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P13035

- GLPD_ECOLI

UniProt

P13035 - GLPD_ECOLI

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
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (01 May 1992)
      Previous versions | rss
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    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

    FAD.

    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

    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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEAQDLACA TSSASSKLIH    50
    GGLRYLEHYE FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM 100
    IRIGLFMYDH LGKRTSLPGS TGLRFGANSV LKPEIKRGFE YSDCWVDDAR 150
    LVLANAQMVV RKGGEVLTRT RATSARRENG LWIVEAEDID TGKKYSWQAR 200
    GLVNATGPWV KQFFDDGMHL PSPYGIRLIK GSHIVVPRVH TQKQAYILQN 250
    EDKRIVFVIP WMDEFSIIGT TDVEYKGDPK AVKIEESEIN YLLNVYNTHF 300
    KKQLSRDDIV WTYSGVRPLC DDESDSPQAI TRDYTLDIHD ENGKAPLLSV 350
    FGGKLTTYRK LAEHALEKLT PYYQGIGPAW TKESVLPGGA IEGDRDDYAA 400
    RLRRRYPFLT ESLARHYART YGSNSELLLG NAGTVSDLGE DFGHEFYEAE 450
    LKYLVDHEWV RRADDALWRR TKQGMWLNAD QQSRVSQWLV EYTQQRLSLA 500
    S 501
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    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: October 1, 2014
    This is version 136 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