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P23893

- GSA_ECOLI

UniProt

P23893 - GSA_ECOLI

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    GO - Molecular functioni

    1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: EcoCyc
    2. identical protein binding Source: EcoCyc
    3. protein binding Source: IntAct
    4. pyridoxal phosphate binding Source: InterPro
    5. transaminase activity Source: InterPro

    GO - Biological processi

    1. protoporphyrinogen IX biosynthetic process Source: EcoCyc
    2. tetrapyrrole biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Porphyrin biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:GSAAMINOTRANS-MONOMER.
    ECOL316407:JW0150-MONOMER.
    MetaCyc:GSAAMINOTRANS-MONOMER.
    UniPathwayiUPA00251; UER00317.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate-1-semialdehyde 2,1-aminomutase (EC:5.4.3.8)
    Short name:
    GSA
    Alternative name(s):
    Glutamate-1-semialdehyde aminotransferase
    Short name:
    GSA-AT
    Gene namesi
    Name:hemL
    Synonyms:gsa, popC
    Ordered Locus Names:b0154, JW0150
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10432. hemL.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi265 – 2651K → R: 2% of wild-type activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 426426Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120408Add
    BLAST

    Amino acid modifications

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

    Proteomic databases

    PaxDbiP23893.
    PRIDEiP23893.

    Expressioni

    Inductioni

    Induced by low extracellular levels of magnesium via the PhoQ/PhoP two-component regulatory system.1 Publication

    Gene expression databases

    GenevestigatoriP23893.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    glcCP0ACL54EBI-909193,EBI-1115389

    Protein-protein interaction databases

    DIPiDIP-9886N.
    IntActiP23893. 2 interactions.
    STRINGi511145.b0154.

    Structurei

    3D structure databases

    ProteinModelPortaliP23893.
    SMRiP23893. Positions 1-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0001.
    HOGENOMiHOG000020210.
    KOiK01845.
    OMAiRAIKPYP.
    OrthoDBiEOG6QVRHN.
    PhylomeDBiP23893.

    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.

    P23893-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKSENLYSA ARELIPGGVN SPVRAFTGVG GTPLFIEKAD GAYLYDVDGK    50
    AYIDYVGSWG PMVLGHNHPA IRNAVIEAAE RGLSFGAPTE MEVKMAQLVT 100
    ELVPTMDMVR MVNSGTEATM SAIRLARGFT GRDKIIKFEG CYHGHADCLL 150
    VKAGSGALTL GQPNSPGVPA DFAKYTLTCT YNDLASVRAA FEQYPQEIAC 200
    IIVEPVAGNM NCVPPLPEFL PGLRALCDEF GALLIIDEVM TGFRVALAGA 250
    QDYYGVVPDL TCLGKIIGGG MPVGAFGGRR DVMDALAPTG PVYQAGTLSG 300
    NPIAMAAGFA CLNEVAQPGV HETLDELTTR LAEGLLEAAE EAGIPLVVNH 350
    VGGMFGIFFT DAESVTCYQD VMACDVERFK RFFHMMLDEG VYLAPSAFEA 400
    GFMSVAHSME DINNTIDAAR RVFAKL 426
    Length:426
    Mass (Da):45,366
    Last modified:November 1, 1997 - v2
    Checksum:iBED817E100468CF2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21S → R(PubMed:1900346)Curated
    Sequence conflicti2 – 21S → R(PubMed:8202364)Curated
    Sequence conflicti9 – 91S → Q(PubMed:1900346)Curated
    Sequence conflicti9 – 91S → Q(PubMed:8202364)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53696 Genomic DNA. Translation: CAA37734.1.
    U00096 Genomic DNA. Translation: AAC73265.1.
    AP009048 Genomic DNA. Translation: BAB96731.2.
    U70214 Genomic DNA. Translation: AAB08584.1.
    PIRiB64739.
    RefSeqiNP_414696.1. NC_000913.3.
    YP_488457.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73265; AAC73265; b0154.
    BAB96731; BAB96731; BAB96731.
    GeneIDi12931839.
    946892.
    KEGGiecj:Y75_p0151.
    eco:b0154.
    PATRICi32115417. VBIEscCol129921_0160.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53696 Genomic DNA. Translation: CAA37734.1 .
    U00096 Genomic DNA. Translation: AAC73265.1 .
    AP009048 Genomic DNA. Translation: BAB96731.2 .
    U70214 Genomic DNA. Translation: AAB08584.1 .
    PIRi B64739.
    RefSeqi NP_414696.1. NC_000913.3.
    YP_488457.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P23893.
    SMRi P23893. Positions 1-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9886N.
    IntActi P23893. 2 interactions.
    STRINGi 511145.b0154.

    Proteomic databases

    PaxDbi P23893.
    PRIDEi P23893.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73265 ; AAC73265 ; b0154 .
    BAB96731 ; BAB96731 ; BAB96731 .
    GeneIDi 12931839.
    946892.
    KEGGi ecj:Y75_p0151.
    eco:b0154.
    PATRICi 32115417. VBIEscCol129921_0160.

    Organism-specific databases

    EchoBASEi EB0427.
    EcoGenei EG10432. hemL.

    Phylogenomic databases

    eggNOGi COG0001.
    HOGENOMi HOG000020210.
    KOi K01845.
    OMAi RAIKPYP.
    OrthoDBi EOG6QVRHN.
    PhylomeDBi P23893.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    BioCyci EcoCyc:GSAAMINOTRANS-MONOMER.
    ECOL316407:JW0150-MONOMER.
    MetaCyc:GSAAMINOTRANS-MONOMER.

    Miscellaneous databases

    PROi P23893.

    Gene expression databases

    Genevestigatori P23893.

    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. "Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli."
      Grimm B., Bull A., Breu V.
      Mol. Gen. Genet. 225:1-10(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
      Fujita N., Mori H., Yura T., Ishihama A.
      Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 2 AND 9.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase."
      Ilag L.L., Jahn D., Eggertsson G., Soell D.
      J. Bacteriol. 173:3408-3413(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R."
      Ilag L.L., Jahn D.
      Biochemistry 31:7143-7151(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-265.
    8. "Identification and molecular characterization of the Mg2+ stimulon of Escherichia coli."
      Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T., Mori H., Ishihama A., Utsumi R.
      J. Bacteriol. 185:3696-3702(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: K12.

    Entry informationi

    Entry nameiGSA_ECOLI
    AccessioniPrimary (citable) accession number: P23893
    Secondary accession number(s): P78277
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 139 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, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3