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Q14HS1

- GSA_FRAT1

UniProt

Q14HS1 - GSA_FRAT1

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (22 Aug 2006)
      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

    BioCyciFTUL393115:GJUT-945-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:FTF0927
    OrganismiFrancisella tularensis subsp. tularensis (strain FSC 198)
    Taxonomic identifieri393115 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
    ProteomesiUP000001821: 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 – 431431Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000300914Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei269 – 2691N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi393115.FTF0927.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14HS1.
    SMRiQ14HS1. Positions 1-424.
    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.

    Q14HS1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENKSNSQIL FAEAQQYIPG GVNSPVRAFK SVGQEFPRFI KFAKGAYLYD    50
    VDWNKYIDYI GSWGPMILGH CDDDVLEAIQ CQVKNGLSYG APCKQEVDLA 100
    KKIIELMPNI EQVRFVNSGT EATMSAIRLA RAYTCRNKII KFEGCYHGHA 150
    DEFLVAAGSG ALSLGQPNSP GVPEDVVKDT LVASFNDMES IQALFEKYKD 200
    EIACIIIEPI AGNMNMIFPQ DDFLAKLRAI CDQNSSLLIF DEVMTGFRVA 250
    LGGAQSIYNV KPDLTTLGKV IGGGMPVGAF GGRKEIMQKV SPAGPVYQAG 300
    TLSGNPIAMT AGIKTLEKIS QPGFFDELGA KAQKLVDGLN EAAKAYDFNF 350
    HAKCLGGMFG LFFCSDKIAV NTFVDLGKTN LKMFNQFFAY MLDNGVYLAP 400
    SAYEAGFISI AHSDEDIEKT IYLAKKFFQE N 431
    Length:431
    Mass (Da):47,186
    Last modified:August 22, 2006 - v1
    Checksum:iB88FE73756171C25
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM286280 Genomic DNA. Translation: CAL08943.1.
    RefSeqiYP_667055.1. NC_008245.1.

    Genome annotation databases

    EnsemblBacteriaiCAL08943; CAL08943; FTF0927.
    GeneIDi4200378.
    KEGGiftf:FTF0927.
    PATRICi17960786. VBIFraTul133500_1058.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM286280 Genomic DNA. Translation: CAL08943.1 .
    RefSeqi YP_667055.1. NC_008245.1.

    3D structure databases

    ProteinModelPortali Q14HS1.
    SMRi Q14HS1. Positions 1-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 393115.FTF0927.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL08943 ; CAL08943 ; FTF0927 .
    GeneIDi 4200378.
    KEGGi ftf:FTF0927.
    PATRICi 17960786. VBIFraTul133500_1058.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    BioCyci FTUL393115:GJUT-945-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 sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
      Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
      PLoS ONE 2:E352-E352(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FSC 198.

    Entry informationi

    Entry nameiGSA_FRAT1
    AccessioniPrimary (citable) accession number: Q14HS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 59 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