ID   ULAG_SHIFL              Reviewed;         354 AA.
AC   Q83IJ0; Q7BYI7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 115.
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};
GN   OrderedLocusNames=SF4347, S4617;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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=AAN45764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAP19546.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005674; AAN45764.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014073; AAP19546.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_710057.1; NC_004337.2.
DR   RefSeq; WP_005053827.1; NZ_WPGW01000113.1.
DR   AlphaFoldDB; Q83IJ0; -.
DR   SMR; Q83IJ0; -.
DR   STRING; 198214.SF4347; -.
DR   EnsemblBacteria; AAN45764; AAN45764; SF4347.
DR   EnsemblBacteria; AAP19546; AAP19546; S4617.
DR   GeneID; 1025412; -.
DR   KEGG; sfl:SF4347; -.
DR   KEGG; sft:NCTC1_04722; -.
DR   KEGG; sfx:S4617; -.
DR   PATRIC; fig|198214.7.peg.5126; -.
DR   HOGENOM; CLU_074775_0_0_6; -.
DR   OrthoDB; 767622at2; -.
DR   UniPathway; UPA00263; UER00377.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome.
FT   CHAIN           1..354
FT                   /note="Probable L-ascorbate-6-phosphate lactonase UlaG"
FT                   /id="PRO_0000231491"
SQ   SEQUENCE   354 AA;  40043 MW;  F4DACD310612A40B 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
     IKKDRLKYGF KPFIWQVGGK FTWPLDKDNF EYHYPRGFDD CFTIEPDLPF KSFL