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Q980U5

- GSA_SULSO

UniProt

Q980U5 - GSA_SULSO

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 2 (19 Sep 2006)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.1 PublicationUniRule annotation

    Cofactori

    Pyridoxal phosphate.1 PublicationUniRule annotation

    Enzyme regulationi

    Inhibited by gabaculine.1 Publication

    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

    BioCyciSSOL273057:GCH2-171-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:SSO0182
    OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
    Taxonomic identifieri273057 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000001974: 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 – 418418Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei260 – 2601N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    STRINGi273057.SSO0182.

    Structurei

    3D structure databases

    ProteinModelPortaliQ980U5.
    SMRiQ980U5. Positions 2-417.
    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.
    OMAiHYPSIDM.

    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.

    Q980U5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSEELWAQA KQLFAGGVNS PVRAAVKPFP FYVERGKGAY IYTVDGKKFI    50
    DYVLGYGPLI LGHSPESVKR RIVEQLERGW LFGTPSELEI ELARKIRSHI 100
    PSAQKIRFVN SGTEATMAAI RLARGYTKRS KILKFSGNYH GAHDYALVEA 150
    GSAATEYNVA TSDGVPMEIM KTVEICEFND LDCVDKKLRN EDIATVILEP 200
    VMGNAGVILP EKDFLFGLRE LTKTYNSLLI FDEVITGFRI SIGGAQSYYQ 250
    IYPDITTLGK IIGGGFPIGA VAGKAEIIDN FTPAGKVFNA GTFNANPISM 300
    IAGIATIEEL EKEYPYIIAN QAAKTLVEEL ERLLKTKHTI NHVGSMFQIF 350
    FGIDEVRNYS DAKRADKEYY IKFHERLLKE GVFIPPSQYE TIFTSAAHKD 400
    DVIADTIDKL MKVIGELN 418
    Length:418
    Mass (Da):46,477
    Last modified:September 19, 2006 - v2
    Checksum:iC290C1884A38E710
    GO

    Sequence cautioni

    The sequence AAK40528.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251A → F AA sequence (PubMed:8973563)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006641 Genomic DNA. Translation: AAK40528.1. Different initiation.
    PIRiA90159.
    RefSeqiNP_341738.1. NC_002754.1.

    Genome annotation databases

    EnsemblBacteriaiAAK40528; AAK40528; SSO0182.
    GeneIDi1455338.
    KEGGisso:SSO0182.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006641 Genomic DNA. Translation: AAK40528.1 . Different initiation.
    PIRi A90159.
    RefSeqi NP_341738.1. NC_002754.1.

    3D structure databases

    ProteinModelPortali Q980U5.
    SMRi Q980U5. Positions 2-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273057.SSO0182.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK40528 ; AAK40528 ; SSO0182 .
    GeneIDi 1455338.
    KEGGi sso:SSO0182.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    BioCyci SSOL273057:GCH2-171-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    2. "Glutamate-1-semialdehyde aminotransferase from Sulfolobus solfataricus."
      Palmieri G., Di Palo M., Scaloni A., Orru S., Marino G., Sannia G.
      Biochem. J. 320:541-545(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-25, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT.
      Strain: DSM 5833 / MT-4.

    Entry informationi

    Entry nameiGSA_SULSO
    AccessioniPrimary (citable) accession number: Q980U5
    Secondary accession number(s): Q9UWG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: September 19, 2006
    Last modified: October 1, 2014
    This is version 78 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, Direct protein sequencing, 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