ID   CAH1_CHLRE              Reviewed;         377 AA.
AC   P20507;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Carbonic anhydrase 1;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase 1;
DE            Short=CA1;
DE   Contains:
DE     RecName: Full=Carbonic anhydrase 1 large chain;
DE   Contains:
DE     RecName: Full=Carbonic anhydrase 1 small chain;
DE   Flags: Precursor;
GN   Name=CAH1;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2112252; DOI=10.1073/pnas.87.11.4383;
RA   Fukuzawa H., Fujiwara S., Yamamoto Y., Dionisio-Sese M.L., Miyachi S.;
RT   "cDNA cloning, sequence, and expression of carbonic anhydrase in
RT   Chlamydomonas reinhardtii: regulation by environmental CO2 concentration.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4383-4387(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2124702; DOI=10.1073/pnas.87.24.9779;
RA   Fujiwara S., Fukuzawa H., Tachiki A., Miyachi S.;
RT   "Structure and differential expression of two genes encoding carbonic
RT   anhydrase in Chlamydomonas reinhardtii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9779-9783(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IAM C-9;
RX   PubMed=2243800; DOI=10.1093/nar/18.21.6441;
RA   Fukuzawa H., Fujiwara S., Tachiki A., Miyachi S.;
RT   "Nucleotide sequences of two genes CAH1 and CAH2 which encode carbonic
RT   anhydrase polypeptides in Chlamydomonas reinhardtii.";
RL   Nucleic Acids Res. 18:6441-6442(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 21-37 AND 341-377.
RX   PubMed=2120056; DOI=10.1111/j.1432-1033.1990.tb19261.x;
RA   Kamo T., Shimogawara K., Fukuzawa H., Muto S., Miyachi S.;
RT   "Subunit constitution of carbonic anhydrase from Chlamydomonas
RT   reinhardtii.";
RL   Eur. J. Biochem. 192:557-562(1990).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-101;
RP   ASN-135 AND ASN-297.
RX   PubMed=8508810; DOI=10.1111/j.1432-1033.1993.tb17890.x;
RA   Ishida S., Muto S., Miyachi S.;
RT   "Structural analysis of periplasmic carbonic anhydrase 1 of Chlamydomonas
RT   reinhardtii.";
RL   Eur. J. Biochem. 214:9-16(1993).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC   -!- SUBUNIT: Tetramer of two large and two small subunits linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- INDUCTION: Requires light in addition to a decrease in CO(2)
CC       concentration during growth.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; D90206; BAA14232.2; -; Genomic_DNA.
DR   PIR; S14187; A35795.
DR   RefSeq; XP_001692291.1; XM_001692239.1.
DR   PDB; 3B1B; X-ray; 1.88 A; A/B=1-377.
DR   PDBsum; 3B1B; -.
DR   AlphaFoldDB; P20507; -.
DR   SMR; P20507; -.
DR   GlyCosmos; P20507; 3 sites, No reported glycans.
DR   iPTMnet; P20507; -.
DR   PaxDb; 3055-EDP04241; -.
DR   ProMEX; P20507; -.
DR   EnsemblPlants; PNW84147; PNW84147; CHLRE_04g223100v5.
DR   GeneID; 5717875; -.
DR   Gramene; PNW84147; PNW84147; CHLRE_04g223100v5.
DR   KEGG; cre:CHLRE_04g223100v5; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   HOGENOM; CLU_728358_0_0_1; -.
DR   OMA; MNENDQA; -.
DR   OrthoDB; 314900at2759; -.
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   InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR   PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF265; CARBONIC ANHYDRASE; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Lyase; Metal-binding; Periplasm; Signal; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:2120056"
FT   CHAIN           21..377
FT                   /note="Carbonic anhydrase 1"
FT                   /id="PRO_0000004257"
FT   CHAIN           21..305
FT                   /note="Carbonic anhydrase 1 large chain"
FT                   /id="PRO_0000004258"
FT   CHAIN           341..377
FT                   /note="Carbonic anhydrase 1 small chain"
FT                   /id="PRO_0000004259"
FT   DOMAIN          38..318
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        112
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         260..261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8508810"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8508810"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8508810"
FT   DISULFID        21
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:8508810"
FT   DISULFID        61..264
FT                   /evidence="ECO:0000269|PubMed:8508810"
FT   DISULFID        194..198
FT                   /evidence="ECO:0000269|PubMed:8508810"
FT   DISULFID        296..351
FT                   /note="Interchain (between large and small chains)"
FT                   /evidence="ECO:0000269|PubMed:8508810"
FT   STRAND          36..38
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   TURN            43..48
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   TURN            61..63
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   HELIX           74..78
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          101..109
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          114..120
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          125..133
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   HELIX           142..145
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          152..167
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          169..172
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          178..187
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   HELIX           192..194
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          198..212
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   TURN            215..217
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   HELIX           218..221
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          230..233
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   HELIX           242..245
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          252..258
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          266..275
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          277..280
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   HELIX           281..290
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          293..298
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   HELIX           346..348
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          350..355
FT                   /evidence="ECO:0007829|PDB:3B1B"
FT   STRAND          371..374
FT                   /evidence="ECO:0007829|PDB:3B1B"
SQ   SEQUENCE   377 AA;  41628 MW;  26500D573313EB3D CRC64;
     MARTGALLLV ALALAGCAQA CIYKFGTSPD SKATVSGDHW DHGLNGENWE GKDGAGNAWV
     CKTGRKQSPI NVPQYQVLDG KGSKIANGLQ TQWSYPDLMS NGTSVQVINN GHTIQVQWTY
     NYAGHATIAI PAMHNQTNRI VDVLEMRPND AADRVTAVPT QFHFHSTSEH LLAGKIYPLE
     LHIVHQVTEK LEACKGGCFS VTGILFQLDN GPDNELLEPI FANMPSREGT FSNLPAGTTI
     KLGELLPSDR DYVTYEGSLT TPPCSEGLLW HVMTQPQRIS FGQWNRYRLA VGLKECNSTE
     TAADAGHHHH HRRLLHNHAH LEEVPAATSE PKHYFRRVML AESANPDAYT CKAVAFGQNF
     RNPQYANGRT IKLARYH
//