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Q9RWW0

- GSA_DEIRA

UniProt

Q9RWW0 - GSA_DEIRA

Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (01 Jun 2001)
      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

    BioCyciDRAD243230:GH46-569-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:DR_0555
    OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
    Taxonomic identifieri243230 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
    ProteomesiUP000002524: Chromosome I

    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 – 444444Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120407Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei278 – 2781N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243230.DR_0555.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9RWW0.
    SMRiQ9RWW0. Positions 12-439.
    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.

    Q9RWW0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLSETHPTA RSEALFVRAR AVTPGGVNSP VRAFRSVGGV PRFIASAQGA    50
    YLTDADGARY LDYIGSWGPM ILGHNHPAVR DAVAQALASG TSFGAPNERE 100
    VELAELIVEL TGAERVRFVS SGTEATMSAL RLARGYTGRK FIVKFRGNYH 150
    GHADGLLVEA GSGLLTNAEG DLGAAAPSSA GVPEEYAGLT LVLDYNDPEA 200
    LDALMAQRGD EIAAVIFEPV VGNAGVLIPT SDFLAALHRV RDFGAVLIAD 250
    EVMTGFRLSL NGATGLLSLD PDLRCWGKIV GGGLPVGAYG GRADIMDFVS 300
    PQGPVYQAGT LSGNPLAMAA GIATLRELKA NPGLYRQLDE YAARLAAGLR 350
    GAAERAGVAV SINHIGSMLT VFFQDAPDGS VRDYAAAARS DTAAFAAWFQ 400
    GLLARGIYWA PSQFESIFIS AAHGEPELAA TLEAAAQAFE GVKP 444
    Length:444
    Mass (Da):46,305
    Last modified:June 1, 2001 - v2
    Checksum:i344BFE4E3107A8C8
    GO

    Sequence cautioni

    The sequence AAF10132.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000513 Genomic DNA. Translation: AAF10132.1. Different initiation.
    PIRiE75505.
    RefSeqiNP_294278.1. NC_001263.1.

    Genome annotation databases

    EnsemblBacteriaiAAF10132; AAF10132; DR_0555.
    GeneIDi1799707.
    KEGGidra:DR_0555.
    PATRICi21628634. VBIDeiRad64572_0730.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000513 Genomic DNA. Translation: AAF10132.1 . Different initiation.
    PIRi E75505.
    RefSeqi NP_294278.1. NC_001263.1.

    3D structure databases

    ProteinModelPortali Q9RWW0.
    SMRi Q9RWW0. Positions 12-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243230.DR_0555.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF10132 ; AAF10132 ; DR_0555 .
    GeneIDi 1799707.
    KEGGi dra:DR_0555.
    PATRICi 21628634. VBIDeiRad64572_0730.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00317 .
    BioCyci DRAD243230:GH46-569-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

    Entry informationi

    Entry nameiGSA_DEIRA
    AccessioniPrimary (citable) accession number: Q9RWW0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 102 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3