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Protein

L-lysine cyclodeaminase

Gene

rapL

Organism
Streptomyces hygroscopicus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Converts L-lysine to L-pipecolate, which is incorporated into multiple secondary metabolite products, including rapamycin, tobulysin, virginiamycin and pristinamycin.1 Publication

Catalytic activityi

L-lysine = L-pipecolate + NH3.1 Publication

Cofactori

NAD+1 Publication

Enzyme regulationi

Inhibited by nipecotic acid and thiazolidine-2-carboxylic acid.1 Publication

Kineticsi

kcat is 0.61 min(-1) with L-lysine as substrate.

  1. KM=46 µM for L-lysine1 Publication

    Pathwayi: Antibiotic biosynthesis

    This protein is involved in Antibiotic biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in Antibiotic biosynthesis.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17627.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-lysine cyclodeaminase (EC:4.3.1.28)
    Alternative name(s):
    Rapamycin biosynthesis protein L
    Gene namesi
    Name:rapL
    OrganismiStreptomyces hygroscopicus
    Taxonomic identifieri1912 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

    Pathology & Biotechi

    Disruption phenotypei

    Cells do not produce significant amounts of rapamycin. Cells supplemented by L-pipecolate restore levels of rapamycin.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004239871 – 343L-lysine cyclodeaminaseAdd BLAST343

    Structurei

    3D structure databases

    ProteinModelPortaliQ54304.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    KOiK20500.

    Family and domain databases

    Gene3Di3.30.1780.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR003462. ODC_Mu_crystall.
    IPR023401. ODC_N.
    [Graphical view]
    PfamiPF02423. OCD_Mu_crystall. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001439. CryM. 1 hit.
    SUPFAMiSSF51735. SSF51735. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q54304-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQTKVLCQRD IKRILSVVGR DVMMDRLISE VHAGFARLGR GETDEPPPRP
    60 70 80 90 100
    GFARGGDVPG VIEFMPHRAS GIGVTMKTVS YSPENFERFN LPTIVGTVSR
    110 120 130 140 150
    LGDDSGSMVA LADAATITAM RTGAVASVTT RLLARPGSTT LALIGAGAQA
    160 170 180 190 200
    VTQAHALSRV LPLERILISD IKAEHAESFA GRVAFLELPV EVTDAATAMA
    210 220 230 240 250
    TADVLCTVTS VPVGGGPVVP AEPRQAHLHV NGIGADEQGK TELPKALLDD
    260 270 280 290 300
    AFICVDHPGQ ARAEGEFQQL PDRELGPSLA DLCAAPEIAA PHPERLSVFD
    310 320 330 340
    STGSAFADHI ALDVLLGFAD ELGLGHKMSI ESTPEDVLDP YSL
    Length:343
    Mass (Da):36,076
    Last modified:November 1, 1996 - v1
    Checksum:i1123731B76C6D2A3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X86780 Genomic DNA. Translation: CAA60467.1.
    PIRiT30233.

    Genome annotation databases

    KEGGiag:CAA60467.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X86780 Genomic DNA. Translation: CAA60467.1.
    PIRiT30233.

    3D structure databases

    ProteinModelPortaliQ54304.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:CAA60467.

    Phylogenomic databases

    KOiK20500.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17627.

    Family and domain databases

    Gene3Di3.30.1780.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR003462. ODC_Mu_crystall.
    IPR023401. ODC_N.
    [Graphical view]
    PfamiPF02423. OCD_Mu_crystall. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001439. CryM. 1 hit.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiRAPL_STRHY
    AccessioniPrimary (citable) accession number: Q54304
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 16, 2013
    Last sequence update: November 1, 1996
    Last modified: November 2, 2016
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.