GenomeNet

Database: UniProt
Entry: K1QUE3_CRAGI
LinkDB: K1QUE3_CRAGI
Original site: K1QUE3_CRAGI 
ID   K1QUE3_CRAGI            Unreviewed;       678 AA.
AC   K1QUE3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN   ORFNames=CGI_10027598 {ECO:0000313|EMBL:EKC34889.1};
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC34889.1};
RN   [1] {ECO:0000313|EMBL:EKC34889.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC34889.1};
RX   PubMed=22992520; DOI=10.1038/nature11413;
RA   Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA   Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA   Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA   Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA   Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA   Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA   Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA   Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA   Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA   Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA   Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT   "The oyster genome reveals stress adaptation and complexity of shell
RT   formation.";
RL   Nature 490:49-54(2012).
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|RuleBase:RU367011};
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH816283; EKC34889.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1QUE3; -.
DR   HOGENOM; CLU_405589_0_0_1; -.
DR   InParanoid; K1QUE3; -.
DR   GO; GO:0005576; C:extracellular region; 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; cd00326; alpha_CA; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 2.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
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; 2.
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|RuleBase:RU367011};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367011}; Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
SQ   SEQUENCE   678 AA;  76517 MW;  28D8EDD972A3FD20 CRC64;
     MDKYIIVAIC IVIDSEVQAD MCYENGIDVC CSGYILNKTS GQCDKCPPGY TGMECAYRCH
     YPTYGEDCFM TCECSADLCD FAYGCFYTST TECPPGYTGS DCVYKCLYPY YGDDCLMKCR
     CSADLCDFVS GCKHTTVTVT SSEHQITSTK DNLNKIYKQC RHAFISPLID YLALNGIEVC
     CSGYRLNNTS GNCDKCPPGY IGMDCAYRCH YPTYGEDCFM ACECPADLCD FVSGCKVTST
     TETDNIRKIV QVILPGPKRA KNLNSDGYIQ VSRGTRKECP PGYTGSDCAY RCHYPTYGED
     CFMTCECSAD LCDFVSGETI SFKSGILQST NNNEKYATLT RHFITLGMEK PPRQNKYKGT
     DHGDSHASGH SPHFETESEA VGLYNVPGLP GQKFIFNEFH VHLGRSFSHG SEHLIDGNKF
     PMEAHLVFYN ARYGDAVTAK RSPRGLAVIG VMIQVAGDDD DDESGDDYEE RKDKDCGERR
     HRPYSRCVCN DNDPYSAYSC KSSGQCKCDD DNDCPGSSKC RRNDVIPGRY CGKPKRCRVR
     YARKLSYLME KYYKKIRYYN NVADGLDDRE WVDVTEGITP SEVLPYDWSY FTYQGSLTTP
     PCFETVTWIN MRCPIKVSKR AYKHLSLVRD VNGAYLKKFG LDRPPQRGTY DGPRVTIERN
     FQWDSVGRET LFCSQDRY
//
DBGET integrated database retrieval system