ID   CAH_METTT               Reviewed;         247 AA.
AC   P40881; A0A0E3NC87;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   24-JAN-2024, entry version 123.
DE   RecName: Full=Carbonic anhydrase {ECO:0000303|PubMed:8041719};
DE            Short=CA {ECO:0000303|PubMed:8041719};
DE            Short=Cam {ECO:0000303|PubMed:8665839};
DE            EC=4.2.1.1 {ECO:0000269|PubMed:8041719};
DE   Flags: Precursor;
GN   ORFNames=MSTHT_0588;
OS   Methanosarcina thermophila (strain ATCC 43570 / DSM 1825 / OCM 12 / VKM
OS   B-1830 / TM-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=523844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-60, FUNCTION,
RP   CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1;
RX   PubMed=8041719; DOI=10.1073/pnas.91.15.6909;
RA   Alber B.E., Ferry J.G.;
RT   "A carbonic anhydrase from the archaeon Methanosarcina thermophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:6909-6913(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1;
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0007744|PDB:1THJ}
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 35-247 IN COMPLEX WITH ZINC ION,
RP   POSSIBLE FUNCTION, COFACTOR, AND SUBUNIT.
RX   PubMed=8665839; DOI=10.1002/j.1460-2075.1996.tb00588.x;
RA   Kisker C., Schindelin H., Alber B.E., Ferry J.G., Rees D.C.;
RT   "A left-hand beta-helix revealed by the crystal structure of a carbonic
RT   anhydrase from the archaeon Methanosarcina thermophila.";
RL   EMBO J. 15:2323-2330(1996).
RN   [4] {ECO:0007744|PDB:1QQ0, ECO:0007744|PDB:1QRE, ECO:0007744|PDB:1QRF, ECO:0007744|PDB:1QRG, ECO:0007744|PDB:1QRL, ECO:0007744|PDB:1QRM}
RP   X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP   SUBSTRATE, POSSIBLE FUNCTION, COFACTOR, SUBUNIT, AND ACTIVE SITE.
RX   PubMed=10924115; DOI=10.1021/bi000204s;
RA   Iverson T.M., Alber B.E., Kisker C., Ferry J.G., Rees D.C.;
RT   "A closer look at the active site of gamma-class carbonic anhydrases: high-
RT   resolution crystallographic studies of the carbonic anhydrase from
RT   Methanosarcina thermophila.";
RL   Biochemistry 39:9222-9231(2000).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide. Important for growth
CC       on acetate (PubMed:8041719). As a probably extracellular enzyme, it may
CC       support a H(+)/CH(3)COO(-) symport mechanism and/or conversion of CO(2)
CC       to HCO(3)(-), removing excess CO(2) produced by growth on acetate
CC       (Probable). {ECO:0000269|PubMed:8041719, ECO:0000305|PubMed:10924115,
CC       ECO:0000305|PubMed:8041719, ECO:0000305|PubMed:8665839}.
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; Evidence={ECO:0000269|PubMed:8041719};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:10924115, ECO:0000269|PubMed:8665839};
CC       Note=Binds 1 Zn(2+) per subunit, at the subunit interface.
CC       {ECO:0000269|PubMed:10924115, ECO:0000269|PubMed:8665839};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10924115,
CC       ECO:0000269|PubMed:8665839}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:8041719}. Note=When
CC       isolated from M.thermophila. {ECO:0000269|PubMed:8041719}.
CC   -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC       {ECO:0000305|PubMed:10924115}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AKB12346.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U08885; AAA73428.1; -; Genomic_DNA.
DR   EMBL; CP009501; AKB12346.1; ALT_INIT; Genomic_DNA.
DR   PIR; A57712; A57712.
DR   RefSeq; WP_052721819.1; NZ_CP009501.1.
DR   PDB; 1QQ0; X-ray; 1.76 A; A=1-247.
DR   PDB; 1QRE; X-ray; 1.46 A; A=1-247.
DR   PDB; 1QRF; X-ray; 1.55 A; A=35-247.
DR   PDB; 1QRG; X-ray; 1.72 A; A=35-247.
DR   PDB; 1QRL; X-ray; 1.85 A; A=35-247.
DR   PDB; 1QRM; X-ray; 1.95 A; A=35-247.
DR   PDB; 1THJ; X-ray; 2.80 A; A/B/C=35-247.
DR   PDB; 3OTM; X-ray; 1.50 A; A=36-247.
DR   PDB; 3OTZ; X-ray; 1.60 A; A=35-247.
DR   PDB; 3OU9; X-ray; 1.80 A; A=35-247.
DR   PDB; 3OUP; X-ray; 1.65 A; A=35-247.
DR   PDB; 3OW5; X-ray; 1.80 A; A=35-247.
DR   PDBsum; 1QQ0; -.
DR   PDBsum; 1QRE; -.
DR   PDBsum; 1QRF; -.
DR   PDBsum; 1QRG; -.
DR   PDBsum; 1QRL; -.
DR   PDBsum; 1QRM; -.
DR   PDBsum; 1THJ; -.
DR   PDBsum; 3OTM; -.
DR   PDBsum; 3OTZ; -.
DR   PDBsum; 3OU9; -.
DR   PDBsum; 3OUP; -.
DR   PDBsum; 3OW5; -.
DR   AlphaFoldDB; P40881; -.
DR   SMR; P40881; -.
DR   STRING; 523844.MSTHT_0588; -.
DR   BindingDB; P40881; -.
DR   ChEMBL; CHEMBL3932; -.
DR   DrugCentral; P40881; -.
DR   GeneID; 41601394; -.
DR   KEGG; mthr:MSTHT_0588; -.
DR   PATRIC; fig|523844.20.peg.754; -.
DR   HOGENOM; CLU_064827_3_0_2; -.
DR   BRENDA; 4.2.1.1; 3281.
DR   EvolutionaryTrace; P40881; -.
DR   Proteomes; UP000066529; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0071890; F:bicarbonate binding; IDA:CAFA.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IDA:CACAO.
DR   GO; GO:0050897; F:cobalt ion binding; IDA:CAFA.
DR   GO; GO:0043199; F:sulfate binding; IDA:CAFA.
DR   GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR   CDD; cd00710; LbH_gamma_CA; 1.
DR   DisProt; DP00110; -.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR047223; CA_gamma_LbH.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; NF040597; carb_anhyd; 1.
DR   PANTHER; PTHR43360; CARBON DIOXIDE CONCENTRATING MECHANISM PROTEIN CCMM; 1.
DR   PANTHER; PTHR43360:SF1; CARBOXYSOME ASSEMBLY PROTEIN CCMM; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Lyase; Metal-binding; Secreted;
KW   Signal; Zinc.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000269|PubMed:8041719"
FT   CHAIN           35..247
FT                   /note="Carbonic anhydrase"
FT                   /id="PRO_0000004273"
FT   ACT_SITE        96
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000305|PubMed:10924115"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000305|PubMed:10924115"
FT   BINDING         93..95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:10924115"
FT   BINDING         109..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:10924115"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:10924115,
FT                   ECO:0000269|PubMed:8665839, ECO:0007744|PDB:1QRG,
FT                   ECO:0007744|PDB:1QRL, ECO:0007744|PDB:1QRM,
FT                   ECO:0007744|PDB:1THJ"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:10924115,
FT                   ECO:0000269|PubMed:8665839, ECO:0007744|PDB:1QRG,
FT                   ECO:0007744|PDB:1QRL, ECO:0007744|PDB:1QRM,
FT                   ECO:0007744|PDB:1THJ"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:10924115,
FT                   ECO:0000269|PubMed:8665839, ECO:0007744|PDB:1QRG,
FT                   ECO:0007744|PDB:1QRL, ECO:0007744|PDB:1QRM,
FT                   ECO:0007744|PDB:1THJ"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:10924115"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          73..80
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          91..97
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          113..116
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:1QRG"
FT   TURN            122..124
FT                   /evidence="ECO:0007829|PDB:1QRG"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          137..143
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          154..161
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          172..178
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          189..192
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   HELIX           210..214
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   TURN            224..227
FT                   /evidence="ECO:0007829|PDB:1QRE"
FT   HELIX           228..244
FT                   /evidence="ECO:0007829|PDB:1QRE"
SQ   SEQUENCE   247 AA;  26414 MW;  1256EB566DB9207C CRC64;
     MMFNKQIFTI LILSLSLALA GSGCISEGAE DNVAQEITVD EFSNIRENPV TPWNPEPSAP
     VIDPTAYIDP QASVIGEVTI GANVMVSPMA SIRSDEGMPI FVGDRSNVQD GVVLHALETI
     NEEGEPIEDN IVEVDGKEYA VYIGNNVSLA HQSQVHGPAA VGDDTFIGMQ AFVFKSKVGN
     NCVLEPRSAA IGVTIPDGRY IPAGMVVTSQ AEADKLPEVT DDYAYSHTNE AVVYVNVHLA
     EGYKETS
//