: Q2G713_NOVAD
LinkDB: Q2G713_NOVAD
Original site: Q2G713_NOVAD 
ID   Q2G713_NOVAD            Unreviewed;       224 AA.
AC   Q2G713;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 101.
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=Saro_1920 {ECO:0000313|EMBL:ABD26360.1};
OS   Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS   56034 / CIP 105152 / NBRC 16084 / F199).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD26360.1, ECO:0000313|Proteomes:UP000009134};
RN   [1] {ECO:0000313|Proteomes:UP000009134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC   / F199 {ECO:0000313|Proteomes:UP000009134};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL   Submitted (JAN-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; 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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; CP000248; ABD26360.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2G713; -.
DR   STRING; 279238.Saro_1920; -.
DR   KEGG; nar:Saro_1920; -.
DR   eggNOG; COG0288; Bacteria.
DR   HOGENOM; CLU_053879_5_3_5; -.
DR   OMA; MIPHANN; -.
DR   Proteomes; UP000009134; 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:SF13; 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; PS00704; PROK_CO2_ANHYDRASE_1; 1.
DR   PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003956};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009134};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
SQ   SEQUENCE   224 AA;  24480 MW;  20E4608B13418B7A CRC64;
     MGPLARPMTQ DASPELDRLI AGYRRFREQG WTPKLERWRE LRDGQEPQVM IIACSDSRVD
     PAQIFDVDPG EIFVVRNVAA MVPPFETNPG HHGVSAALEF AVQVLKVKEV VVMGHGMCGG
     CKAALTQDLK GTEPGEGGFI ADWIALLDGV RDEVVDKHGT TGRPAERAME EAGVRASLAN
     LRTFPCIRRK EATGELKLRG TFFAISDGVL HVLDETTGDF SPVN
//
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