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Q5KYA2

- PROA_GEOKA

UniProt

Q5KYA2 - PROA_GEOKA

Protein

Gamma-glutamyl phosphate reductase

Gene

proA

Organism
Geobacillus kaustophilus (strain HTA426)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Feb 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.UniRule annotation

    Catalytic activityi

    L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.UniRule annotation

    Pathwayi

    GO - Molecular functioni

    1. glutamate-5-semialdehyde dehydrogenase activity Source: UniProtKB-HAMAP
    2. NADP binding Source: InterPro

    GO - Biological processi

    1. L-proline biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Proline biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciGKAU235909:GJO7-2137-MONOMER.
    UniPathwayiUPA00098; UER00360.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-glutamyl phosphate reductaseUniRule annotation (EC:1.2.1.41UniRule annotation)
    Short name:
    GPRUniRule annotation
    Alternative name(s):
    Glutamate-5-semialdehyde dehydrogenaseUniRule annotation
    Glutamyl-gamma-semialdehyde dehydrogenaseUniRule annotation
    Short name:
    GSA dehydrogenaseUniRule annotation
    Gene namesi
    Name:proAUniRule annotation
    Ordered Locus Names:GK2049
    OrganismiGeobacillus kaustophilus (strain HTA426)
    Taxonomic identifieri235909 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
    ProteomesiUP000001172: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 414414Gamma-glutamyl phosphate reductasePRO_0000189728Add
    BLAST

    Proteomic databases

    PRIDEiQ5KYA2.

    Interactioni

    Protein-protein interaction databases

    STRINGi235909.GK2049.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5KYA2.
    SMRiQ5KYA2. Positions 3-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the gamma-glutamyl phosphate reductase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0014.
    HOGENOMiHOG000246356.
    KOiK00147.
    OMAiALTSYKW.
    OrthoDBiEOG6FFSCX.

    Family and domain databases

    Gene3Di3.40.309.10. 1 hit.
    3.40.605.10. 2 hits.
    HAMAPiMF_00412. ProA.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR000965. G-glutamylP_reductase.
    IPR020593. G-glutamylP_reductase_CS.
    IPR012134. Glu-5-SA_DH.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000151. GPR. 1 hit.
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR00407. proA. 1 hit.
    PROSITEiPS01223. PROA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5KYA2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSELLEKAER LKTASQTLAM LSAEEKNEAL EQIAQTLDRE RAFILQENEK    50
    DMAQGREQGL SPALLDRLQL TNERLDQIID GVRQVASLPD PVGEIIAEWT 100
    RPNGLRIQTV RVPLGVIGMV YEARPNVTVD AASLCLKTGN AVLLRGSTSA 150
    LHSNKALVAV MKEALRTTAI PETAIELLED TSRETAQRMF RLNNYLDVLI 200
    PRGGAGLIRS VVENATVPVL ETGVGNCHIF VDESAERQMA IEIVLNAKLQ 250
    RPSVCNAVET VLIHERWPYA ADLLETLHAR GVELRGDQRL ASAYPFISEA 300
    TEDDWYTEYL APILAVKLVA DVDEAIGHIR RYGTKHSEAI ITENEVNVRR 350
    FFQAVDAAVL YHNASTRFTD GEQFGYGAEI GISTQKLHAR GPMGLVAITT 400
    TKSLVYGTGQ IRTV 414
    Length:414
    Mass (Da):45,650
    Last modified:February 1, 2005 - v1
    Checksum:iD57558B51B02E565
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000043 Genomic DNA. Translation: BAD76334.1.
    RefSeqiYP_147902.1. NC_006510.1.

    Genome annotation databases

    EnsemblBacteriaiBAD76334; BAD76334; GK2049.
    GeneIDi3186428.
    KEGGigka:GK2049.
    PATRICi21965487. VBIGeoKau81518_2199.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000043 Genomic DNA. Translation: BAD76334.1 .
    RefSeqi YP_147902.1. NC_006510.1.

    3D structure databases

    ProteinModelPortali Q5KYA2.
    SMRi Q5KYA2. Positions 3-413.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 235909.GK2049.

    Proteomic databases

    PRIDEi Q5KYA2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD76334 ; BAD76334 ; GK2049 .
    GeneIDi 3186428.
    KEGGi gka:GK2049.
    PATRICi 21965487. VBIGeoKau81518_2199.

    Phylogenomic databases

    eggNOGi COG0014.
    HOGENOMi HOG000246356.
    KOi K00147.
    OMAi ALTSYKW.
    OrthoDBi EOG6FFSCX.

    Enzyme and pathway databases

    UniPathwayi UPA00098 ; UER00360 .
    BioCyci GKAU235909:GJO7-2137-MONOMER.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 2 hits.
    HAMAPi MF_00412. ProA.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR000965. G-glutamylP_reductase.
    IPR020593. G-glutamylP_reductase_CS.
    IPR012134. Glu-5-SA_DH.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000151. GPR. 1 hit.
    SUPFAMi SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR00407. proA. 1 hit.
    PROSITEi PS01223. PROA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
      Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
      Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HTA426.

    Entry informationi

    Entry nameiPROA_GEOKA
    AccessioniPrimary (citable) accession number: Q5KYA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3