ID A0A091RF48_9GRUI Unreviewed; 252 AA.
AC A0A091RF48;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
DE Flags: Fragment;
GN ORFNames=N332_13191 {ECO:0000313|EMBL:KFQ27257.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ27257.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ27257.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ27257.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KK798851; KFQ27257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RF48; -.
DR Proteomes; UP000053369; Unassembled WGS sequence.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd03149; alpha_CA_VII; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR InterPro; IPR041890; Alpha_CA_VII.
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:SF124; CARBONIC ANHYDRASE 7; 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|RuleBase:RU367011};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000053369};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT DOMAIN 1..250
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ27257.1"
FT NON_TER 252
FT /evidence="ECO:0000313|EMBL:KFQ27257.1"
SQ SEQUENCE 252 AA; 28441 MW; FA0145C8628DA8FA CRC64;
EGPSEWHKSY PIAQGNRQSP IDIVSARAVY DPNLKPLIVS YESCSSLNIS NNGHSVMVEF
EDTDDKTAIS GGPFENPFRL KQFHFHWGTK HSQGSEHTID GKPFPCELHL VHWNARKYAT
FGEAAAAPDG LAVVGVFLET GKEHANMNRL TDALYMVKFK GTKAQFRSFN PKCLLPLSLD
YWTYLGSLTT PPLNESVTWI VLKEPISVSE KQLEKFRMLL FTSEEDKKIQ MVNNFRPPQP
LKGRVVRASF KA
//