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A4YD91

- GSA_METS5

UniProt

A4YD91 - GSA_METS5

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
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 (29 May 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

    BioCyciMSED399549:GH1O-229-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:Msed_0216
    OrganismiMetallosphaera sedula (strain ATCC 51363 / DSM 5348)
    Taxonomic identifieri399549 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera
    ProteomesiUP000000242: 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 – 417417Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382396Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei259 – 2591N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi399549.Msed_0216.

    Structurei

    3D structure databases

    ProteinModelPortaliA4YD91.
    SMRiA4YD91. Positions 1-417.
    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.

    A4YD91-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSDLWNKAQ AVFAGGVNSP VRAAVKPFPF YTRSAKGAYL VTEDSRRLID    50
    FVLGYGPLIL GHAHPKVIEA VKDQLERGWL YGTPSRAEVE LASMITKHVP 100
    SAQKVRFVNS GTEATMTALR LSRGFTGRSK ILKFDGNYHG AHDYVLIDAG 150
    SAASEFGVPF SQGIPTEVSS TVLVCPYNDL TCVETVLKRE EIAGVIVEPV 200
    MGNMGVIPPE KDFLPGLRKL TREYGSVLIF DEVITGFRLG LGGAQSYFGV 250
    TPDLTTLGKI IGGGFPIGAV CGRKEIMDQL TPSGRVFNAG TFNANPISMT 300
    AGIATIQELE KKEVYTVSER AARVLAEEID RAIKMDHVVN RVYNFFQFFL 350
    GVKDVRNAND ARKAKRDLYV KVHESLLKEG VFIPPSQFEA LFTSGAHDDD 400
    VVNESARVFK KVLEDLT 417
    Length:417
    Mass (Da):45,616
    Last modified:May 29, 2007 - v1
    Checksum:i8963A2BC2653D404
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000682 Genomic DNA. Translation: ABP94393.1.
    RefSeqiWP_011921361.1. NC_009440.1.
    YP_001190317.1. NC_009440.1.

    Genome annotation databases

    EnsemblBacteriaiABP94393; ABP94393; Msed_0216.
    GeneIDi5104082.
    KEGGimse:Msed_0216.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000682 Genomic DNA. Translation: ABP94393.1 .
    RefSeqi WP_011921361.1. NC_009440.1.
    YP_001190317.1. NC_009440.1.

    3D structure databases

    ProteinModelPortali A4YD91.
    SMRi A4YD91. Positions 1-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 399549.Msed_0216.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABP94393 ; ABP94393 ; Msed_0216 .
    GeneIDi 5104082.
    KEGGi mse:Msed_0216.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    BioCyci MSED399549:GH1O-229-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 sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
      Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
      Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51363 / DSM 5348.

    Entry informationi

    Entry nameiGSA_METS5
    AccessioniPrimary (citable) accession number: A4YD91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 1, 2009
    Last sequence update: May 29, 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