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Database: UniProt
Entry: A0A1S3B6Q0_CUCME
LinkDB: A0A1S3B6Q0_CUCME
Original site: A0A1S3B6Q0_CUCME 
ID   A0A1S3B6Q0_CUCME        Unreviewed;       273 AA.
AC   A0A1S3B6Q0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Alpha carbonic anhydrase 1, chloroplastic {ECO:0000313|RefSeq:XP_008442846.1};
GN   Name=LOC103486616 {ECO:0000313|RefSeq:XP_008442846.1};
GN   Synonyms=103486616 {ECO:0000313|EnsemblPlants:MELO3C009476.2.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008442846.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|EnsemblPlants:MELO3C009476.2.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_008442846.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|ARBA:ARBA00002904}.
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000256|ARBA:ARBA00004470}.
CC   -!- SIMILARITY: Belongs to the alpha-class carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00006365}.
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DR   RefSeq; XP_008442846.1; XM_008444624.2.
DR   EnsemblPlants; MELO3C009476.2.1; MELO3C009476.2.1; MELO3C009476.2.
DR   GeneID; 103486616; -.
DR   Gramene; MELO3C009476.2.1; MELO3C009476.2.1; MELO3C009476.2.
DR   KEGG; cmo:103486616; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   InParanoid; A0A1S3B6Q0; -.
DR   OrthoDB; 751784at2759; -.
DR   Proteomes; UP000089565; Unplaced.
DR   Proteomes; UP000596662; Unplaced.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
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; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF266; CARBONIC ANHYDRASE 2, ISOFORM A; 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   Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..273
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041122239"
FT   DOMAIN          30..268
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   273 AA;  30314 MW;  6194BCE048322E6B CRC64;
     MAPPFSSIFA FSLLFVGVLV QAHDQVGQSA VFTYEGSHGP EKWGSLSPSY ATCSNGKFQS
     PVDISKDNSV FGKKLQTLVR KYNIANATLT NNGVNIGVHF WKNSGGVAII DGKNYTLKQL
     HWHSPAEHRL NGKQYAAELH LVHQADDGTY SVIAILLQIG DPEPLLAKIH DKLVELANEK
     CGSNEEAHIA LGDLDTKHLR KKTRKYFRYI GSLTTPPCTE NVIWNVLGKV RTISQQQVDA
     LKAPLNPVYK NNARPVQPLY GRKIEIYDEL SKH
//
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