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B2TPD4

- GSA_CLOBB

UniProt

B2TPD4 - GSA_CLOBB

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Clostridium botulinum (strain Eklund 17B / Type B)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (01 Jul 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

    BioCyciCBOT508765:GJ4H-2893-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:CLL_A2904
    OrganismiClostridium botulinum (strain Eklund 17B / Type B)
    Taxonomic identifieri935198 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000001195: 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000121871Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei264 – 2641N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi508765.CLL_A2904.

    Structurei

    3D structure databases

    ProteinModelPortaliB2TPD4.
    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.
    OMAiLMAHIAP.
    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.

    B2TPD4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNNLEIFEES KKYMPGGVNS PVRCFKEMGM NPPVIKSGKG VIIKDEDGKE    50
    YIDFVLAWGP LLLGHCDEDV VKAIKETSEN ALAFGAPTKL ELELSKFMCE 100
    NLDNVDMIRM VNSGTEATMS AVKLARGYTG KSKIVKFAGC YHGHFDGFLI 150
    EAGSGVLTEG IPGSLGVPKE SVENTLIGLY NDKTQIKELF KKQGNEIAAV 200
    IIEPVAGNMG VIKANEDFIK ELRSLCDEYG ALLIFDEVMT GFRVAFKGAQ 250
    TLFDIKPDLI TYAKIMGGGL PCGAYAGKKE IMEKLSPCGG VYQAGTMSGN 300
    PVVMSAGLAT LTKLKNNIEL YDHVEKIGEK LQEGLIKISK ENDVPLIINR 350
    VGGMLTLFFT ELEKVNTYED VKTCDNERFK RYFKHMLNEG FNIAPSQFEA 400
    MFLSVKHTEE HIDKFLDAFK RFAINEK 427
    Length:427
    Mass (Da):47,203
    Last modified:July 1, 2008 - v1
    Checksum:i6455DF7FA23DC18E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001056 Genomic DNA. Translation: ACD21981.1.
    RefSeqiYP_001887091.1. NC_010674.1.

    Genome annotation databases

    EnsemblBacteriaiACD21981; ACD21981; CLL_A2904.
    GeneIDi6294866.
    KEGGicbk:CLL_A2904.
    PATRICi19398622. VBICloBot123574_2814.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001056 Genomic DNA. Translation: ACD21981.1 .
    RefSeqi YP_001887091.1. NC_010674.1.

    3D structure databases

    ProteinModelPortali B2TPD4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 508765.CLL_A2904.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACD21981 ; ACD21981 ; CLL_A2904 .
    GeneIDi 6294866.
    KEGGi cbk:CLL_A2904.
    PATRICi 19398622. VBICloBot123574_2814.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    BioCyci CBOT508765:GJ4H-2893-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 sequence of Clostridium botulinum strain Eklund."
      Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
      Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Eklund 17B / Type B.

    Entry informationi

    Entry nameiGSA_CLOBB
    AccessioniPrimary (citable) accession number: B2TPD4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 47 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