ID U1NR21_9EURY Unreviewed; 287 AA.
AC U1NR21;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=J07HQX50_01109 {ECO:0000313|EMBL:ERG99955.1};
OS Haloquadratum sp. J07HQX50.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=1238426 {ECO:0000313|EMBL:ERG99955.1, ECO:0000313|Proteomes:UP000030642};
RN [1] {ECO:0000313|EMBL:ERG99955.1, ECO:0000313|Proteomes:UP000030642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HQX50 {ECO:0000313|Proteomes:UP000030642};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
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; KE356562; ERG99955.1; -; Genomic_DNA.
DR AlphaFoldDB; U1NR21; -.
DR STRING; 1238426.J07HQX50_01109; -.
DR HOGENOM; CLU_036110_3_1_2; -.
DR Proteomes; UP000030642; 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:SF47; 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:UP000030642}.
FT DOMAIN 15..252
FT /note="SMP-30/Gluconolactonase/LRE-like region"
FT /evidence="ECO:0000259|Pfam:PF08450"
SQ SEQUENCE 287 AA; 31338 MW; 7728A707E3453186 CRC64;
MHTPTCIADT THHTGEGPLW HPEENRLFWV DIPPGRLYSY DPATKSHSLA YEFPDVPLGG
FTIEQDGALL CFTHSAVLRY VPGSDTATQV ASIDANTRFN DVIADPEGRV FCGTMPGETE
LGDLYRLDPD GQSQVVINDV DISNGMGFSP DLSRFYFTES NTNRIFVYDY AVETGHISNG
RALVETPPDD GIPDGMTVDS AGNIWSARWN GSKIVQYTEA GETLQQVSFP ATKVSAVTFG
GSNYTELYVT TALNDNSRDR EGTRAGGLFR IQDVSPSGTA EYRSDIA
//
