ATCA8_ARATH
ID ATCA8_ARATH Reviewed; 389 AA.
AC Q9FM99;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Alpha carbonic anhydrase 8;
DE Short=AtaCA8;
DE Short=AtalphaCA8;
DE EC=4.2.1.1;
DE AltName: Full=Alpha carbonate dehydratase 8;
DE Flags: Precursor;
GN Name=ACA8; OrderedLocusNames=At5g56330; ORFNames=MCD7.6;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 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 -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-class carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED96750.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AED96750.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB11260.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB11260.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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 EMBL; AB009049; BAB11260.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96750.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_200444.1; NM_125016.2.
DR AlphaFoldDB; Q9FM99; -.
DR SMR; Q9FM99; -.
DR PRIDE; Q9FM99; -.
DR GeneID; 835733; -.
DR KEGG; ath:AT5G56330; -.
DR Araport; AT5G56330; -.
DR TAIR; locus:2161043; AT5G56330.
DR HOGENOM; CLU_793084_0_0_1; -.
DR OrthoDB; 1377476at2759; -.
DR BioCyc; ARA:AT5G56330-MON; -.
DR PRO; PR:Q9FM99; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FM99; baseline and differential.
DR Genevisible; Q9FM99; AT.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
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 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 PANTHER; PTHR18952; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 3: Inferred from homology;
KW Chloroplast; Disulfide bond; Glycoprotein; Lyase; Metal-binding; Plastid;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..389
FT /note="Alpha carbonic anhydrase 8"
FT /id="PRO_0000429734"
FT DOMAIN 138..374
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 21..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 320..321
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 163..324
FT /evidence="ECO:0000250"
SQ SEQUENCE 389 AA; 42567 MW; 4F8BE5E07B8E75A9 CRC64;
MKISSLGWVL VLIFISITIV SSAPAPKPPK PKPAPAPTPP KPKPTPAPTP PKPKPKPAPT
PPKPKPAPAP TPPKPKPAPA PTPPKPKPKP APTPPNPKPT PAPTPPKPKP APAPAPTPAP
KPKPAPKPAP GGEVEDETEF SYETKGNKGP AKWGTLDAEW KMCGIGKMQS PIDLRDKNVV
VSNKFGLLRS QYLPSNTTIK NRGHDIMLKF KGGNKGIGVT IRGTRYQLQQ LHWHSPSEHT
INGKRFALEE HLVHESKDKR YAVVAFLYNL GASDPFLFSL EKQLKKITDT HASEEHVGII
DPKKLSFESK HYYRYSGSLT APPCSENVIW SVSKEIRTVS SKQVKLLRVA VHDASDSNAR
PLQAVNKRKV YLYKPKVKLM KKYCNISSY
