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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001697571 – 354Probable L-ascorbate-6-phosphate lactonase UlaGAdd BLAST354

Proteomic databases

PaxDbiP39300.
PRIDEiP39300.

Expressioni

Inductioni

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

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1354
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Helixi9 – 14Combined sources6
Turni19 – 22Combined sources4
Helixi23 – 30Combined sources8
Beta strandi38 – 44Combined sources7
Beta strandi47 – 51Combined sources5
Beta strandi57 – 61Combined sources5
Helixi104 – 106Combined sources3
Beta strandi111 – 114Combined sources4
Beta strandi116 – 118Combined sources3
Helixi120 – 122Combined sources3
Helixi125 – 134Combined sources10
Beta strandi141 – 143Combined sources3
Helixi145 – 154Combined sources10
Helixi158 – 160Combined sources3
Beta strandi161 – 163Combined sources3
Beta strandi169 – 172Combined sources4
Beta strandi175 – 181Combined sources7
Turni206 – 208Combined sources3
Beta strandi209 – 216Combined sources8
Beta strandi219 – 223Combined sources5
Helixi233 – 239Combined sources7
Beta strandi244 – 249Combined sources6
Helixi262 – 272Combined sources11
Beta strandi275 – 281Combined sources7
Turni282 – 284Combined sources3
Helixi286 – 288Combined sources3
Helixi293 – 302Combined sources10
Turni303 – 307Combined sources5
Beta strandi320 – 323Combined sources4
Turni324 – 328Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WYLX-ray2.59A/B/C/D/E/F1-354[»]
2WYMX-ray2.60A/B/C/D/E/F1-354[»]
ProteinModelPortaliP39300.
SMRiP39300.
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.
PhylomeDBiP39300.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
HAMAPiMF_01266. UlaG. 1 hit.
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 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WYLX-ray2.59A/B/C/D/E/F1-354[»]
2WYMX-ray2.60A/B/C/D/E/F1-354[»]
ProteinModelPortaliP39300.
SMRiP39300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262712. 5 interactors.
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.
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. 1 hit.
InterProiIPR023951. L-ascorbate_6P_UlaG.
IPR001279. Metallo-B-lactamas.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 121 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.