CAH_METTT
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 03-AUG-2022, entry version 118.
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_CP009502.1.
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 EnsemblBacteria; AKB12346; AKB12346; MSTHT_0588.
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 DisProt; DP00110; -.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 2.
DR SUPFAM; SSF51161; SSF51161; 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
