ULAG_ECOLI
ID ULAG_ECOLI Reviewed; 354 AA.
AC P39300; Q2M6B3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable L-ascorbate-6-phosphate lactonase UlaG;
DE EC=3.1.1.-;
DE AltName: Full=L-ascorbate utilization protein G;
GN Name=ulaG; Synonyms=yjfR; OrderedLocusNames=b4192, JW5868;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=12374842; DOI=10.1128/jb.184.21.6065-6068.2002;
RA Campos E., Aguilar J., Baldoma L., Badia J.;
RT "The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is
RT involved in L-ascorbate metabolism in Escherichia coli.";
RL J. Bacteriol. 184:6065-6068(2002).
RN [5]
RP PROBABLE FUNCTION, AND ROLE IN L-ASCORBATE UTILIZATION.
RC STRAIN=K12 / BW25113;
RX PubMed=12644495; DOI=10.1128/jb.185.7.2243-2250.2003;
RA Zhang Z., Aboulwafa M., Smith M.H., Saier M.H. Jr.;
RT "The ascorbate transporter of Escherichia coli.";
RL J. Bacteriol. 185:2243-2250(2003).
RN [6]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=14996803; DOI=10.1128/jb.186.6.1720-1728.2004;
RA Campos E., Baldoma L., Aguilar J., Badia J.;
RT "Regulation of expression of the divergent ulaG and ulaABCDEF operons
RT involved in L-ascorbate dissimilation in Escherichia coli.";
RL J. Bacteriol. 186:1720-1728(2004).
RN [7]
RP FUNCTION.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(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. Also shows phosphodiesterase activity,
CC hydrolyzing phosphodiester bond in the artificial chromogenic substrate
CC bis-p-nitrophenyl phosphate (bis-pNPP). {ECO:0000269|PubMed:12644495,
CC ECO:0000269|PubMed:15808744}.
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;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC phosphate from L-ascorbate: step 1/4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by L-ascorbate. Repressed by UlaR.
CC {ECO:0000269|PubMed:12374842, ECO:0000269|PubMed:14996803}.
CC -!- SIMILARITY: Belongs to the UlaG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97088.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97088.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77149.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78193.1; -; Genomic_DNA.
DR RefSeq; NP_418613.2; NC_000913.3.
DR RefSeq; WP_001295191.1; NZ_SSUV01000014.1.
DR PDB; 2WYL; X-ray; 2.59 A; A/B/C/D/E/F=1-354.
DR PDB; 2WYM; X-ray; 2.60 A; A/B/C/D/E/F=1-354.
DR PDBsum; 2WYL; -.
DR PDBsum; 2WYM; -.
DR AlphaFoldDB; P39300; -.
DR SMR; P39300; -.
DR BioGRID; 4262712; 6.
DR DIP; DIP-12596N; -.
DR STRING; 511145.b4192; -.
DR DrugBank; DB04464; N-Formylmethionine.
DR PaxDb; P39300; -.
DR PRIDE; P39300; -.
DR EnsemblBacteria; AAC77149; AAC77149; b4192.
DR EnsemblBacteria; BAE78193; BAE78193; BAE78193.
DR GeneID; 66671895; -.
DR GeneID; 948705; -.
DR KEGG; ecj:JW5868; -.
DR KEGG; eco:b4192; -.
DR PATRIC; fig|1411691.4.peg.2509; -.
DR EchoBASE; EB2385; -.
DR eggNOG; COG2220; Bacteria.
DR HOGENOM; CLU_074775_0_0_6; -.
DR InParanoid; P39300; -.
DR OMA; HWDMWKG; -.
DR PhylomeDB; P39300; -.
DR BioCyc; EcoCyc:G7855-MON; -.
DR BioCyc; MetaCyc:G7855-MON; -.
DR BRENDA; 3.1.4.1; 2026.
DR UniPathway; UPA00263; UER00377.
DR EvolutionaryTrace; P39300; -.
DR PRO; PR:P39300; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035460; F:L-ascorbate 6-phosphate lactonase activity; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..354
FT /note="Probable L-ascorbate-6-phosphate lactonase UlaG"
FT /id="PRO_0000169757"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:2WYL"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:2WYL"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:2WYL"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2WYL"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:2WYL"
FT TURN 303..307
FT /evidence="ECO:0007829|PDB:2WYL"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:2WYL"
FT TURN 324..328
FT /evidence="ECO:0007829|PDB:2WYL"
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
