CAHC_SPIOL
ID CAHC_SPIOL Reviewed; 319 AA.
AC P16016;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Carbonic anhydrase, chloroplastic;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase;
DE Flags: Precursor;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Hybrid 424;
RX PubMed=2108138; DOI=10.1016/s0021-9258(19)39375-5;
RA Fawcett T.W., Browse J.A., Volokita M., Bartlett S.G.;
RT "Spinach carbonic anhydrase primary structure deduced from the sequence of
RT a cDNA clone.";
RL J. Biol. Chem. 265:5414-5417(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-319, AND PROTEIN SEQUENCE OF 99-118.
RX PubMed=16667262; DOI=10.1104/pp.92.1.37;
RA Burnell J.N., Gibbs M.J., Mason J.G.;
RT "Spinach chloroplastic carbonic anhydrase: nucleotide sequence analysis of
RT cDNA.";
RL Plant Physiol. 92:37-40(1990).
RN [3]
RP PROTEIN SEQUENCE OF 99-118.
RX PubMed=6430173; DOI=10.1111/j.1749-6632.1984.tb12359.x;
RA Hewett-Emmett D., Hopkins P.J., Tashian R.E., Czelusniak J.;
RT "Origins and molecular evolution of the carbonic anhydrase isozymes.";
RL Ann. N. Y. Acad. Sci. 429:338-358(1984).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
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 -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC {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; J05403; AAA34027.1; -; mRNA.
DR EMBL; M27295; AAA34026.1; -; mRNA.
DR PIR; A35163; A35163.
DR AlphaFoldDB; P16016; -.
DR SMR; P16016; -.
DR BRENDA; 4.2.1.1; 5812.
DR SABIO-RK; P16016; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd00884; beta_CA_cladeB; 1.
DR Gene3D; 3.40.1050.10; -; 1.
DR InterPro; IPR045066; Beta_CA_cladeB.
DR InterPro; IPR001765; Carbonic_anhydrase.
DR InterPro; IPR015892; Carbonic_anhydrase_CS.
DR InterPro; IPR036874; Carbonic_anhydrase_sf.
DR PANTHER; PTHR11002; PTHR11002; 1.
DR Pfam; PF00484; Pro_CA; 1.
DR SMART; SM00947; Pro_CA; 1.
DR SUPFAM; SSF53056; SSF53056; 1.
DR PROSITE; PS00704; PROK_CO2_ANHYDRASE_1; 1.
DR PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Lyase; Plastid; Transit peptide;
KW Zinc.
FT TRANSIT 1..98
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:16667262,
FT ECO:0000269|PubMed:6430173"
FT CHAIN 99..319
FT /note="Carbonic anhydrase, chloroplastic"
FT /id="PRO_0000004271"
FT CONFLICT 99
FT /note="E -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="F -> S (in Ref. 2; AAA34026)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="Y -> F (in Ref. 2; AAA34026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 34570 MW; 2229B19F02423EEF CRC64;
MSTINGCLTS ISPSRTQLKN TSTLRPTFIA NSRVNPSSSV PPSLIRNQPV FAAPAPIITP
TLKEDMAYEE AIAALKKLLS EKGELENEAA SKVAQITSEL ADGGTPSASY PVQRIKEGFI
KFKKEKYEKN PALYGELSKG QAPKFMVFAC SDSRVCPSHV LDFQPGEAFM VRNIANMVPV
FDKDKYAGVG AAIEYAVLHL KVENIVVIGH SACGGIKGLM SFPDAGPTTT DFIEDWVKIC
LPAKHKVLAE HGNATFAEQC THCEKEAVNV SLGNLLTYPF VRDGLVKKTL ALQGGYYDFV
NGSFELWGLE YGLSPSQSV
