ID   ULAG_SALCH              Reviewed;         354 AA.
AC   Q57GK0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 90.
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=SCH_4256;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAX68162.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017220; AAX68162.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001541373.1; NC_006905.1.
DR   AlphaFoldDB; Q57GK0; -.
DR   SMR; Q57GK0; -.
DR   EnsemblBacteria; AAX68162; AAX68162; SCH_4256.
DR   KEGG; sec:SCH_4256; -.
DR   HOGENOM; CLU_074775_0_0_6; -.
DR   UniPathway; UPA00263; UER00377.
DR   Proteomes; UP000000538; 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_0000231485"
SQ   SEQUENCE   354 AA;  40087 MW;  EE663A837A2733C7 CRC64;
     MSKVQSITRE SWILSTFPEW GSWLNEEIEQ EQVAPGTFAM WWLGCTGIWL KSEGGTNVCV
     DFWCGTGKQS HGNPLMKTGH QMQRMAGVKK LQPNLRTTPF VLDPFAIRQI DAVLATHDHN
     DHIDVNVAAA VMQNCADDVP FIGPQTCVDL WVGWGVPKER CIVVKPGDVV KVKDIEIHAL
     DAFDRTALIT LPADQKAAGV LPEGMDVRAV NYLFKTPGGN LYHSGDSHYS NYYAKHGNEH
     QIDVALGSYG ENPRGITDKM TSADILRMAE SLNTKVVIPF HHDIWSNFQA DPQEIRVLWE
     MKKDRLKYGF KPFIWQVGGK FTWPLDKDNF EYHYPRGFDD CFTIEPDLPF KSFL