CAH1_CHLRE
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 03-AUG-2022, entry version 149.
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 STRING; 3055.EDP04241; -.
DR iPTMnet; P20507; -.
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; 1377476at2759; -.
DR GO; GO:0042597; C:periplasmic space; 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 CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; -; 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; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 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
