ATCA2_ARATH
ID ATCA2_ARATH Reviewed; 245 AA.
AC F4IHR4; Q9SL34;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Alpha carbonic anhydrase 2;
DE Short=AtaCA2;
DE Short=AtalphaCA2;
DE EC=4.2.1.1;
DE AltName: Full=Alpha carbonate dehydratase 2;
DE Flags: Precursor;
GN Name=ACA2; OrderedLocusNames=At2g28210; ORFNames=T3B23.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP TISSUE SPECIFICITY, INDUCTION BY CO2, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=17407539; DOI=10.1111/j.1365-3040.2007.01651.x;
RA Fabre N., Reiter I.M., Becuwe-Linka N., Genty B., Rumeau D.;
RT "Characterization and expression analysis of genes encoding alpha and beta
RT carbonic anhydrases in Arabidopsis.";
RL Plant Cell Environ. 30:617-629(2007).
CC -!- FUNCTION: Reversible hydration of carbon dioxide. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC Note=Targeted to the chloroplast via a protein-targeting pathway that
CC uses the secretory system. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in stems and roots.
CC {ECO:0000269|PubMed:17407539}.
CC -!- INDUCTION: Accumulates in low CO(2) conditions.
CC {ECO:0000269|PubMed:17407539}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD29832.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006202; AAD29832.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B84682; B84682.
DR AlphaFoldDB; F4IHR4; -.
DR SMR; F4IHR4; -.
DR STRING; 3702.AT2G28210.1; -.
DR PaxDb; F4IHR4; -.
DR PeptideAtlas; F4IHR4; -.
DR ProteomicsDB; 246722; -.
DR EnsemblPlants; AT2G28210.1; AT2G28210.1; AT2G28210.
DR Gramene; AT2G28210.1; AT2G28210.1; AT2G28210.
DR Araport; AT2G28210; -.
DR TAIR; locus:2062819; AT2G28210.
DR eggNOG; KOG0382; Eukaryota.
DR HOGENOM; CLU_039326_0_0_1; -.
DR PRO; PR:F4IHR4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IHR4; baseline and differential.
DR Genevisible; F4IHR4; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0010037; P:response to carbon dioxide; IEP:TAIR.
DR CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; -; 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; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Disulfide bond; Glycoprotein; Lyase; Metal-binding; Plastid;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..245
FT /note="Alpha carbonic anhydrase 2"
FT /id="PRO_0000429728"
FT DOMAIN 37..245
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 218..219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..222
FT /evidence="ECO:0000250"
SQ SEQUENCE 245 AA; 28362 MW; 5DBF74EC448157D2 CRC64;
MDKISIRCFI FLVLTSFVTT VSCLSAATDY REVEDEHEFS YEWNQENGPA KWGKLRPEWK
MCGKGEMQSP IDLMNKRVRL VTHLKKLTRH YKPCNATLKN RGHDMMLKFG EEGSGSITVN
GTEYKLLQLH WHSPSEHTMN GRRFALELHM VHENINGSLA VVTVLYKIGR PDSFLGLLEN
KLSAITDQNE AEKYVDVIDP RDIKIGSRKF YRYIGSLTTP PCTQNVIWTV VKKVNTHRYF
LLFFT
