ID   ULAG_SALG2              Reviewed;         354 AA.
AC   B5R9D9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-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=SG4224;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(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}.
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; AM933173; CAR39987.1; -; Genomic_DNA.
DR   RefSeq; WP_000049162.1; NC_011274.1.
DR   AlphaFoldDB; B5R9D9; -.
DR   SMR; B5R9D9; -.
DR   EnsemblBacteria; CAR39987; CAR39987; SG4224.
DR   KEGG; seg:SG4224; -.
DR   HOGENOM; CLU_074775_0_0_6; -.
DR   OMA; HWDMWKG; -.
DR   UniPathway; UPA00263; UER00377.
DR   Proteomes; UP000008321; 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_1000140103"
SQ   SEQUENCE   354 AA;  40103 MW;  48C7EA863F327293 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 TSTDILRMAE SLNTKVVIPF HHDIWSNFQA DPQEIRVLWE
     MKKDRLKYGF KPFIWQVGGK FTWPLDKDNF EYHYPRGFDD CFTIEPDLPF KSFL