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Database: UniProt
Entry: A0A093RMY5_PYGAD
LinkDB: A0A093RMY5_PYGAD
Original site: A0A093RMY5_PYGAD 
ID   A0A093RMY5_PYGAD        Unreviewed;       299 AA.
AC   A0A093RMY5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Regucalcin {ECO:0000256|ARBA:ARBA00016808};
DE            EC=3.1.1.17 {ECO:0000256|ARBA:ARBA00013227};
DE   AltName: Full=Gluconolactonase {ECO:0000256|ARBA:ARBA00032464};
GN   ORFNames=AS28_02774 {ECO:0000313|EMBL:KFW72239.1};
OS   Pygoscelis adeliae (Adelie penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX   NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW72239.1, ECO:0000313|Proteomes:UP000054081};
RN   [1] {ECO:0000313|EMBL:KFW72239.1, ECO:0000313|Proteomes:UP000054081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW72239.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucono-1,5-lactone + H2O = D-gluconate + H(+);
CC         Xref=Rhea:RHEA:10440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16217, ChEBI:CHEBI:18391; EC=3.1.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00001589};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the SMP-30/CGR1 family.
CC       {ECO:0000256|ARBA:ARBA00008853}.
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DR   EMBL; KL225453; KFW72239.1; -; Genomic_DNA.
DR   RefSeq; XP_009329562.1; XM_009331287.1.
DR   AlphaFoldDB; A0A093RMY5; -.
DR   STRING; 9238.A0A093RMY5; -.
DR   GeneID; 103923039; -.
DR   KEGG; padl:103923039; -.
DR   OrthoDB; 3091635at2759; -.
DR   Proteomes; UP000054081; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0004341; F:gluconolactonase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR008367; Regucalcin.
DR   InterPro; IPR013658; SGL.
DR   InterPro; IPR005511; SMP-30.
DR   PANTHER; PTHR10907; REGUCALCIN; 1.
DR   PANTHER; PTHR10907:SF54; REGUCALCIN; 1.
DR   Pfam; PF08450; SGL; 1.
DR   PRINTS; PR01791; REGUCALCIN.
DR   PRINTS; PR01790; SMP30FAMILY.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054081}.
FT   DOMAIN          16..263
FT                   /note="SMP-30/Gluconolactonase/LRE-like region"
FT                   /evidence="ECO:0000259|Pfam:PF08450"
SQ   SEQUENCE   299 AA;  33287 MW;  6B1ED5CA0E467B92 CRC64;
     MSSVKIECVA KEGYRIGESP VWDEKESALL CVDITGRKVC RWSSVTKQVQ AISVDAPVSS
     VALRKSGDYV ITLGTRFAAL KWKEQLVTTL THVDKDKPNN RFNDGKVDPA GRYFAGTMAE
     EIRPAVLERH QGSLYTLFSD LSVVKHFDQV DISNGLDWSL DHKTFFYIDS LSYSVDAFDY
     DLQTGKIGNR RSIYRLEKEE SIPDGMCIDT EGKLWVACYD GGRVIRLDPE TGKRLQTVKL
     PVDKTTSCCF GGEDYSEMYV TSASDGMDKE WLSRQPQAGG VFKITGLGVK GVPPYPFAG
//
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