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Protein

Putative 2-dehydro-3-deoxy-D-gluconate aldolase YagE

Gene

yagE

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

Functioni

Catalyzes the formation of 2-keto-3-deoxy-gluconate (KDG) from pyruvate and glyceraldehyde (PubMed:21294156). May also function as a 2-dehydro-3-deoxy-D-pentonate aldolase (PubMed:23233208). Overexpression leads to increased growth (over 2 hours) in the presence of the antibiotics norfloxacin, ampicillin and streptomycin (PubMed:21294156).1 Publication1 Publication

Miscellaneous

Part of prophage CP4-6.

Catalytic activityi

2-dehydro-3-deoxy-D-gluconate = pyruvate + D-glyceraldehyde.1 Publication
2-dehydro-3-deoxy-D-pentonate = pyruvate + glycolaldehyde.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei49Charge relay system1 Publication1
Active sitei112Charge relay system1 Publication1
Active sitei138Proton donor1 Publication1
Active sitei167Schiff-base intermediate with substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

  • aldonic acid catabolic process Source: EcoCyc

Keywordsi

Molecular functionLyase
LigandSchiff base

Enzyme and pathway databases

BioCyciEcoCyc:G6140-MONOMER
MetaCyc:G6140-MONOMER
BRENDAi4.1.2.20 2026

Names & Taxonomyi

Protein namesi
Recommended name:
Putative 2-dehydro-3-deoxy-D-gluconate aldolase YagECurated (EC:4.1.2.511 Publication)
Short name:
KDG aldolase YagECurated
Alternative name(s):
Putative 2-dehydro-3-deoxy-D-pentonate aldolase YagECurated (EC:4.1.2.281 Publication)
Gene namesi
Name:yagE
Ordered Locus Names:b0268, JW0261
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13344 yagE

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Disruption mutant has reduced ability to catabolize D-xylonic acid. YjhH-yagE double mutant cannot use D-xylonate as the sole source of carbon.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001032441 – 302Putative 2-dehydro-3-deoxy-D-gluconate aldolase YagEAdd BLAST302

Proteomic databases

PaxDbiP75682
PRIDEiP75682

Interactioni

Subunit structurei

A dimer of dimers.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261826, 7 interactors
DIPiDIP-11232N
IntActiP75682, 3 interactors
STRINGi316385.ECDH10B_0255

Structurei

Secondary structure

1302
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 24Combined sources3
Helixi26 – 38Combined sources13
Beta strandi44 – 48Combined sources5
Helixi49 – 51Combined sources3
Helixi53 – 55Combined sources3
Helixi58 – 72Combined sources15
Beta strandi78 – 81Combined sources4
Helixi87 – 99Combined sources13
Beta strandi103 – 108Combined sources6
Beta strandi111 – 113Combined sources3
Helixi117 – 129Combined sources13
Beta strandi135 – 139Combined sources5
Helixi141 – 144Combined sources4
Helixi150 – 159Combined sources10
Beta strandi163 – 168Combined sources6
Helixi173 – 186Combined sources14
Beta strandi191 – 196Combined sources6
Helixi197 – 199Combined sources3
Helixi200 – 205Combined sources6
Helixi214 – 216Combined sources3
Helixi220 – 232Combined sources13
Helixi235 – 247Combined sources13
Helixi248 – 254Combined sources7
Beta strandi255 – 257Combined sources3
Helixi259 – 268Combined sources10
Helixi286 – 298Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V8ZX-ray2.20A/B/C/D1-302[»]
2V9DX-ray2.15A/B/C/D1-302[»]
3N2XX-ray2.20A/B/C/D5-302[»]
3NEVX-ray2.19A/B/C/D5-302[»]
4OE7X-ray1.99A/B/C/D1-302[»]
4ONVX-ray2.57A/B/C/D1-302[»]
4PTNX-ray1.99A/B/C/D1-302[»]
4U4MX-ray3.09A/B/C/D5-302[»]
ProteinModelPortaliP75682
SMRiP75682
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP75682

Family & Domainsi

Sequence similaritiesi

Belongs to the DapA family.Curated

Phylogenomic databases

eggNOGiENOG4105CDP Bacteria
COG0329 LUCA
HOGENOMiHOG000173604
InParanoidiP75682
KOiK22397

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR002220 DapA-like
IPR020625 Schiff_base-form_aldolases_AS
IPR020624 Schiff_base-form_aldolases_CS
PANTHERiPTHR12128 PTHR12128, 1 hit
PfamiView protein in Pfam
PF00701 DHDPS, 1 hit
PIRSFiPIRSF001365 DHDPS, 1 hit
PRINTSiPR00146 DHPICSNTHASE
SMARTiView protein in SMART
SM01130 DHDPS, 1 hit
PROSITEiView protein in PROSITE
PS00665 DHDPS_1, 1 hit
PS00666 DHDPS_2, 1 hit

Sequencei

Sequence statusi: Complete.

P75682-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQSALFTGI IPPVSTIFTA DGQLDKPGTA ALIDDLIKAG VDGLFFLGSG
60 70 80 90 100
GEFSQLGAEE RKAIARFAID HVDRRVPVLI GTGGTNARET IELSQHAQQA
110 120 130 140 150
GADGIVVINP YYWKVSEANL IRYFEQVADS VTLPVMLYNF PALTGQDLTP
160 170 180 190 200
ALVKTLADSR SNIIGIKDTI DSVAHLRSMI HTVKGAHPHF TVLCGYDDHL
210 220 230 240 250
FNTLLLGGDG AISASGNFAP QVSVNLLKAW RDGDVAKAAG YHQTLLQIPQ
260 270 280 290 300
MYQLDTPFVN VIKEAIVLCG RPVSTHVLPP ASPLDEPRKA QLKTLLQQLK

LC
Length:302
Mass (Da):32,530
Last modified:November 16, 2011 - v2
Checksum:i3ED5545FA2D739BA
GO

Sequence cautioni

The sequence BAA77934 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA Translation: AAC73371.2
AP009048 Genomic DNA Translation: BAA77934.2 Different initiation.
PIRiD64752
RefSeqiNP_414802.2, NC_000913.3
WP_001136613.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73371; AAC73371; b0268
BAA77934; BAA77934; BAA77934
GeneIDi944925
KEGGiecj:JW0261
eco:b0268
PATRICifig|1411691.4.peg.2012

Similar proteinsi

Entry informationi

Entry nameiYAGE_ECOLI
AccessioniPrimary (citable) accession number: P75682
Secondary accession number(s): Q9R2D5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 16, 2011
Last modified: March 28, 2018
This is version 125 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health