ID W0EZU0_9BACT Unreviewed; 301 AA.
AC W0EZU0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=NIASO_07915 {ECO:0000313|EMBL:AHF15103.1};
OS Niabella soli DSM 19437.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niabella.
OX NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF15103.1, ECO:0000313|Proteomes:UP000003586};
RN [1] {ECO:0000313|EMBL:AHF15103.1, ECO:0000313|Proteomes:UP000003586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007035; AHF15103.1; -; Genomic_DNA.
DR AlphaFoldDB; W0EZU0; -.
DR STRING; 929713.NIASO_07915; -.
DR KEGG; nso:NIASO_07915; -.
DR eggNOG; COG3386; Bacteria.
DR HOGENOM; CLU_036110_3_1_10; -.
DR OrthoDB; 2633250at2; -.
DR Proteomes; UP000003586; Chromosome.
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:UP000003586}.
FT DOMAIN 16..258
FT /note="SMP-30/Gluconolactonase/LRE-like region"
FT /evidence="ECO:0000259|Pfam:PF08450"
SQ SEQUENCE 301 AA; 33370 MW; B6BEC385081A2C53 CRC64;
MLFTMIEIAC EHKTQLGEGP VWDEQKNILY WVDIAKGIIH ELNVLSGKHA SYTIGQLTGA
IALCNNNDLL VAAQKGPGIF NTHKHSFIQQ PPPYPATTAN RFNDGKCDAA GRFWLGTMAL
DEKKAAGSLF CMTEDFTFRK MLPHLTIPNG MAWTSDNKIF YFIDTPAFAV MAYDFDLATA
QISNPRKVIT IKEKEGAPDG MTIDKEGMLW IAHWDGWQVT RWDPETGAQL LSVRLPVARV
TSCTFGGPAL SDLYITTACD RLNPDQYNAQ PHAGALFVWS NSGFTGMPAN RFQTKHVLPA
I
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