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Q06774

- GSA_PROFF

UniProt

Q06774 - GSA_PROFF

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Propionibacterium freudenreichii subsp. freudenreichii
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    GO - Molecular functioni

    1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-HAMAP
    2. pyridoxal phosphate binding Source: InterPro
    3. transaminase activity Source: InterPro

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    UniPathwayiUPA00251; UER00317.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate-1-semialdehyde 2,1-aminomutase (EC:5.4.3.8)
    Short name:
    GSA
    Alternative name(s):
    Glutamate-1-semialdehyde aminotransferase
    Short name:
    GSA-AT
    Gene namesi
    Name:hemL
    OrganismiPropionibacterium freudenreichii subsp. freudenreichii
    Taxonomic identifieri66712 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120432Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei270 – 2701N6-(pyridoxal phosphate)lysineBy similarity

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ06774.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    HAMAPiMF_00375. HemL_aminotrans_3.
    InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11986. PTHR11986. 1 hit.
    PfamiPF00202. Aminotran_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q06774-1 [UniParc]FASTAAdd to Basket

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    MSVSDELFAE ALKVMPGGVS SPVRAYRSVG GTPRFVKRAL GSHIVDVDDK    50
    RYVDLVCSWG PMIAGHAHPE VVAAVLQAVA DSTSFGAPSE VELRLAQAVV 100
    ARMGGAIDKV RFTCSGTEAV MTAARLARGI TKRPLLVKFV GCYHGHSDSF 150
    LVSAGSGVAS LGLPDSPGVP KEVAGDTVAL PYGRIDMVEE LFAERGDQVA 200
    AIVTEGVPAN MGVIVPPEGF NRRLHDIAHA HGALLIQDEV LTGFRLSPTG 250
    AWGLQGAKEG WTPDLFTFGK VIGGGMPLAA VGGSAQLMDY LAPEGPVYQA 300
    GTLSGNPAAC AAGLATLALM DDAAYSRLDA TADRVSAMAD AALESAGVPH 350
    RINKVSNLFS VFLTDAPVTD FASASKQDTK AFSRFFHAAL DAGLWLAPSG 400
    FEAWFCSTAL DDDDLEVIDA GLHKAAQAAA QGLSSLEDVR R 441
    Length:441
    Mass (Da):45,932
    Last modified:June 1, 1994 - v1
    Checksum:i0F07395A67CAE4D2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12643 Genomic DNA. Translation: BAA02164.1.
    D85417 Genomic DNA. Translation: BAA21914.1.
    PIRiA48959.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12643 Genomic DNA. Translation: BAA02164.1 .
    D85417 Genomic DNA. Translation: BAA21914.1 .
    PIRi A48959.

    3D structure databases

    ProteinModelPortali Q06774.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    HAMAPi MF_00375. HemL_aminotrans_3.
    InterProi IPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11986. PTHR11986. 1 hit.
    Pfami PF00202. Aminotran_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the gene encoding glutamate 1-semialdehyde 2,1-aminomutase, which is involved in delta-aminolevulinic acid synthesis in Propionibacterium freudenreichii."
      Murakami K., Hashimoto Y., Murooka Y.
      Appl. Environ. Microbiol. 59:347-350(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 6207 / DSM 20271 / LMG 16412 / NBRC 12424 / NCIMB 5959 / NCTC 10470 / NRRL B-3523.

    Entry informationi

    Entry nameiGSA_PROFF
    AccessioniPrimary (citable) accession number: Q06774
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3