ID   GNL_ZYMMO               Reviewed;         356 AA.
AC   Q01578; Q5NLY7;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Gluconolactonase {ECO:0000303|PubMed:1482681};
DE            EC=3.1.1.17 {ECO:0000305|PubMed:1482681};
DE   AltName: Full=D-glucono-delta-lactone lactonohydrolase;
DE   Contains:
DE     RecName: Full=Gluconolactonase;
DE   Contains:
DE     RecName: Full=Gluconolactonase minor isoform;
DE   Flags: Precursor;
GN   Name=gnl; OrderedLocusNames=ZMO1649;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-58, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC   11199 / NRRL B-4490 / ZM6;
RX   PubMed=1482681; DOI=10.1016/0167-4781(92)90120-o;
RA   Kanagasundaram V., Scopes R.;
RT   "Isolation and characterization of the gene encoding gluconolactonase from
RT   Zymomonas mobilis.";
RL   Biochim. Biophys. Acta 1171:198-200(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
CC   -!- FUNCTION: Hydrolyzes the gluconolactone formed by glucose-fructose
CC       oxidoreductase, and that formed in aerobic conditions by the glucose
CC       dehydrogenase present. {ECO:0000305|PubMed:1482681}.
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:0000305|PubMed:1482681};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate biosynthesis; D-
CC       gluconate from D-glucono-1,5-lactone: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1482681}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:1482681}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has been experimentally proven.
CC       {ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000269|PubMed:1482681}.
CC   -!- CAUTION: It is possible that in some cases Met-40 is the initiator in
CC       this case the expressed enzyme would remain cytoplasmic.
CC       {ECO:0000305|PubMed:1482681}.
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DR   EMBL; X67189; CAA47637.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV90273.1; -; Genomic_DNA.
DR   PIR; S28218; S28218.
DR   RefSeq; WP_011241398.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q01578; -.
DR   SMR; Q01578; -.
DR   STRING; 264203.ZMO1649; -.
DR   EnsemblBacteria; AAV90273; AAV90273; ZMO1649.
DR   GeneID; 58027364; -.
DR   KEGG; zmo:ZMO1649; -.
DR   eggNOG; COG3386; Bacteria.
DR   HOGENOM; CLU_036110_0_0_5; -.
DR   OMA; PAIWAEG; -.
DR   OrthoDB; 966287at2; -.
DR   BioCyc; MetaCyc:MON-13276; -.
DR   BRENDA; 3.1.1.17; 14380.
DR   UniPathway; UPA00814; UER00785.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004341; F:gluconolactonase activity; IDA:CACAO.
DR   GO; GO:0046178; P:D-gluconate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR013658; SGL.
DR   InterPro; IPR005511; SMP-30.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF08450; SGL; 1.
DR   PRINTS; PR01790; SMP30FAMILY.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Periplasm; Reference proteome;
KW   Serine esterase; Signal.
FT   SIGNAL          1..35
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT                   ECO:0000269|PubMed:1482681"
FT   CHAIN           36..356
FT                   /note="Gluconolactonase"
FT                   /id="PRO_0000021336"
FT   CHAIN           41..356
FT                   /note="Gluconolactonase minor isoform"
FT                   /evidence="ECO:0000305|PubMed:1482681"
FT                   /id="PRO_0000021337"
FT   CONFLICT        34
FT                   /note="Q -> E (in Ref. 1; CAA47637)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="Missing (in Ref. 1; CAA47637)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320..356
FT                   /note="SGNPGQPLSNCCFGEKGQTLFISASHNVVRVRTKTFG -> FW (in Ref.
FT                   1; CAA47637)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   356 AA;  38453 MW;  4B9D922A8AED9262 CRC64;
     MTTGRMSRRE CLSAAVMVPI AAMTATATIT GSAQAAKNNM NGSTIGKITK FSPRLDAILD
     VSTPIEVIAS DIQWSEGPVW VKNGNFLLFS DPPANIMRKW TPDAGVSIFL KPSGHAEPIP
     AGQFREPGSN GMKVGPDGKI WVADSGTRAI MKVDPVTRQR SVVVDNYKGK RFNSPNDLFF
     SKSGAVYFTD PPYGLTNLDE SDIKEMNYNG VFRLSPDGRL DLIEAGLSRP NGLALSPDET
     KLYVSNSDRA SPNIWVYSLD SNGLPTSRTL LRNFRKEYFD QGLAGLPDGM NIDKQGNLFA
     SAPGGIYIFA PDGECLGLIS GNPGQPLSNC CFGEKGQTLF ISASHNVVRV RTKTFG