ID   ULAG_SALDC              Reviewed;         354 AA.
AC   B5FS94;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=SeD_A4779;
OS   Salmonella dublin (strain CT_02021853).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT_02021853;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001144; ACH77967.1; -; Genomic_DNA.
DR   RefSeq; WP_000049161.1; NC_011205.1.
DR   AlphaFoldDB; B5FS94; -.
DR   SMR; B5FS94; -.
DR   GeneID; 66758606; -.
DR   KEGG; sed:SeD_A4779; -.
DR   HOGENOM; CLU_074775_0_0_6; -.
DR   OMA; HWDMWKG; -.
DR   UniPathway; UPA00263; UER00377.
DR   Proteomes; UP000008322; 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_1000140101"
SQ   SEQUENCE   354 AA;  40073 MW;  556C9A927A2623D6 CRC64;
     MSKVQSITRE SWILSTFPEW GSWLNEEIEQ EQVAPGTFAM WWLGCTGIWL KSEGGTNVCV
     DFWCGTGKQS HGNPLMKTGH QMQRMAGVKK LQPNLRTTPF VLDPFAIRQI DAVLATHDHN
     DHIDVNVAAA VMQNCADDVP FIGPQTCVDL WVGWGVPKER CIVVKPGDVV KVKDIEIHAL
     DAFDRTALIT LPADQKAAGV LPDGMDVRAV NYLFKTPGGN LYHSGDSHYS NYYAKHGNEH
     QIDVALGSYG ENPRGITDKM TSADILRMAE SLNTKVVIPF HHDIWSNFQA DPQEIRVLWE
     MKKDRLKYGF KPFIWQVGGK FTWPLDKDNF EYHYPRGFDD CFTIEPDLPF KSFL