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Protein

Aerobic glycerol-3-phosphate dehydrogenase

Gene

glpD

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

Functioni

Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor.

Miscellaneous

There are two sn-glycerol-3-phosphate dehydrogenase isozymes in E.coli: one is aerobic, the other anaerobic.

Catalytic activityi

sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.

Cofactori

Pathwayi: glycerol degradation via glycerol kinase pathway

This protein is involved in step 1 of the subpathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (aerobic route).
Proteins known to be involved in this subpathway in this organism are:
  1. Aerobic glycerol-3-phosphate dehydrogenase (glpD)
This subpathway is part of the pathway glycerol degradation via glycerol kinase pathway, which is itself part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (aerobic route), the pathway glycerol degradation via glycerol kinase pathway and in Polyol metabolism.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi5 – 33FADSequence analysisAdd BLAST29

GO - Molecular functioni

  • electron carrier activity Source: EcoCyc
  • FAD binding Source: EcoCyc
  • sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity Source: UniProtKB-EC
  • sn-glycerol-3-phosphate:ubiquinone oxidoreductase activity Source: EcoCyc

GO - Biological processi

  • glycerol-3-phosphate catabolic process Source: EcoCyc
  • glycerol catabolic process Source: UniProtKB-UniPathway

Keywordsi

Molecular functionOxidoreductase
Biological processGlycerol metabolism
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyciEcoCyc:AERGLYC3PDEHYDROG-MONOMER.
MetaCyc:AERGLYC3PDEHYDROG-MONOMER.
BRENDAi1.1.1.94. 2026.
UniPathwayiUPA00618; UER00674.

Names & Taxonomyi

Protein namesi
Recommended name:
Aerobic glycerol-3-phosphate dehydrogenase (EC:1.1.5.3)
Gene namesi
Name:glpD
Synonyms:glyD
Ordered Locus Names:b3426, JW3389
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10394. glpD.

Subcellular locationi

GO - Cellular componenti

  • glycerol-3-phosphate dehydrogenase complex Source: EcoCyc
  • integral component of plasma membrane Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001260981 – 501Aerobic glycerol-3-phosphate dehydrogenaseAdd BLAST501

Proteomic databases

PaxDbiP13035.
PRIDEiP13035.

2D gel databases

SWISS-2DPAGEiP13035.

Interactioni

Protein-protein interaction databases

BioGridi4261265. 401 interactors.
DIPiDIP-9793N.
IntActiP13035. 90 interactors.
MINTiMINT-1248675.
STRINGi316385.ECDH10B_3600.

Structurei

Secondary structure

1501
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi13 – 24Combined sources12
Beta strandi29 – 32Combined sources4
Beta strandi34 – 36Combined sources3
Helixi41 – 43Combined sources3
Helixi53 – 58Combined sources6
Helixi61 – 77Combined sources17
Turni79 – 81Combined sources3
Beta strandi82 – 90Combined sources9
Turni93 – 95Combined sources3
Helixi98 – 109Combined sources12
Beta strandi110 – 112Combined sources3
Beta strandi115 – 117Combined sources3
Beta strandi121 – 124Combined sources4
Beta strandi129 – 131Combined sources3
Beta strandi137 – 146Combined sources10
Helixi148 – 161Combined sources14
Beta strandi165 – 167Combined sources3
Beta strandi169 – 178Combined sources10
Beta strandi181 – 188Combined sources8
Turni189 – 191Combined sources3
Beta strandi194 – 200Combined sources7
Beta strandi202 – 204Combined sources3
Helixi207 – 209Combined sources3
Helixi210 – 216Combined sources7
Beta strandi229 – 237Combined sources9
Beta strandi239 – 241Combined sources3
Beta strandi245 – 249Combined sources5
Beta strandi255 – 261Combined sources7
Turni262 – 264Combined sources3
Beta strandi265 – 269Combined sources5
Helixi279 – 281Combined sources3
Helixi286 – 299Combined sources14
Beta strandi300 – 302Combined sources3
Helixi306 – 308Combined sources3
Beta strandi311 – 317Combined sources7
Helixi327 – 329Combined sources3
Beta strandi335 – 341Combined sources7
Beta strandi344 – 351Combined sources8
Helixi355 – 357Combined sources3
Helixi358 – 369Combined sources12
Helixi370 – 372Combined sources3
Helixi381 – 383Combined sources3
Beta strandi391 – 393Combined sources3
Turni394 – 397Combined sources4
Helixi398 – 405Combined sources8
Helixi411 – 420Combined sources10
Helixi422 – 424Combined sources3
Helixi425 – 429Combined sources5
Helixi435 – 438Combined sources4
Helixi448 – 457Combined sources10
Helixi463 – 468Combined sources6
Helixi473 – 475Combined sources3
Helixi479 – 494Combined sources16
Beta strandi495 – 498Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QCUX-ray1.75A/B1-501[»]
2R45X-ray2.30A/B1-501[»]
2R46X-ray2.10A/B1-501[»]
2R4EX-ray2.10A/B1-501[»]
2R4JX-ray1.96A/B1-501[»]
ProteinModelPortaliP13035.
SMRiP13035.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13035.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C6V. Bacteria.
COG0578. LUCA.
HOGENOMiHOG000004811.
InParanoidiP13035.
KOiK00111.
PhylomeDBiP13035.

Family and domain databases

InterProiView protein in InterPro
IPR031656. DAO_C.
IPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR000447. G3P_DH_FAD-dep.
PANTHERiPTHR11985. PTHR11985. 1 hit.
PfamiView protein in Pfam
PF01266. DAO. 1 hit.
PF16901. DAO_C. 1 hit.
PRINTSiPR01001. FADG3PDH.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiView protein in PROSITE
PS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P13035-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEAQDLACA TSSASSKLIH
60 70 80 90 100
GGLRYLEHYE FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM
110 120 130 140 150
IRIGLFMYDH LGKRTSLPGS TGLRFGANSV LKPEIKRGFE YSDCWVDDAR
160 170 180 190 200
LVLANAQMVV RKGGEVLTRT RATSARRENG LWIVEAEDID TGKKYSWQAR
210 220 230 240 250
GLVNATGPWV KQFFDDGMHL PSPYGIRLIK GSHIVVPRVH TQKQAYILQN
260 270 280 290 300
EDKRIVFVIP WMDEFSIIGT TDVEYKGDPK AVKIEESEIN YLLNVYNTHF
310 320 330 340 350
KKQLSRDDIV WTYSGVRPLC DDESDSPQAI TRDYTLDIHD ENGKAPLLSV
360 370 380 390 400
FGGKLTTYRK LAEHALEKLT PYYQGIGPAW TKESVLPGGA IEGDRDDYAA
410 420 430 440 450
RLRRRYPFLT ESLARHYART YGSNSELLLG NAGTVSDLGE DFGHEFYEAE
460 470 480 490 500
LKYLVDHEWV RRADDALWRR TKQGMWLNAD QQSRVSQWLV EYTQQRLSLA

S
Length:501
Mass (Da):56,751
Last modified:May 1, 1992 - v3
Checksum:i1C4D341E9E4536AB
GO

Sequence cautioni

The sequence AAA23888 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23A → G in BAA00327 (Ref. 2) Curated1
Sequence conflicti328 – 353QAITR…SVFGG → HVLPVITPLIFMMKMAKHRC CRYSAA in BAA00327 (Ref. 2) CuratedAdd BLAST26
Sequence conflicti464 – 501DDALW…LSLAS → ARRPVASHKTRHVAKCGSTI SCESVAGGVYAAEVIAGVVN in BAA00327 (Ref. 2) CuratedAdd BLAST38

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55989 Genomic DNA. Translation: AAA24636.1.
M96795 Genomic DNA. Translation: AAC28164.1.
D00425 Genomic DNA. Translation: BAA00327.1.
U18997 Genomic DNA. Translation: AAA58224.1.
U00096 Genomic DNA. Translation: AAC76451.1.
AP009048 Genomic DNA. Translation: BAE77866.1.
M21277 Genomic DNA. Translation: AAA23885.1.
M54940 Genomic DNA. Translation: AAA23888.1. Different initiation.
PIRiA39186. DEECGD.
RefSeqiNP_417884.1. NC_000913.3.
WP_000448136.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76451; AAC76451; b3426.
BAE77866; BAE77866; BAE77866.
GeneIDi947934.
KEGGiecj:JW3389.
eco:b3426.
PATRICifig|511145.12.peg.3521.

Similar proteinsi

Entry informationi

Entry nameiGLPD_ECOLI
AccessioniPrimary (citable) accession number: P13035
Secondary accession number(s): P78115, Q2M790, Q47234
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 1, 1992
Last modified: August 30, 2017
This is version 159 of the entry and version 3 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

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