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Database: UniProt
Entry: F4HUC4
LinkDB: F4HUC4
Original site: F4HUC4 
ID   ATCA5_ARATH             Reviewed;         277 AA.
AC   F4HUC4;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Alpha carbonic anhydrase 5;
DE            Short=AtaCA5;
DE            Short=AtalphaCA5;
DE            EC=4.2.1.1;
DE   AltName: Full=Alpha carbonate dehydratase 5;
DE   Flags: Precursor;
GN   Name=ACA5; OrderedLocusNames=At1g08065; ORFNames=T6D22.30;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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; AC026875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002684; AEE28238.1; -; Genomic_DNA.
DR   RefSeq; NP_172285.2; NM_100681.2.
DR   AlphaFoldDB; F4HUC4; -.
DR   SMR; F4HUC4; -.
DR   STRING; 3702.F4HUC4; -.
DR   GlyCosmos; F4HUC4; 2 sites, No reported glycans.
DR   PaxDb; 3702-AT1G08065-1; -.
DR   ProteomicsDB; 246826; -.
DR   EnsemblPlants; AT1G08065.1; AT1G08065.1; AT1G08065.
DR   GeneID; 837324; -.
DR   Gramene; AT1G08065.1; AT1G08065.1; AT1G08065.
DR   KEGG; ath:AT1G08065; -.
DR   Araport; AT1G08065; -.
DR   TAIR; AT1G08065; ACA5.
DR   eggNOG; KOG0382; Eukaryota.
DR   HOGENOM; CLU_039326_0_0_1; -.
DR   InParanoid; F4HUC4; -.
DR   OMA; YVVEQIH; -.
DR   OrthoDB; 3674322at2759; -.
DR   PhylomeDB; F4HUC4; -.
DR   PRO; PR:F4HUC4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4HUC4; baseline and differential.
DR   Genevisible; F4HUC4; AT.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0098572; C:stromal side of plastid thylakoid membrane; IDA:TAIR.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   PANTHER; PTHR18952:SF217; ALPHA CARBONIC ANHYDRASE 5-RELATED; 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; 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..277
FT                   /note="Alpha carbonic anhydrase 5"
FT                   /id="PRO_0000429731"
FT   DOMAIN          33..269
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         215..216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        58..219
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  32164 MW;  DCC445DD2C627430 CRC64;
     MKIPSIGYVF FLIFISITIV SSSPDHGEVE DETQFNYEKK GEKGPENWGR LKPEWAMCGK
     GNMQSPIDLT DKRVLIDHNL GYLRSQYLPS NATIKNRGHD IMMKFEGGNA GLGITINGTE
     YKLQQIHWHS PSEHTLNGKR FVLEEHMVHQ SKDGRNAVVA FFYKLGKPDY FLLTLERYLK
     RITDTHESQE FVEMVHPRTF GFESKHYYRF IGSLTTPPCS ENVIWTISKE MRTVTLKQLI
     MLRVTVHDQS NSNARPLQRK NERPVALYIP TWHSKLY
//
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