ID K1RJ02_CRAGI Unreviewed; 543 AA.
AC K1RJ02;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN ORFNames=CGI_10014170 {ECO:0000313|EMBL:EKC34226.1};
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:EKC34226.1};
RN [1] {ECO:0000313|EMBL:EKC34226.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC34226.1};
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 -!- SIMILARITY: Belongs to the globin family.
CC {ECO:0000256|ARBA:ARBA00008705, ECO:0000256|PROSITE-ProRule:PRU00238}.
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; JH816257; EKC34226.1; -; Genomic_DNA.
DR AlphaFoldDB; K1RJ02; -.
DR HOGENOM; CLU_501791_0_0_1; -.
DR InParanoid; K1RJ02; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd00326; alpha_CA; 1.
DR CDD; cd12137; GbX; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 2.
DR Gene3D; 1.10.490.10; Globins; 1.
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 InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF265; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00194; Carb_anhydrase; 2.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00188; PLANTGLOBIN.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR SUPFAM; SSF46458; Globin-like; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS01033; GLOBIN; 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 Signal {ECO:0000256|RuleBase:RU367011};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT CHAIN 21..543
FT /note="Carbonic anhydrase"
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT /id="PRO_5036530371"
FT DOMAIN 42..399
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 390..520
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
SQ SEQUENCE 543 AA; 62395 MW; AA54429856AD4693 CRC64;
MAQCLSSVVL LWISLGTVLG AGFLGVRPQS NDKCRYDDIN EAHFSYDQNH CEGPMKWCNV
HQCWSTCGSN IRQSPINIQT AETIREGFGD LQFRNLHLRV PANISNNGHS PDFDCKVETD
EALRLKKNII LTNVPMRGDK QYIFAQLHIH IGNETNRTSD SNINDDEGSE HSIDGQFYPM
EAHLVFYDSS FDNIGVAKPV NDSLVVLGVM IKDKDLCSLE EGKMNEKFYR KHCYRKRTKC
KGRFAKRLSD NMEHYFEEIR NHDPVKPDLE KSSDDDIREY QCGDHPDLDF IYNNCMKRST
YESRNYREVE SGISPLDVLP CDQSFYTYAG SLTTPPCYET VQWIVFKCPI TVSKKAYRNL
QLVQDSNEDD LKLLGVKRHI MTRGGPEPSL SEDQLELLEK SWNSIKVNIA NIGVVAFMNL
FQTHPEVKDA FLPFQQLAED DMEHSAILRS HALRVMGTVD KCLTRIRTPE KLQSLMHELG
ERHVNYSAKY DFIDMVGGQF VHAIKPHLQD SWSEELGEAW VQLFRVLCYY MKKGMRDNNA
NAD
//
