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P13035

- GLPD_ECOLI

UniProt

P13035 - GLPD_ECOLI

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Protein

Aerobic glycerol-3-phosphate dehydrogenase

Gene

glpD

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi5 – 3329FADSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. electron carrier activity Source: EcoCyc
  2. sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity Source: UniProtKB-EC
  3. sn-glycerol-3-phosphate:ubiquinone oxidoreductase activity Source: EcoCyc

GO - Biological processi

  1. glycerol-3-phosphate catabolic process Source: EcoCyc
  2. glycerol catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycerol metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciEcoCyc:AERGLYC3PDEHYDROG-MONOMER.
ECOL316407:JW3389-MONOMER.
MetaCyc:AERGLYC3PDEHYDROG-MONOMER.
RETL1328306-WGS:GSTH-6855-MONOMER.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10394. glpD.

Subcellular locationi

GO - Cellular componenti

  1. glycerol-3-phosphate dehydrogenase complex Source: EcoCyc
  2. integral component of plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Aerobic glycerol-3-phosphate dehydrogenasePRO_0000126098Add
BLAST

Proteomic databases

PaxDbiP13035.
PRIDEiP13035.

2D gel databases

SWISS-2DPAGEP13035.

Expressioni

Gene expression databases

GenevestigatoriP13035.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
acrRP0ACS91EBI-548509,EBI-1117360
citDP693301EBI-548509,EBI-1119230
phoUP0A9K71EBI-548509,EBI-1133614
yaiIP0A8D31EBI-548509,EBI-1116378

Protein-protein interaction databases

DIPiDIP-9793N.
IntActiP13035. 90 interactions.
MINTiMINT-1248675.
STRINGi511145.b3426.

Structurei

Secondary structure

1
501
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi13 – 2412Combined sources
Beta strandi29 – 324Combined sources
Beta strandi34 – 363Combined sources
Helixi41 – 433Combined sources
Helixi53 – 586Combined sources
Helixi61 – 7717Combined sources
Turni79 – 813Combined sources
Beta strandi82 – 909Combined sources
Turni93 – 953Combined sources
Helixi98 – 10912Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi137 – 14610Combined sources
Helixi148 – 16114Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi169 – 17810Combined sources
Beta strandi181 – 1888Combined sources
Turni189 – 1913Combined sources
Beta strandi194 – 2007Combined sources
Beta strandi202 – 2043Combined sources
Helixi207 – 2093Combined sources
Helixi210 – 2167Combined sources
Beta strandi229 – 2379Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi255 – 2617Combined sources
Turni262 – 2643Combined sources
Beta strandi265 – 2695Combined sources
Helixi279 – 2813Combined sources
Helixi286 – 29914Combined sources
Beta strandi300 – 3023Combined sources
Helixi306 – 3083Combined sources
Beta strandi311 – 3177Combined sources
Helixi327 – 3293Combined sources
Beta strandi335 – 3417Combined sources
Beta strandi344 – 3518Combined sources
Helixi355 – 3573Combined sources
Helixi358 – 36912Combined sources
Helixi370 – 3723Combined sources
Helixi381 – 3833Combined sources
Beta strandi391 – 3933Combined sources
Turni394 – 3974Combined sources
Helixi398 – 4058Combined sources
Helixi411 – 42010Combined sources
Helixi422 – 4243Combined sources
Helixi425 – 4295Combined sources
Helixi435 – 4384Combined sources
Helixi448 – 45710Combined sources
Helixi463 – 4686Combined sources
Helixi473 – 4753Combined sources
Helixi479 – 49416Combined sources
Beta strandi495 – 4984Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-501.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13035.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0578.
HOGENOMiHOG000004811.
InParanoidiP13035.
KOiK00111.
OMAiRYPFISE.
OrthoDBiEOG651SR7.
PhylomeDBiP13035.

Family and domain databases

InterProiIPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PRINTSiPR01001. FADG3PDH.
PROSITEiPS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view]

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 AAA23888.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231A → G in BAA00327. 1 PublicationCurated
Sequence conflicti328 – 35326QAITR…SVFGG → HVLPVITPLIFMMKMAKHRC CRYSAA in BAA00327. 1 PublicationCuratedAdd
BLAST
Sequence conflicti464 – 50138DDALW…LSLAS → ARRPVASHKTRHVAKCGSTI SCESVAGGVYAAEVIAGVVN in BAA00327. 1 PublicationCuratedAdd
BLAST

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.
YP_492007.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76451; AAC76451; b3426.
BAE77866; BAE77866; BAE77866.
GeneIDi12932271.
947934.
KEGGiecj:Y75_p3751.
eco:b3426.
PATRICi32122288. VBIEscCol129921_3521.

Cross-referencesi

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.
PIRi A39186. DEECGD.
RefSeqi NP_417884.1. NC_000913.3.
YP_492007.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QCU X-ray 1.75 A/B 1-501 [» ]
2R45 X-ray 2.30 A/B 1-501 [» ]
2R46 X-ray 2.10 A/B 1-501 [» ]
2R4E X-ray 2.10 A/B 1-501 [» ]
2R4J X-ray 1.96 A/B 1-501 [» ]
ProteinModelPortali P13035.
SMRi P13035. Positions 1-501.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9793N.
IntActi P13035. 90 interactions.
MINTi MINT-1248675.
STRINGi 511145.b3426.

2D gel databases

SWISS-2DPAGE P13035.

Proteomic databases

PaxDbi P13035.
PRIDEi P13035.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76451 ; AAC76451 ; b3426 .
BAE77866 ; BAE77866 ; BAE77866 .
GeneIDi 12932271.
947934.
KEGGi ecj:Y75_p3751.
eco:b3426.
PATRICi 32122288. VBIEscCol129921_3521.

Organism-specific databases

EchoBASEi EB0389.
EcoGenei EG10394. glpD.

Phylogenomic databases

eggNOGi COG0578.
HOGENOMi HOG000004811.
InParanoidi P13035.
KOi K00111.
OMAi RYPFISE.
OrthoDBi EOG651SR7.
PhylomeDBi P13035.

Enzyme and pathway databases

UniPathwayi UPA00618 ; UER00674 .
BioCyci EcoCyc:AERGLYC3PDEHYDROG-MONOMER.
ECOL316407:JW3389-MONOMER.
MetaCyc:AERGLYC3PDEHYDROG-MONOMER.
RETL1328306-WGS:GSTH-6855-MONOMER.

Miscellaneous databases

EvolutionaryTracei P13035.
PROi P13035.

Gene expression databases

Genevestigatori P13035.

Family and domain databases

InterProi IPR006076. FAD-dep_OxRdtase.
IPR000447. G3P_DH_FAD-dep.
[Graphical view ]
Pfami PF01266. DAO. 1 hit.
[Graphical view ]
PRINTSi PR01001. FADG3PDH.
PROSITEi PS00977. FAD_G3PDH_1. 1 hit.
PS00978. FAD_G3PDH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12."
    Austin D., Larson T.J.
    J. Bacteriol. 173:101-107(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Nucleotide sequence of the glycerol-3-phosphate dehydrogenase gene of Escherichia coli and regulation by the cAMP-CRP complex."
    Choi Y.-L., Kawase S., Kawamukai M., Utsumi R., Sakai H., Komano T.
    Agric. Biol. Chem. 53:1135-1143(1989)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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.
  5. "Structures of the promoter and operator of the glpD gene encoding aerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12."
    Ye S., Larson T.J.
    J. Bacteriol. 170:4209-4215(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
    Strain: K12.
  6. "Nucleotide sequence of the glpR gene encoding the repressor for the glycerol-3-phosphate regulon of Escherichia coli K12."
    Choi Y.-L., Kawase S., Nishida T., Sakai H., Komano T., Kawamukai M., Utsumi R., Kohara Y., Akiyama K.
    Nucleic Acids Res. 16:7732-7732(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiGLPD_ECOLI
AccessioniPrimary (citable) accession number: P13035
Secondary accession number(s): P78115, Q2M790, Q47234
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 1, 1992
Last modified: November 26, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3