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P18158

- GLPD_BACSU

UniProt

P18158 - GLPD_BACSU

Protein

Aerobic glycerol-3-phosphate dehydrogenase

Gene

glpD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    FAD.

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi24 – 5229FADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycerol-3-phosphate metabolic process Source: InterPro
    2. glycerol catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycerol metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciBSUB:BSU09300-MONOMER.
    UniPathwayiUPA00618; UER00674.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aerobic glycerol-3-phosphate dehydrogenase (EC:1.1.5.3)
    Gene namesi
    Name:glpD
    Ordered Locus Names:BSU09300
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU09300. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. glycerol-3-phosphate dehydrogenase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 555555Aerobic glycerol-3-phosphate dehydrogenasePRO_0000126097Add
    BLAST

    Proteomic databases

    PaxDbiP18158.

    Expressioni

    Inductioni

    Requires glycerol 3-phosphate and the GlpP product; repressed by glucose.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU09300.

    Structurei

    3D structure databases

    ProteinModelPortaliP18158.
    SMRiP18158. Positions 6-555.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0578.
    HOGENOMiHOG000004812.
    KOiK00111.
    OrthoDBiEOG651SR7.
    PhylomeDBiP18158.

    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.

    P18158-1 [UniParc]FASTAAdd to Basket

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    MMNHQFSSLE RDRMLTDMTK KTYDLFIIGG GITGAGTALD AASRGMKVAL    50
    SEMQDFAAGT SSRSTKLVHG GLRYLKQFEV KMVAEVGKER AIVYENGPHV 100
    TTPEWMLLPF HKGGTFGSFT TSIGLRVYDF LAGVKKSERR SMLSAKETLQ 150
    KEPLVKKDGL KGGGYYVEYR TDDARLTIEV MKEAVKFGAE PVNYSKVKEL 200
    LYEKGKAVGV LIEDVLTKKE YKVYAKKIVN ATGPWVDQLR EKDHSKNGKH 250
    LQHTKGIHLV FDQSVFPLKQ AVYFDTPDGR MVFAIPREGK TYVGTTDTVY 300
    KEALEHPRMT TEDRDYVIKS INYMFPELNI TANDIESSWA GLRPLIHEEG 350
    KDPSEISRKD EIWTSDSGLI TIAGGKLTGY RKMAEHIVDL VRDRLKEEGE 400
    KDFGPCKTKN MPISGGHVGG SKNLMSFVTA KTKEGIAAGL SEKDAKQLAI 450
    RYGSNVDRVF DRVEALKDEA AKRNIPVHIL AEAEYSIEEE MTATPADFFV 500
    RRTGRLFFDI NWVRTYKDAV IDFMSERFQW DEQAKNKHTE NLNKLLHDAV 550
    VPLEQ 555
    Length:555
    Mass (Da):62,568
    Last modified:June 16, 2009 - v2
    Checksum:iA4181ACBC7E7F87A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti385 – 3862EH → DD in AAA22487. (PubMed:2127799)Curated
    Sequence conflicti385 – 3862EH → DD in CAA74430. (PubMed:9579061)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34393 Genomic DNA. Translation: AAA22487.1.
    Y14079 Genomic DNA. Translation: CAA74430.1.
    AL009126 Genomic DNA. Translation: CAB12758.2.
    PIRiC45868.
    RefSeqiNP_388811.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12758; CAB12758; BSU09300.
    GeneIDi936250.
    KEGGibsu:BSU09300.
    PATRICi18973556. VBIBacSub10457_0972.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34393 Genomic DNA. Translation: AAA22487.1 .
    Y14079 Genomic DNA. Translation: CAA74430.1 .
    AL009126 Genomic DNA. Translation: CAB12758.2 .
    PIRi C45868.
    RefSeqi NP_388811.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P18158.
    SMRi P18158. Positions 6-555.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU09300.

    Proteomic databases

    PaxDbi P18158.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12758 ; CAB12758 ; BSU09300 .
    GeneIDi 936250.
    KEGGi bsu:BSU09300.
    PATRICi 18973556. VBIBacSub10457_0972.

    Organism-specific databases

    GenoListi BSU09300. [Micado ]

    Phylogenomic databases

    eggNOGi COG0578.
    HOGENOMi HOG000004812.
    KOi K00111.
    OrthoDBi EOG651SR7.
    PhylomeDBi P18158.

    Enzyme and pathway databases

    UniPathwayi UPA00618 ; UER00674 .
    BioCyci BSUB:BSU09300-MONOMER.

    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. "Glycerol catabolism in Bacillus subtilis: nucleotide sequence of the genes encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase (glpD)."
      Holmberg C., Beijer L., Rutberg B., Rutberg L.
      J. Gen. Microbiol. 136:2367-2375(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
      Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
      Microbiology 144:859-875(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 385-386.
    5. "Expression of the gene encoding glycerol-3-phosphate dehydrogenase (glpD) in Bacillus subtilis is controlled by antitermination."
      Holmberg C., Rutberg B.
      Mol. Microbiol. 5:2891-2900(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSCRIPTIONAL REGULATION.

    Entry informationi

    Entry nameiGLPD_BACSU
    AccessioniPrimary (citable) accession number: P18158
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 108 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

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3