ID A0A0D3C8F8_BRAOL Unreviewed; 415 AA.
AC A0A0D3C8F8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo5g008760.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo5g008760.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo5g008760.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000256|ARBA:ARBA00002904, 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|ARBA:ARBA00000943,
CC 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000256|ARBA:ARBA00004470}.
CC -!- SIMILARITY: Belongs to the PPR family. PCMP-H subfamily.
CC {ECO:0000256|ARBA:ARBA00006643}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|RuleBase:RU367011}.
CC -!- SIMILARITY: Belongs to the alpha-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00006365}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0D3C8F8; -.
DR STRING; 109376.A0A0D3C8F8; -.
DR EnsemblPlants; Bo5g008760.1; Bo5g008760.1; Bo5g008760.
DR Gramene; Bo5g008760.1; Bo5g008760.1; Bo5g008760.
DR eggNOG; KOG0382; Eukaryota.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_662861_0_0_1; -.
DR Proteomes; UP000032141; Chromosome C5.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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 InterPro; IPR032867; DYW_dom.
DR InterPro; IPR046848; E_motif.
DR PANTHER; PTHR18952:SF284; ALPHA CARBONIC ANHYDRASE 7; 1.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR Pfam; PF14432; DYW_deaminase; 1.
DR Pfam; PF20431; E_motif; 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:UP000032141};
KW Signal {ECO:0000256|RuleBase:RU367011};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT CHAIN 25..415
FT /note="Carbonic anhydrase"
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT /id="PRO_5025077222"
FT DOMAIN 35..268
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 415 AA; 47502 MW; 8C2FF0DBAAABFEE0 CRC64;
MESSSIQCIF FVFIVFTFIS LSTAASSHGE VEDEHEFNYK KNDGKGPERW GEIKPEWEMC
GKGEIQSPID LMNERVKIVS HLGRLIRDYE PSNATIKNRG HDIMLKFEDG AAGSIKINGF
QYELQQLHWH SPSEHTINGR RFALELHMVH EGKKGRMAVV TVLYKIGRAD TFIRSLEKEL
EAITDLDDAE KHVRMIDPKQ IKIGSRKYYR YIGSLTTPPC TQNVTWSVVR KIRTVTREQV
RLLRVAVHDR KLIEIEPANS GSYILLSNIY ATAGRWKDVA RIRAVLSGKG MKKVPGYSQR
VKFLQHLLFR CGLTPVKVRP GSATGCSSIE IDFVGEACFV SDTSEVLLEM EEEWKEGALR
HHSEKLAILT VVKNLSMCRN CHEATKLMSK IYKMEIVARE RTRFHHFCNI PSCYI
//
