ID A0A093J8E7_FULGA Unreviewed; 495 AA.
AC A0A093J8E7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
DE Flags: Fragment;
GN ORFNames=N327_07331 {ECO:0000313|EMBL:KFW11285.1};
OS Fulmarus glacialis (Northern fulmar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC Fulmarus.
OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW11285.1, ECO:0000313|Proteomes:UP000053806};
RN [1] {ECO:0000313|EMBL:KFW11285.1, ECO:0000313|Proteomes:UP000053806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW11285.1};
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. Its role in saliva is
CC unknown. {ECO:0000256|ARBA:ARBA00025355}.
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|ARBA:ARBA00000943,
CC 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01172}.
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; KK609645; KFW11285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093J8E7; -.
DR Proteomes; UP000053806; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd03125; alpha_CA_VI; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 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; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001759; Pentraxin-related.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF110; CARBONIC ANHYDRASE 6; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR Pfam; PF00354; Pentaxin; 1.
DR PRINTS; PR00895; PENTAXIN.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SMART; SM00159; PTX; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS51828; PTX_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:UP000053806};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT DOMAIN 1..253
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW11285.1"
FT NON_TER 495
FT /evidence="ECO:0000313|EMBL:KFW11285.1"
SQ SEQUENCE 495 AA; 55584 MW; 9A119284E48230F7 CRC64;
EGELDEEHWG KHFAGCAGKH QSPIDIQRKK VRYNPQLLQL ELSGYDGPLQ GDFTMTNNGH
SVQIDLPPTM HISRGLPGLY TAVQMHLHWG GLDLETSGSE HTIDGMRYFA ELHIVHYNSA
DYSSFEEAKD KPHGLAVLAF LYADGHFENT YYSEFISKLA KIRFAGQSTK LLSLDVQAML
PENLSHFYRY QGSLTTPPCS ESVIWTIFHS PIVLSHTQIS LLENTLLDWQ NKTLRNDYRH
AQPLNGRVVE SSFRAKLIQE QCHPEEFNLR LEQIQMQLQD MKRELLNGVS HIGIKSNTFP
AFYFPVENIE SFVNVHPLHD MSLQAFTLCF WARAQRAGSQ TVLSYSTQER DNELVMTVGT
DVGLWIGGHF ISFPLYHKAQ DWLHYCMAWA SQTGMANLWF NGAAGKAKSI QKGYVSQAGG
TLVLGKDRDT LLGTFSNGFA GWMTHVNLWS QVLSPADVRA LALCKPGQLK GDIIAWGETS
MTLLGGVVLE SDTSC
//
