ULAG_ECODH
ID ULAG_ECODH Reviewed; 354 AA.
AC B1XDU3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=ECDH10B_4387;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(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; CP000948; ACB05180.1; -; Genomic_DNA.
DR RefSeq; WP_001295191.1; NC_010473.1.
DR AlphaFoldDB; B1XDU3; -.
DR SMR; B1XDU3; -.
DR GeneID; 66671895; -.
DR KEGG; ecd:ECDH10B_4387; -.
DR HOGENOM; CLU_074775_0_0_6; -.
DR OMA; HWDMWKG; -.
DR BioCyc; ECOL316385:ECDH10B_RS22380-MON; -.
DR UniPathway; UPA00263; UER00377.
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_1000140095"
SQ SEQUENCE 354 AA; 40061 MW; 00DECD310615BF66 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
MKKDRLKYGF KPFIWQVGGK FTWPLDKDNF EYHYPRGFDD CFTIEPDLPF KSFL