ULAG_SALHS
ID ULAG_SALHS Reviewed; 354 AA.
AC B4TFC6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=SeHA_C4800;
OS Salmonella heidelberg (strain SL476).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL476;
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; CP001120; ACF67914.1; -; Genomic_DNA.
DR RefSeq; WP_000049164.1; NC_011083.1.
DR AlphaFoldDB; B4TFC6; -.
DR SMR; B4TFC6; -.
DR KEGG; seh:SeHA_C4800; -.
DR HOGENOM; CLU_074775_0_0_6; -.
DR OMA; HWDMWKG; -.
DR UniPathway; UPA00263; UER00377.
DR Proteomes; UP000001866; 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_1000140104"
SQ SEQUENCE 354 AA; 40072 MW; BF2894783A822996 CRC64;
MSKVQSITRE SWILSTFPEW GSWLNEEIEQ EQVAPGTFAM WWLGCTGIWL KSEGGTNVCV
DFWCGTGKQS HGNPLMKTGH QMQRMAGVKK LQPNLRTTPF VLDPFAIRQI DAVLATHDHN
DHIDVNVAAA VMQNCADNVP FIGPQTCVDL WVGWGVPKER CIVVKPGDVV KVKDIEIHAL
DAFDRTALIT LPADQKAAGV LPDGMDVRAV NYLFKTPGGN LYHSGDSHYS NYYAKHGNEH
QIDVALGSYG ENPRGITDKM TSADILRMAE SLNTKVVIPF HHDIWSNFQA DPQEIRVLWE
MKKDRLKYGF KPFIWQVGGK FTWPLDKDNF EYHYPRGFDD CFTIEPDLPF KSFL