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B9J3N2

- GSA1_BACCQ

UniProt

B9J3N2 - GSA1_BACCQ

Protein

Glutamate-1-semialdehyde 2,1-aminomutase 1

Gene

hemL1

Organism
Bacillus cereus (strain Q1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (24 Mar 2009)
      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

    BioCyciBCER361100:GJ7M-549-MONOMER.
    UniPathwayiUPA00251; UER00317.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate-1-semialdehyde 2,1-aminomutase 1UniRule annotation (EC:5.4.3.8UniRule annotation)
    Short name:
    GSA 1UniRule annotation
    Alternative name(s):
    Glutamate-1-semialdehyde aminotransferase 1UniRule annotation
    Short name:
    GSA-AT 1UniRule annotation
    Gene namesi
    Name:hemL1UniRule annotation
    Ordered Locus Names:BCQ_0559
    OrganismiBacillus cereus (strain Q1)
    Taxonomic identifieri361100 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000000441: 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 – 434434Glutamate-1-semialdehyde 2,1-aminomutase 1PRO_0000382273Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi361100.BCQ_0559.

    Structurei

    3D structure databases

    ProteinModelPortaliB9J3N2.
    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.
    OMAiETRANGM.
    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.

    B9J3N2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVKFTKSEA LHKEALEHIV GGVNSPSRSF KAVGGGAPVA MERGKGAYFW    50
    DVDGNKYIDY LAAYGPIITG HAHPHITKAI TTAAENGVLY GTPTALEVKF 100
    AKMLKEAMPA LDKVRFVNSG TEAVMTTIRV ARAYTGRTKI MKFAGCYHGH 150
    SDLVLVAAGS GPSTLGTPDS AGVPQSIAQE VITVPFNNVE TLKEALDKWG 200
    HEVAAILVEP IVGNFGIVEP KPGFLEKVNE LVHEAGALVI YDEVITAFRF 250
    MYGGAQDLLG VTPDLTALGK VIGGGLPIGA YGGKKEIMEQ VAPLGPAYQA 300
    GTMAGNPASM ASGIACLEVL QQEGLYEKLD ELGAMLEKGI LEQAEKHNID 350
    ITLNRLKGAL TVYFTTNTIE DYDAAQDTDG EMFGKFFKLM LQEGINLAPS 400
    KYEAWFLTTE HTKEDIEYTI EAVGRAFAAL ANNK 434
    Length:434
    Mass (Da):46,489
    Last modified:March 24, 2009 - v1
    Checksum:iB02A06345C49D46D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000227 Genomic DNA. Translation: ACM11031.1.
    RefSeqiYP_002528323.1. NC_011969.1.

    Genome annotation databases

    EnsemblBacteriaiACM11031; ACM11031; BCQ_0559.
    GeneIDi7372376.
    KEGGibcq:BCQ_0559.
    PATRICi18908581. VBIBacCer120424_0505.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000227 Genomic DNA. Translation: ACM11031.1 .
    RefSeqi YP_002528323.1. NC_011969.1.

    3D structure databases

    ProteinModelPortali B9J3N2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 361100.BCQ_0559.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACM11031 ; ACM11031 ; BCQ_0559 .
    GeneIDi 7372376.
    KEGGi bcq:BCQ_0559.
    PATRICi 18908581. VBIBacCer120424_0505.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    BioCyci BCER361100:GJ7M-549-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. "Complete genome sequence of the extremophilic Bacillus cereus strain Q1 with industrial applications."
      Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., Xue Y., Zhu Y., Jin Q.
      J. Bacteriol. 191:1120-1121(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Q1.

    Entry informationi

    Entry nameiGSA1_BACCQ
    AccessioniPrimary (citable) accession number: B9J3N2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 1, 2009
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 43 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