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Database: UniProt
Entry: A0A0Q4US23_9MICO
LinkDB: A0A0Q4US23_9MICO
Original site: A0A0Q4US23_9MICO 
ID   A0A0Q4US23_9MICO        Unreviewed;       218 AA.
AC   A0A0Q4US23;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
GN   ORFNames=ASF23_07815 {ECO:0000313|EMBL:KQO62827.1};
OS   Curtobacterium sp. Leaf261.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO62827.1, ECO:0000313|Proteomes:UP000050821};
RN   [1] {ECO:0000313|EMBL:KQO62827.1, ECO:0000313|Proteomes:UP000050821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf261 {ECO:0000313|EMBL:KQO62827.1,
RC   ECO:0000313|Proteomes:UP000050821};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQO62827.1, ECO:0000313|Proteomes:UP000050821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf261 {ECO:0000313|EMBL:KQO62827.1,
RC   ECO:0000313|Proteomes:UP000050821};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide to form
CC       bicarbonate. {ECO:0000256|ARBA:ARBA00024993}.
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   -!- 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQO62827.1}.
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DR   EMBL; LMMJ01000008; KQO62827.1; -; Genomic_DNA.
DR   RefSeq; WP_055952199.1; NZ_LMMJ01000008.1.
DR   AlphaFoldDB; A0A0Q4US23; -.
DR   STRING; 1736311.ASF23_07815; -.
DR   OrthoDB; 9797527at2; -.
DR   Proteomes; UP000050821; Unassembled WGS sequence.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR036874; Carbonic_anhydrase_sf.
DR   PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR11002:SF76; CARBONIC ANHYDRASE; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050821};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   218 AA;  22298 MW;  5E00F2B78D14E678 CRC64;
     MTDRAASTPA EALRLLTEGN ARFAADRRRV GRTDPERRTE LADAQAPFAT VLGCSDSRVP
     FEHVFDAGIG DVFAIRNAGQ IADEVVLGSI EFAVVALGTP LVVVLRHTLC GAVKAARSGE
     PVPAPHLQAL VDAIAPSVER VRATDPGVEQ EAVGAAHLEA TMRTILERSG AVSDAIAEGR
     LAVVGATYDL ASGLVTVDTV VGDAGVGSGD TGVAPGAV
//
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