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Q3AWP4

- GSA_SYNS9

UniProt

Q3AWP4 - GSA_SYNS9

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Synechococcus sp. (strain CC9902)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 2 (27 Jun 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. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
    2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Chlorophyll biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciSSP316279:GJCI-1717-MONOMER.
    UniPathwayiUPA00251; UER00317.
    UPA00668.

    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:Syncc9902_1701
    OrganismiSynechococcus sp. (strain CC9902)
    Taxonomic identifieri316279 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000002712: 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 – 428428Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000243628Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei267 – 2671N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi316279.Syncc9902_1701.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3AWP4.
    SMRiQ3AWP4. Positions 3-421.
    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.
    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.

    Q3AWP4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTSRSQAIF GAAQGLMPGG VSSPVRAFKS VGGQPIVFDR VKGPYAWDVD    50
    GNKYIDYIGS WGPAICGHAH PEVISALQEA IEKGTSFGAP CALENTLAEM 100
    VIDAVPSVEM VRFVNSGTEA CMAVLRLMRA FTGRDKVIKF EGCYHGHADM 150
    FLVKAGSGVA TLGLPDSPGV PRSTTANTLT APYNDLEAVK ALFAENPDAI 200
    SGVILEPIVG NAGFIQPEPG FLEGLRELTK ENGALLVFDE VMTGFRISYG 250
    GAQAHFGVTP DLTTMGKVIG GGLPVGAYGG RADIMQMVSP AGPMYQAGTL 300
    SGNPLAMTAG IKTLELLKQP GTYEKLAATT ERLISGIKTA AGEAGFPITG 350
    GSVSAMFGFF LCEGPVRNFE EAKATDSERF GRLHRAMLER GVYLAPSAYE 400
    AGFTSLAHSD ADIEATINAF RESFAVIG 428
    Length:428
    Mass (Da):44,935
    Last modified:June 27, 2006 - v2
    Checksum:iFC11BD86952A8B27
    GO

    Sequence cautioni

    The sequence ABB26659.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000097 Genomic DNA. Translation: ABB26659.1. Different initiation.
    RefSeqiYP_377703.2. NC_007513.1.

    Genome annotation databases

    EnsemblBacteriaiABB26659; ABB26659; Syncc9902_1701.
    GeneIDi3742191.
    KEGGisye:Syncc9902_1701.
    PATRICi23800879. VBISynSp76179_1891.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000097 Genomic DNA. Translation: ABB26659.1 . Different initiation.
    RefSeqi YP_377703.2. NC_007513.1.

    3D structure databases

    ProteinModelPortali Q3AWP4.
    SMRi Q3AWP4. Positions 3-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 316279.Syncc9902_1701.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB26659 ; ABB26659 ; Syncc9902_1701 .
    GeneIDi 3742191.
    KEGGi sye:Syncc9902_1701.
    PATRICi 23800879. VBISynSp76179_1891.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    UPA00668 .
    BioCyci SSP316279:GJCI-1717-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 Synechococcus sp. CC9902."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CC9902.

    Entry informationi

    Entry nameiGSA_SYNS9
    AccessioniPrimary (citable) accession number: Q3AWP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: June 27, 2006
    Last modified: October 1, 2014
    This is version 70 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

    Documents

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

    External Data

    Dasty 3