ID Q8CVC3_STRMU Unreviewed; 256 AA.
AC Q8CVC3;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00014628, ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU367011};
GN Name=cah {ECO:0000313|EMBL:AAN59237.1};
GN OrderedLocusNames=SMU_1595 {ECO:0000313|EMBL:AAN59237.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN59237.1, ECO:0000313|Proteomes:UP000002512};
RN [1] {ECO:0000313|EMBL:AAN59237.1, ECO:0000313|Proteomes:UP000002512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000256|RuleBase:RU367011}.
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 Evidence={ECO:0000256|RuleBase:RU367011};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU367011};
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR EMBL; AE014133; AAN59237.1; -; Genomic_DNA.
DR RefSeq; NP_721931.1; NC_004350.2.
DR RefSeq; WP_002268260.1; NC_004350.2.
DR AlphaFoldDB; Q8CVC3; -.
DR STRING; 210007.SMU_1595; -.
DR GeneID; 66819021; -.
DR KEGG; smu:SMU_1595; -.
DR PATRIC; fig|210007.7.peg.1419; -.
DR eggNOG; COG3338; Bacteria.
DR HOGENOM; CLU_039326_0_2_9; -.
DR OrthoDB; 5327615at2; -.
DR PhylomeDB; Q8CVC3; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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:SF266; CARBONIC ANHYDRASE 2, ISOFORM A; 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 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU367011};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000002512};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..256
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 256 AA; 29230 MW; 08078196F6891CA5 CRC64;
MKKKFIYLTV LVVVAVFCIS TFLTLKGDSQ DREAHWSYSG STSPEHWGDL SDDYKAAKDG
KEQSPINITG AKDVDLPSLQ LNSKNSKAEV ENNGHTIEVK LKNKKNTLKF NGKTYTLEQF
HFHAPSENQI DGKTYPLEGH FVYTTKDKKI TVISILYQYG KENKTLKQVW KKMPQKAETK
KNLSQPVAIS QLFPKDLDYY NFEGSLTTPP CTEGVNWIVF KKQENISKAQ VKKFSKTLGF
NNNRPIQKLN GREIKE
//
