ULAG_ECOSM
ID ULAG_ECOSM Reviewed; 354 AA.
AC B1LQL2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=EcSMS35_4663;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(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}.
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DR EMBL; CP000970; ACB18748.1; -; Genomic_DNA.
DR RefSeq; WP_012311879.1; NC_010498.1.
DR AlphaFoldDB; B1LQL2; -.
DR SMR; B1LQL2; -.
DR EnsemblBacteria; ACB18748; ACB18748; EcSMS35_4663.
DR KEGG; ecm:EcSMS35_4663; -.
DR HOGENOM; CLU_074775_0_0_6; -.
DR OMA; HWDMWKG; -.
DR UniPathway; UPA00263; UER00377.
DR Proteomes; UP000007011; 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_1000140098"
SQ SEQUENCE 354 AA; 40057 MW; 06018935408AB9E9 CRC64;
MSKVKSITRE SWILSTFPEW GSWLNEEIEQ EQVAPGTFAM WWLGCTGIWL KSEGGTNVCV
DFWCGTGKQS HGNPLMKQGH QMQRMAGVKK LQPNLRTTPF VLDPFAIRQI DAVLATHDHN
DHIDVNVAAA VMQNCADDVP FIGPKTCVDL WIGWGVPKER CIVVKPGDVV KVKDIEIHAL
DAFDRTALIT LPADQKAAGV LPDGMDDRAV NYLFKTPGGT LYHSGDSHYS NYYAKHGNEH
QIDVALGSYG ENPRGITDKM TSADILRMGE ALNAKVVIPF HHDIWSNFQA DPQEIRVLWE
MKKDRLKYGF KPFIWQVGGK FTWPLDKDNF EYHYPRGFDD CFTIEPDLPF KSFL
