ID   ULAG_ECOSE              Reviewed;         354 AA.
AC   B6I297;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Probable L-ascorbate-6-phosphate lactonase UlaG {ECO:0000255|HAMAP-Rule:MF_01266};
DE            EC=3.1.1.- {ECO:0000255|HAMAP-Rule:MF_01266};
DE   AltName: Full=L-ascorbate utilization protein G {ECO:0000255|HAMAP-Rule:MF_01266};
GN   Name=ulaG {ECO:0000255|HAMAP-Rule:MF_01266}; OrderedLocusNames=ECSE_4490;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
CC   -!- FUNCTION: Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3-
CC       keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under
CC       anaerobic conditions. {ECO:0000255|HAMAP-Rule:MF_01266}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-ascorbate 6-phosphate = 3-dehydro-L-gulonate 6-
CC         phosphate; Xref=Rhea:RHEA:28803, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58774, ChEBI:CHEBI:61698; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01266};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01266};
CC   -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC       phosphate from L-ascorbate: step 1/4. {ECO:0000255|HAMAP-
CC       Rule:MF_01266}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01266}.
CC   -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC       {ECO:0000255|HAMAP-Rule:MF_01266}.
CC   -!- SIMILARITY: Belongs to the UlaG family. {ECO:0000255|HAMAP-
CC       Rule:MF_01266}.
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DR   EMBL; AP009240; BAG80014.1; -; Genomic_DNA.
DR   RefSeq; WP_001295191.1; NC_011415.1.
DR   AlphaFoldDB; B6I297; -.
DR   SMR; B6I297; -.
DR   EnsemblBacteria; BAG80014; BAG80014; ECSE_4490.
DR   GeneID; 66671895; -.
DR   KEGG; ecy:ECSE_4490; -.
DR   HOGENOM; CLU_074775_0_0_6; -.
DR   OMA; HWDMWKG; -.
DR   UniPathway; UPA00263; UER00377.
DR   Proteomes; UP000008199; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035460; F:L-ascorbate 6-phosphate lactonase activity; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_01266; UlaG; 1.
DR   InterPro; IPR023951; L-ascorbate_6P_UlaG.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..354
FT                   /note="Probable L-ascorbate-6-phosphate lactonase UlaG"
FT                   /id="PRO_1000140097"
SQ   SEQUENCE   354 AA;  40061 MW;  00DECD310615BF66 CRC64;
     MSKVKSITRE SWILSTFPEW GSWLNEEIEQ EQVAPGTFAM WWLGCTGIWL KSEGGTNVCV
     DFWCGTGKQS HGNPLMKQGH QMQRMAGVKK LQPNLRTTPF VLDPFAIRQI DAVLATHDHN
     DHIDVNVAAA VMQNCADDVP FIGPKTCVDL WIGWGVPKER CIVVKPGDVV KVKDIEIHAL
     DAFDRTALIT LPADQKAAGV LPDGMDDRAV NYLFKTPGGS LYHSGDSHYS NYYAKHGNEH
     QIDVALGSYG ENPRGITDKM TSADMLRMGE ALNAKVVIPF HHDIWSNFQA DPQEIRVLWE
     MKKDRLKYGF KPFIWQVGGK FTWPLDKDNF EYHYPRGFDD CFTIEPDLPF KSFL