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Database: UniProt
Entry: I1GXD3_BRADI
LinkDB: I1GXD3_BRADI
Original site: I1GXD3_BRADI 
ID   I1GXD3_BRADI            Unreviewed;       292 AA.
AC   I1GXD3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
GN   Name=100828444 {ECO:0000313|EnsemblPlants:KQK17706};
GN   ORFNames=BRADI_1g36190v3 {ECO:0000313|EMBL:KQK17706.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK17706.1};
RN   [1] {ECO:0000313|EMBL:KQK17706.1, ECO:0000313|EnsemblPlants:KQK17706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK17706.1,
RC   ECO:0000313|EnsemblPlants:KQK17706};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQK17706.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK17706.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQK17706}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK17706};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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|RuleBase:RU367011}.
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DR   EMBL; CM000880; KQK17706.1; -; Genomic_DNA.
DR   RefSeq; XP_003560592.1; XM_003560544.1.
DR   AlphaFoldDB; I1GXD3; -.
DR   STRING; 15368.I1GXD3; -.
DR   EnsemblPlants; KQK17706; KQK17706; BRADI_1g36190v3.
DR   GeneID; 100828444; -.
DR   Gramene; KQK17706; KQK17706; BRADI_1g36190v3.
DR   KEGG; bdi:100828444; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   HOGENOM; CLU_039326_0_0_1; -.
DR   InParanoid; I1GXD3; -.
DR   OMA; RQMHWHA; -.
DR   OrthoDB; 406335at2759; -.
DR   Proteomes; UP000008810; Chromosome 1.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
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:SF121; ALPHA-CARBONIC ANHYDRASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR18952; 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:UP000008810};
KW   Signal {ECO:0000256|RuleBase:RU367011};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT   CHAIN           28..292
FT                   /note="Carbonic anhydrase"
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT                   /id="PRO_5014094145"
FT   DOMAIN          34..275
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   292 AA;  33114 MW;  933BCA77BD422093 CRC64;
     MARIPTAAFL VAVSLCTAAV VTRHARAQET ADEPEYTYRR GADNGPERWG LLRVDWAACY
     WGRQQSPVDV PGGSSAPGPI RYGRLSQHYR PAPATMVNRG HDIMVRFDGD AGGLLIDGLN
     YRLRQMHWHS PSEHALDGRR YDLELHMLHQ TDKPSNKSFA VVAQLFRIGR RGDATLRMLE
     PYIERIEDRR KGSAEEIDYE VDPRRPVRRS DEYYRYTGSF TTPPCTEGVV WTVATRIGHV
     SRHQVDLLRD AVHDHARKNA RPLQDANGRA VALYYNWPLR GRGNTAATSD LN
//
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