ATCA6_ARATH
ID ATCA6_ARATH Reviewed; 260 AA.
AC Q9SUB4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Alpha carbonic anhydrase 6;
DE Short=AtaCA6;
DE Short=AtalphaCA6;
DE EC=4.2.1.1;
DE AltName: Full=Alpha carbonate dehydratase 6;
DE Flags: Precursor;
GN Name=ACA6; OrderedLocusNames=At4g21000; ORFNames=T13K14.160;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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}.
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DR EMBL; AL080282; CAB45895.1; -; Genomic_DNA.
DR EMBL; AL161554; CAB79100.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84386.1; -; Genomic_DNA.
DR PIR; T10642; T10642.
DR RefSeq; NP_193832.1; NM_118218.1.
DR AlphaFoldDB; Q9SUB4; -.
DR SMR; Q9SUB4; -.
DR STRING; 3702.AT4G21000.1; -.
DR PaxDb; Q9SUB4; -.
DR PRIDE; Q9SUB4; -.
DR EnsemblPlants; AT4G21000.1; AT4G21000.1; AT4G21000.
DR GeneID; 827847; -.
DR Gramene; AT4G21000.1; AT4G21000.1; AT4G21000.
DR KEGG; ath:AT4G21000; -.
DR Araport; AT4G21000; -.
DR TAIR; locus:2133129; AT4G21000.
DR eggNOG; KOG0382; Eukaryota.
DR HOGENOM; CLU_039326_0_0_1; -.
DR InParanoid; Q9SUB4; -.
DR OMA; ERFHFHD; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; Q9SUB4; -.
DR BioCyc; ARA:AT4G21000-MON; -.
DR PRO; PR:Q9SUB4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUB4; baseline.
DR Genevisible; Q9SUB4; 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 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 3: Inferred from homology;
KW Chloroplast; Disulfide bond; Glycoprotein; Lyase; Metal-binding; Plastid;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..260
FT /note="Alpha carbonic anhydrase 6"
FT /id="PRO_0000429732"
FT DOMAIN 35..260
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 100
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 211..212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..215
FT /evidence="ECO:0000250"
SQ SEQUENCE 260 AA; 29948 MW; B611B4E89FAA33B8 CRC64;
MDANTKTILF FVVFFIDLFS PNILFVYARE IGNKPLFTYK QKTEKGPAEW GKLDPQWKVC
STGKIQSPID LTDERVSLIH DQALSKHYKP ASAVIQSRGH DVMVSWKGDG GKITIHQTDY
KLVQCHWHSP SEHTINGTSY DLELHMVHTS ASGKTTVVGV LYKLGEPDEF LTKILNGIKG
VGKKEIDLGI VDPRDIRFET NNFYRYIGSL TIPPCTEGVI WTVQKRVLYF FCFCYRLIIF
VTPYINIFWI FVFVFWCMLM
