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Q1R9H5

- GLPB_ECOUT

UniProt

Q1R9H5 - GLPB_ECOUT

Protein

Anaerobic glycerol-3-phosphate dehydrogenase subunit B

Gene

glpB

Organism
Escherichia coli (strain UTI89 / UPEC)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 2 (31 Oct 2006)
      Previous versions | rss
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    Functioni

    Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.UniRule annotation

    Catalytic activityi

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

    Cofactori

    FMN.UniRule annotation

    Pathwayi

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycerol catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    BioCyciECOL364106:GHPQ-2504-MONOMER.
    UniPathwayiUPA00618; UER00673.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anaerobic glycerol-3-phosphate dehydrogenase subunit BUniRule annotation (EC:1.1.5.3UniRule annotation)
    Short name:
    Anaerobic G-3-P dehydrogenase subunit BUniRule annotation
    Short name:
    Anaerobic G3Pdhase BUniRule annotation
    Gene namesi
    Name:glpBUniRule annotation
    Ordered Locus Names:UTI89_C2522
    OrganismiEscherichia coli (strain UTI89 / UPEC)
    Taxonomic identifieri364106 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000001952: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 419419Anaerobic glycerol-3-phosphate dehydrogenase subunit BPRO_0000258900Add
    BLAST

    Interactioni

    Subunit structurei

    Composed of a catalytic GlpA/B dimer and of membrane bound GlpC.UniRule annotation

    Protein-protein interaction databases

    STRINGi364106.UTI89_C2522.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1R9H5.
    SMRiQ1R9H5. Positions 1-60, 255-312, 355-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the anaerobic G-3-P dehydrogenase subunit B family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3075.
    HOGENOMiHOG000278489.
    KOiK00112.
    OMAiFRSVNIS.
    OrthoDBiEOG6K6V62.

    Family and domain databases

    HAMAPiMF_00753. Glycerol3P_GlpB.
    InterProiIPR003953. FAD_bind_dom.
    IPR009158. G3P_DH_GlpB_su.
    [Graphical view]
    PfamiPF00890. FAD_binding_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000141. Anaerobic_G3P_dh. 1 hit.
    TIGRFAMsiTIGR03378. glycerol3P_GlpB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q1R9H5-1 [UniParc]FASTAAdd to Basket

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    MRFDTVIMGG GLAGLLCGLQ LQKHGLRCAI VTRGQSALHF SSGSLDLLSH    50
    LPDGQPVTDI HSGLESLRQQ APAHPYTLLG PQRVLDLACQ AQALIAESGA 100
    QLQGSVELAH QRITPLGTLR STWLSSPEVP VWPLPAKKIC VVGISGLMDF 150
    QAHLAAASLR ELDLAVETAE IELPELDVLR NNATEFRAVN IARFLDNEEN 200
    WPLIIDALIP VANTCEMILM PACFGLADDK LWRWLNEKLP CSLMLLPTLP 250
    PSVLGIRLQN QLQRQFVRQG GVWMPGDEVK KVTCKNGVVN EIWTRNHADI 300
    PLRPRFAVLA SGSFFSGGLV AERDGIREPI LGLDVLQTAT RGEWYKGDFF 350
    APQPWQQFGV TTDEALRPSQ AGQTIENLFA IGSVLGGFDP IAQGCGGGVC 400
    AVSALHAAQQ IAQRAGGQQ 419
    Length:419
    Mass (Da):45,342
    Last modified:October 31, 2006 - v2
    Checksum:i4FC59D8EC01E7A4F
    GO

    Sequence cautioni

    The sequence ABE07989.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000243 Genomic DNA. Translation: ABE07989.1. Different initiation.
    RefSeqiYP_541520.1. NC_007946.1.

    Genome annotation databases

    EnsemblBacteriaiABE07989; ABE07989; UTI89_C2522.
    GeneIDi3992364.
    KEGGieci:UTI89_C2522.
    PATRICi18454626. VBIEscCol42261_2550.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000243 Genomic DNA. Translation: ABE07989.1 . Different initiation.
    RefSeqi YP_541520.1. NC_007946.1.

    3D structure databases

    ProteinModelPortali Q1R9H5.
    SMRi Q1R9H5. Positions 1-60, 255-312, 355-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 364106.UTI89_C2522.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE07989 ; ABE07989 ; UTI89_C2522 .
    GeneIDi 3992364.
    KEGGi eci:UTI89_C2522.
    PATRICi 18454626. VBIEscCol42261_2550.

    Phylogenomic databases

    eggNOGi COG3075.
    HOGENOMi HOG000278489.
    KOi K00112.
    OMAi FRSVNIS.
    OrthoDBi EOG6K6V62.

    Enzyme and pathway databases

    UniPathwayi UPA00618 ; UER00673 .
    BioCyci ECOL364106:GHPQ-2504-MONOMER.

    Family and domain databases

    HAMAPi MF_00753. Glycerol3P_GlpB.
    InterProi IPR003953. FAD_bind_dom.
    IPR009158. G3P_DH_GlpB_su.
    [Graphical view ]
    Pfami PF00890. FAD_binding_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000141. Anaerobic_G3P_dh. 1 hit.
    TIGRFAMsi TIGR03378. glycerol3P_GlpB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
      Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
      Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: UTI89 / UPEC.

    Entry informationi

    Entry nameiGLPB_ECOUT
    AccessioniPrimary (citable) accession number: Q1R9H5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: October 31, 2006
    Last modified: October 1, 2014
    This is version 60 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3