CAHC_PEA
ID CAHC_PEA Reviewed; 328 AA.
AC P17067;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Carbonic anhydrase, chloroplastic;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase;
DE Contains:
DE RecName: Full=Carbonic anhydrase, 27 kDa isoform;
DE Contains:
DE RecName: Full=Carbonic anhydrase, 25 kDa isoform;
DE Flags: Precursor;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2113277; DOI=10.1093/nar/18.11.3413;
RA Roeske C.A., Ogren W.L.;
RT "Nucleotide sequence of pea cDNA encoding chloroplast carbonic anhydrase.";
RL Nucleic Acids Res. 18:3413-3413(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16667962; DOI=10.1104/pp.95.1.264;
RA Majeau N., Coleman J.R.;
RT "Isolation and characterization of a cDNA coding for pea chloroplastic
RT carbonic anhydrase.";
RL Plant Physiol. 95:264-268(1991).
RN [3]
RP PROTEIN SEQUENCE OF 71-76 AND 108-113, AND PROTEOLYTIC PROCESSING.
RX PubMed=1468554; DOI=10.1016/0014-5793(92)81478-5;
RA Johansson I.-M., Forsman C.;
RT "Processing of the chloroplast transit peptide of pea carbonic anhydrase in
RT chloroplasts and in Escherichia coli. Identification of two cleavage
RT sites.";
RL FEBS Lett. 314:232-236(1992).
RN [4]
RP MUTAGENESIS.
RX PubMed=8400138; DOI=10.1007/bf00028967;
RA Provart N.J., Majeau N., Coleman J.R.;
RT "Characterization of pea chloroplastic carbonic anhydrase. Expression in
RT Escherichia coli and site-directed mutagenesis.";
RL Plant Mol. Biol. 22:937-943(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 108-328.
RX PubMed=10747009; DOI=10.1093/emboj/19.7.1407;
RA Kimber M.S., Pai E.F.;
RT "The active site architecture of Pisum sativum beta-carbonic anhydrase is a
RT mirror image of that of alpha-carbonic anhydrases.";
RL EMBO J. 19:1407-1418(2000).
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; X52558; CAA36792.1; -; mRNA.
DR EMBL; M63627; AAA33652.1; -; mRNA.
DR PIR; S10200; S10200.
DR PDB; 1EKJ; X-ray; 1.93 A; A/B/C/D/E/F/G/H=108-328.
DR PDBsum; 1EKJ; -.
DR AlphaFoldDB; P17067; -.
DR SMR; P17067; -.
DR EnsemblPlants; Psat1g058960.3; Psat1g058960.3.cds; Psat1g058960.
DR EnsemblPlants; Psat1g058960.4; Psat1g058960.4.cds; Psat1g058960.
DR EnsemblPlants; Psat1g058960.5; Psat1g058960.5.cds; Psat1g058960.
DR Gramene; Psat1g058960.3; Psat1g058960.3.cds; Psat1g058960.
DR Gramene; Psat1g058960.4; Psat1g058960.4.cds; Psat1g058960.
DR Gramene; Psat1g058960.5; Psat1g058960.5.cds; Psat1g058960.
DR BRENDA; 4.2.1.1; 4872.
DR EvolutionaryTrace; P17067; -.
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 3D-structure; Chloroplast; Direct protein sequencing; Lyase; Plastid;
KW Transit peptide; Zinc.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:1468554"
FT CHAIN 71..328
FT /note="Carbonic anhydrase, 27 kDa isoform"
FT /id="PRO_0000004269"
FT CHAIN 108..328
FT /note="Carbonic anhydrase, 25 kDa isoform"
FT /id="PRO_0000004270"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 159
FT /note="C->S: 100% loss of activity."
FT /evidence="ECO:0000269|PubMed:8400138"
FT MUTAGEN 168
FT /note="H->N: Small loss of activity."
FT /evidence="ECO:0000269|PubMed:8400138"
FT MUTAGEN 203
FT /note="E->A: 100% loss of activity."
FT /evidence="ECO:0000269|PubMed:8400138"
FT MUTAGEN 208
FT /note="H->N: Small loss of activity."
FT /evidence="ECO:0000269|PubMed:8400138"
FT MUTAGEN 219
FT /note="H->N: 100% loss of activity."
FT /evidence="ECO:0000269|PubMed:8400138"
FT MUTAGEN 222
FT /note="C->S: 100% loss of activity."
FT /evidence="ECO:0000269|PubMed:8400138"
FT MUTAGEN 275
FT /note="E->A: Small loss of activity."
FT /evidence="ECO:0000269|PubMed:8400138"
FT CONFLICT 31
FT /note="S -> F (in Ref. 2; AAA33652)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="S -> SS (in Ref. 2; AAA33652)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="E -> K (in Ref. 2; AAA33652)"
FT /evidence="ECO:0000305"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:1EKJ"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:1EKJ"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:1EKJ"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1EKJ"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:1EKJ"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:1EKJ"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 265..284
FT /evidence="ECO:0007829|PDB:1EKJ"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:1EKJ"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:1EKJ"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:1EKJ"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:1EKJ"
SQ SEQUENCE 328 AA; 35377 MW; DD26766D96483B2B CRC64;
MSTSSINGFS LSSLSPAKTS TKRTTLRPFV SASLNTSSSS SSSTFPSLIQ DKPVFASSSP
IITPVLREEM GKGYDEAIEE LQKLLREKTE LKATAAEKVE QITAQLGTTS SSDGIPKSEA
SERIKTGFLH FKKEKYDKNP ALYGELAKGQ SPPFMVFACS DSRVCPSHVL DFQPGEAFVV
RNVANLVPPY DQAKYAGTGA AIEYAVLHLK VSNIVVIGHS ACGGIKGLLS FPFDGTYSTD
FIEEWVKIGL PAKAKVKAQH GDAPFAELCT HCEKEAVNAS LGNLLTYPFV REGLVNKTLA
LKGGYYDFVK GSFELWGLEF GLSSTFSV
