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A9R1E6

- GSA_YERPG

UniProt

A9R1E6 - GSA_YERPG

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      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

    BioCyciYPES349746:GHPB-995-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:YpAngola_A0995
    OrganismiYersinia pestis bv. Antiqua (strain Angola)
    Taxonomic identifieri349746 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
    ProteomesiUP000001204: 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_1000121934Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi349746.YpAngola_A0995.

    Structurei

    3D structure databases

    ProteinModelPortaliA9R1E6.
    SMRiA9R1E6. Positions 2-421.
    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.
    OMAiRAIKPYP.
    OrthoDBiEOG6QVRHN.

    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.

    A9R1E6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKSENLYAQ AQQLIPGGVN SPVRAFTGVG GIPLFIERAD GAYLFDVDGK    50
    AYIDYVGSWG PMILGHNHPA IRQAVIEAVE RGLSFGAPTE MEVKMAQLVT 100
    DLVPTMDMVR MVNSGTEATM SAIRLARGYT GRDKIIKFEG CYHGHADCLL 150
    VKAGSGALTL GQPNSPGVPT DFAKHTLTCT YNDLASVRQA FEQYPQEVAC 200
    IIVEPVAGNM NCIPPLPEFL PGLRALCDEF GALLIIDEVM TGFRVALAGA 250
    QDYYHVIPDL TCLGKIIGGG MPVGAFGGRR EVMNALAPTG PVYQAGTLSG 300
    NPIAMAAGFA CLTEISQVGV YETLTELTDS LATGLRHAAK EENIPLVVNH 350
    VGGMFGLFFT NADTVTCYQD VMNCDVERFK RFFHLMLEEG VYLAPSAFEA 400
    GFMSLAHSNE DIQKTVNAAR RCFAKL 426
    Length:426
    Mass (Da):45,794
    Last modified:February 5, 2008 - v1
    Checksum:i1BB579AE82D49BA4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000901 Genomic DNA. Translation: ABX88310.1.
    RefSeqiYP_001605556.1. NC_010159.1.

    Genome annotation databases

    EnsemblBacteriaiABX88310; ABX88310; YpAngola_A0995.
    GeneIDi5799458.
    KEGGiypg:YpAngola_A0995.
    PATRICi18571038. VBIYerPes97331_1314.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000901 Genomic DNA. Translation: ABX88310.1 .
    RefSeqi YP_001605556.1. NC_010159.1.

    3D structure databases

    ProteinModelPortali A9R1E6.
    SMRi A9R1E6. Positions 2-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 349746.YpAngola_A0995.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX88310 ; ABX88310 ; YpAngola_A0995 .
    GeneIDi 5799458.
    KEGGi ypg:YpAngola_A0995.
    PATRICi 18571038. VBIYerPes97331_1314.

    Phylogenomic databases

    eggNOGi COG0001.
    HOGENOMi HOG000020210.
    KOi K01845.
    OMAi RAIKPYP.
    OrthoDBi EOG6QVRHN.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    BioCyci YPES349746:GHPB-995-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. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
      Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
      J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Angola.

    Entry informationi

    Entry nameiGSA_YERPG
    AccessioniPrimary (citable) accession number: A9R1E6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 52 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

    Documents

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

    External Data

    Dasty 3