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Protein

Probable L-ascorbate-6-phosphate lactonase UlaG

Gene

ulaG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3-keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under anaerobic conditions. Also shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP).2 Publications

Catalytic activityi

L-ascorbate 6-phosphate + H2O = 3-dehydro-L-gulonate 6-phosphate.

Cofactori

Pathwayi: L-ascorbate degradation

This protein is involved in step 1 of the subpathway that synthesizes D-xylulose 5-phosphate from L-ascorbate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Probable L-ascorbate-6-phosphate lactonase UlaG (ulaG)
  2. 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD)
  3. L-ribulose-5-phosphate 3-epimerase UlaE (ulaE)
  4. L-ribulose-5-phosphate 4-epimerase UlaF (ulaF)
This subpathway is part of the pathway L-ascorbate degradation, which is itself part of Cofactor degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-xylulose 5-phosphate from L-ascorbate, the pathway L-ascorbate degradation and in Cofactor degradation.

GO - Molecular functioni

  • L-ascorbate 6-phosphate lactonase activity Source: EcoCyc
  • manganese ion binding Source: EcoCyc

GO - Biological processi

  • L-ascorbic acid catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:G7855-MONOMER.
ECOL316407:JW5868-MONOMER.
MetaCyc:G7855-MONOMER.
BRENDAi3.1.4.1. 2026.
UniPathwayiUPA00263; UER00377.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable L-ascorbate-6-phosphate lactonase UlaG (EC:3.1.1.-)
Alternative name(s):
L-ascorbate utilization protein G
Gene namesi
Name:ulaG
Synonyms:yjfR
Ordered Locus Names:b4192, JW5868
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12492. ulaG.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Probable L-ascorbate-6-phosphate lactonase UlaGPRO_0000169757Add
BLAST

Proteomic databases

PaxDbiP39300.
PRIDEiP39300.

Expressioni

Inductioni

Induced by L-ascorbate. Repressed by UlaR.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4262712. 5 interactions.
DIPiDIP-12596N.
STRINGi511145.b4192.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Helixi9 – 146Combined sources
Turni19 – 224Combined sources
Helixi23 – 308Combined sources
Beta strandi38 – 447Combined sources
Beta strandi47 – 515Combined sources
Beta strandi57 – 615Combined sources
Helixi104 – 1063Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi116 – 1183Combined sources
Helixi120 – 1223Combined sources
Helixi125 – 13410Combined sources
Beta strandi141 – 1433Combined sources
Helixi145 – 15410Combined sources
Helixi158 – 1603Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi169 – 1724Combined sources
Beta strandi175 – 1817Combined sources
Turni206 – 2083Combined sources
Beta strandi209 – 2168Combined sources
Beta strandi219 – 2235Combined sources
Helixi233 – 2397Combined sources
Beta strandi244 – 2496Combined sources
Helixi262 – 27211Combined sources
Beta strandi275 – 2817Combined sources
Turni282 – 2843Combined sources
Helixi286 – 2883Combined sources
Helixi293 – 30210Combined sources
Turni303 – 3075Combined sources
Beta strandi320 – 3234Combined sources
Turni324 – 3285Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WYLX-ray2.59A/B/C/D/E/F1-354[»]
2WYMX-ray2.60A/B/C/D/E/F1-354[»]
ProteinModelPortaliP39300.
SMRiP39300. Positions 1-338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39300.

Family & Domainsi

Sequence similaritiesi

Belongs to the UlaG family.Curated

Phylogenomic databases

eggNOGiENOG4105CP1. Bacteria.
COG2220. LUCA.
HOGENOMiHOG000127385.
InParanoidiP39300.
KOiK03476.
OMAiHGGDTKP.
OrthoDBiEOG696C0T.
PhylomeDBiP39300.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01266. UlaG.
InterProiIPR023951. L-ascorbate_6P_UlaG.
IPR001279. Metallo-B-lactamas.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.

Sequencei

Sequence statusi: Complete.

P39300-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKVKSITRE SWILSTFPEW GSWLNEEIEQ EQVAPGTFAM WWLGCTGIWL
60 70 80 90 100
KSEGGTNVCV DFWCGTGKQS HGNPLMKQGH QMQRMAGVKK LQPNLRTTPF
110 120 130 140 150
VLDPFAIRQI DAVLATHDHN DHIDVNVAAA VMQNCADDVP FIGPKTCVDL
160 170 180 190 200
WIGWGVPKER CIVVKPGDVV KVKDIEIHAL DAFDRTALIT LPADQKAAGV
210 220 230 240 250
LPDGMDDRAV NYLFKTPGGS LYHSGDSHYS NYYAKHGNEH QIDVALGSYG
260 270 280 290 300
ENPRGITDKM TSADMLRMGE ALNAKVVIPF HHDIWSNFQA DPQEIRVLWE
310 320 330 340 350
MKKDRLKYGF KPFIWQVGGK FTWPLDKDNF EYHYPRGFDD CFTIEPDLPF

KSFL
Length:354
Mass (Da):40,061
Last modified:July 15, 1998 - v2
Checksum:i00DECD310615BF66
GO

Sequence cautioni

The sequence AAA97088.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97088.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77149.2.
AP009048 Genomic DNA. Translation: BAE78193.1.
RefSeqiNP_418613.2. NC_000913.3.
WP_001295191.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77149; AAC77149; b4192.
BAE78193; BAE78193; BAE78193.
GeneIDi948705.
KEGGiecj:JW5868.
eco:b4192.
PATRICi32123959. VBIEscCol129921_4324.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97088.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77149.2.
AP009048 Genomic DNA. Translation: BAE78193.1.
RefSeqiNP_418613.2. NC_000913.3.
WP_001295191.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WYLX-ray2.59A/B/C/D/E/F1-354[»]
2WYMX-ray2.60A/B/C/D/E/F1-354[»]
ProteinModelPortaliP39300.
SMRiP39300. Positions 1-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262712. 5 interactions.
DIPiDIP-12596N.
STRINGi511145.b4192.

Proteomic databases

PaxDbiP39300.
PRIDEiP39300.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77149; AAC77149; b4192.
BAE78193; BAE78193; BAE78193.
GeneIDi948705.
KEGGiecj:JW5868.
eco:b4192.
PATRICi32123959. VBIEscCol129921_4324.

Organism-specific databases

EchoBASEiEB2385.
EcoGeneiEG12492. ulaG.

Phylogenomic databases

eggNOGiENOG4105CP1. Bacteria.
COG2220. LUCA.
HOGENOMiHOG000127385.
InParanoidiP39300.
KOiK03476.
OMAiHGGDTKP.
OrthoDBiEOG696C0T.
PhylomeDBiP39300.

Enzyme and pathway databases

UniPathwayiUPA00263; UER00377.
BioCyciEcoCyc:G7855-MONOMER.
ECOL316407:JW5868-MONOMER.
MetaCyc:G7855-MONOMER.
BRENDAi3.1.4.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP39300.
PROiP39300.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01266. UlaG.
InterProiIPR023951. L-ascorbate_6P_UlaG.
IPR001279. Metallo-B-lactamas.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is involved in L-ascorbate metabolism in Escherichia coli."
    Campos E., Aguilar J., Baldoma L., Badia J.
    J. Bacteriol. 184:6065-6068(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.
  5. Cited for: PROBABLE FUNCTION, ROLE IN L-ASCORBATE UTILIZATION.
    Strain: K12 / BW25113.
  6. "Regulation of expression of the divergent ulaG and ulaABCDEF operons involved in L-ascorbate dissimilation in Escherichia coli."
    Campos E., Baldoma L., Aguilar J., Badia J.
    J. Bacteriol. 186:1720-1728(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.
  7. "Enzyme genomics: application of general enzymatic screens to discover new enzymes."
    Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F.
    FEMS Microbiol. Rev. 29:263-279(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiULAG_ECOLI
AccessioniPrimary (citable) accession number: P39300
Secondary accession number(s): Q2M6B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 15, 1998
Last modified: May 11, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.