ID A0A1H8PNX7_9SPHI Unreviewed; 297 AA.
AC A0A1H8PNX7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=SAMN05428947_102353 {ECO:0000313|EMBL:SEO43417.1};
OS Mucilaginibacter sp. OK283.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1881049 {ECO:0000313|EMBL:SEO43417.1, ECO:0000313|Proteomes:UP000199509};
RN [1] {ECO:0000313|EMBL:SEO43417.1, ECO:0000313|Proteomes:UP000199509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK283 {ECO:0000313|EMBL:SEO43417.1,
RC ECO:0000313|Proteomes:UP000199509};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FODR01000002; SEO43417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8PNX7; -.
DR STRING; 1881049.SAMN05428947_102353; -.
DR Proteomes; UP000199509; 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}.
FT DOMAIN 18..261
FT /note="SMP-30/Gluconolactonase/LRE-like region"
FT /evidence="ECO:0000259|Pfam:PF08450"
SQ SEQUENCE 297 AA; 33129 MW; 1E7D1E059779A8C6 CRC64;
MALNNTMVQV AVNHASFLGE GPVWDWRNNI LYWVDIMGGH IHEYNPENKN FRTIDVKQMV
GAVTICNDGQ LLAALKNGLA MVDRQSGQPA FFAHPEVHLP QNRFNDGKCD PAGRFWIGSM
AIDETPNAGK LYTLDGNHDI TPKIHGTTIS NGMAWSPDHK TFYYIDTPTM NVVAYDFDAH
SGTISNKKTV ITIDEKDGYP DGMTIDAEGM LWIAHWNGWQ VSRWNPHTAT KLFTLPLPVA
NVTSCTFGGP NLSDLYITTA QKGLTANELM QQPLAGMLFV WKDCGYQGER AFEYKSK
//