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A2BL27

- GSA_HYPBU

UniProt

A2BL27 - GSA_HYPBU

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Hyperthermus butylicus (strain DSM 5456 / JCM 9403)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (20 Feb 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.UniRule annotation

    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

    BioCyciHBUT415426:GC56-837-MONOMER.
    UniPathwayiUPA00251; UER00317.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation (EC:5.4.3.8UniRule annotation)
    Short name:
    GSAUniRule annotation
    Alternative name(s):
    Glutamate-1-semialdehyde aminotransferaseUniRule annotation
    Short name:
    GSA-ATUniRule annotation
    Gene namesi
    Name:hemLUniRule annotation
    Ordered Locus Names:Hbut_0837
    OrganismiHyperthermus butylicus (strain DSM 5456 / JCM 9403)
    Taxonomic identifieri415426 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus
    ProteomesiUP000002593: 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 – 426426Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000059991Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei265 – 2651N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi415426.Hbut_0837.

    Structurei

    3D structure databases

    ProteinModelPortaliA2BL27.
    SMRiA2BL27. Positions 3-423.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0001.
    HOGENOMiHOG000020210.
    KOiK01845.
    OMAiHGHANAF.

    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.
    TIGRFAMsiTIGR00713. hemL. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A2BL27-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGEVSRSLY EKALTLFPGG VNSPVRAAVK PYPFYVERAE GPYIYTVDGE    50
    KLIDYVLAYG PLILGHKHPR VEEAVRRQLE KGWLYGAPYE LEIRLAEKIL 100
    KYYHPGGMVR FVNTGTEATM TAIRLARGVT GRKYIVKFNG CYHGAHDAVL 150
    VGAGSAAAEY GVPTSKGIPE EVAKLTLVAK YNDIESVEKI MSKHGDEVAA 200
    IIVEPVAGNA GVIPPKKGFL QELRRIASEH GALLIMDEVI TGFRLALGGA 250
    QEYYRVKADI TTLGKIVGGG FPIGVVVADR KIMEHLTPSG KVFNAGTFNA 300
    HPVTMAAGLA TIEVLEEGTP YRVASEAGRA LAEELESLVL SYGIDAAVNH 350
    VESMLQIFFV KGEVWSPEDA AKSDKKLYLK LHEELLKLGV FIAPSQMEAI 400
    FTSAAHTSDV VSETIEKLRK AFKRLR 426
    Length:426
    Mass (Da):46,427
    Last modified:February 20, 2007 - v1
    Checksum:i7FD5942F85CE8581
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000493 Genomic DNA. Translation: ABM80688.1.
    RefSeqiWP_011822006.1. NC_008818.1.
    YP_001013033.1. NC_008818.1.

    Genome annotation databases

    EnsemblBacteriaiABM80688; ABM80688; Hbut_0837.
    GeneIDi4782262.
    KEGGihbu:Hbut_0837.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000493 Genomic DNA. Translation: ABM80688.1 .
    RefSeqi WP_011822006.1. NC_008818.1.
    YP_001013033.1. NC_008818.1.

    3D structure databases

    ProteinModelPortali A2BL27.
    SMRi A2BL27. Positions 3-423.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 415426.Hbut_0837.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM80688 ; ABM80688 ; Hbut_0837 .
    GeneIDi 4782262.
    KEGGi hbu:Hbut_0837.

    Phylogenomic databases

    eggNOGi COG0001.
    HOGENOMi HOG000020210.
    KOi K01845.
    OMAi HGHANAF.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    BioCyci HBUT415426:GC56-837-MONOMER.

    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.
    TIGRFAMsi TIGR00713. hemL. 1 hit.
    PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
      Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
      Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 5456 / JCM 9403.

    Entry informationi

    Entry nameiGSA_HYPBU
    AccessioniPrimary (citable) accession number: A2BL27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 56 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