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Protein

Mycinamicin IV hydroxylase/epoxidase

Gene

mycG

Organism
Micromonospora griseorubida
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic. Catalyzes consecutive hydroxylation (at C14) and epoxidation (at C12-C13) reactions with mycinamicin IV as initial substrate, leading to mycinamicin II. These reactions require prior dimethylation of 6-deoxyallose to mycinose for effective conversion by the dual function MycG enzyme.3 Publications

Cofactori

heme1 Publication

Kineticsi

kcat is 415.7 min(-1) for the epoxydation of mycinamicin V.1 Publication

  1. KM=16.2 µM for mycinamicin V1 Publication

    Pathwayi: mycinamicin biosynthesis

    This protein is involved in the pathway mycinamicin biosynthesis, which is part of Antibiotic biosynthesis.1 Publication1 Publication
    View all proteins of this organism that are known to be involved in the pathway mycinamicin biosynthesis and in Antibiotic biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei81 – 811Substrate; via carbonyl oxygenCombined sources1 Publication
    Binding sitei91 – 911Heme1 Publication
    Binding sitei95 – 951Heme1 Publication
    Binding sitei288 – 2881Heme1 Publication
    Binding sitei344 – 3441Heme1 Publication
    Metal bindingi346 – 3461Iron (heme axial ligand)Combined sources1 Publication

    GO - Molecular functioni

    • heme binding Source: UniProtKB
    • iron ion binding Source: UniProtKB
    • monooxygenase activity Source: UniProtKB
    • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Source: InterPro

    GO - Biological processi

    • antibiotic biosynthetic process Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18369.
    UniPathwayiUPA01019.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mycinamicin IV hydroxylase/epoxidase1 Publication (EC:1.14.-.-1 Publication)
    Alternative name(s):
    Cytochrome P450 MycG1 Publication
    Multifunctional P450 enzyme1 Publication
    Mycinamicin biosynthesis protein G1 Publication
    Gene namesi
    Name:mycG1 Publication
    OrganismiMicromonospora griseorubida
    Taxonomic identifieri28040 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaMicromonosporalesMicromonosporaceaeMicromonospora

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene do not produce mycinamicin I, mycinamicin II and mycinamicin V, and accumulate mycinamicin IV.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi286 – 2861F → A or V: Decrease in catalytic activiy. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 397397Mycinamicin IV hydroxylase/epoxidasePRO_0000434765Add
    BLAST

    Structurei

    Secondary structure

    1
    397
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 94Combined sources
    Beta strandi14 – 163Combined sources
    Helixi21 – 299Combined sources
    Beta strandi31 – 366Combined sources
    Beta strandi38 – 403Combined sources
    Beta strandi43 – 464Combined sources
    Helixi49 – 568Combined sources
    Beta strandi61 – 633Combined sources
    Helixi64 – 674Combined sources
    Beta strandi73 – 775Combined sources
    Helixi83 – 853Combined sources
    Helixi90 – 10112Combined sources
    Helixi104 – 1096Combined sources
    Helixi111 – 12818Combined sources
    Beta strandi130 – 1334Combined sources
    Helixi134 – 1374Combined sources
    Turni138 – 1414Combined sources
    Helixi142 – 15110Combined sources
    Helixi155 – 1573Combined sources
    Helixi158 – 1669Combined sources
    Helixi176 – 19924Combined sources
    Helixi205 – 2117Combined sources
    Helixi221 – 25232Combined sources
    Helixi254 – 2629Combined sources
    Helixi264 – 2663Combined sources
    Helixi267 – 27711Combined sources
    Beta strandi281 – 2833Combined sources
    Beta strandi288 – 2925Combined sources
    Beta strandi294 – 2963Combined sources
    Beta strandi299 – 3013Combined sources
    Beta strandi306 – 3094Combined sources
    Helixi311 – 3144Combined sources
    Turni318 – 3203Combined sources
    Turni322 – 3254Combined sources
    Helixi342 – 3443Combined sources
    Helixi349 – 36618Combined sources
    Beta strandi371 – 3744Combined sources
    Helixi376 – 3783Combined sources
    Beta strandi385 – 3873Combined sources
    Beta strandi394 – 3963Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y46X-ray1.83A/B/C1-397[»]
    2Y5NX-ray1.62A/B1-397[»]
    2Y5ZX-ray2.06A/B/C1-397[»]
    2Y98X-ray1.65A1-397[»]
    2YCAX-ray1.80A1-397[»]
    2YGXX-ray2.39A/B/C/D1-397[»]
    3ZSNX-ray1.90A/B/C1-397[»]
    4AW3X-ray2.05A/B1-397[»]
    ProteinModelPortaliQ59523.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    IPR017972. Cyt_P450_CS.
    [Graphical view]
    PfamiPF00067. p450. 2 hits.
    [Graphical view]
    PRINTSiPR00359. BP450.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q59523-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTSAEPRAYP FNDVHGLTLA GRYGELQETE PVSRVRPPYG EEAWLVTRYE
    60 70 80 90 100
    DVRAVLGDGR FVRGPSMTRD EPRTRPEMVK GGLLSMDPPE HSRLRRLVVK
    110 120 130 140 150
    AFTARRAESL RPRAREIAHE LVDQMAATGQ PADLVAMFAR QLPVRVICEL
    160 170 180 190 200
    LGVPSADHDR FTRWSGAFLS TAEVTAEEMQ EAAEQAYAYM GDLIDRRRKE
    210 220 230 240 250
    PTDDLVSALV QARDQQDSLS EQELLDLAIG LLVAGYESTT TQIADFVYLL
    260 270 280 290 300
    MTRPELRRQL LDRPELIPSA VEELTRWVPL GVGTAFPRYA VEDVTLRGVT
    310 320 330 340 350
    IRAGEPVLAS TGAANRDQAQ FPDADRIDVD RTPNQHLGFG HGVHHCLGAP
    360 370 380 390
    LARVELQVAL EVLLQRLPGI RLGIPETQLR WSEGMLLRGP LELPVVW
    Length:397
    Mass (Da):44,332
    Last modified:November 1, 1996 - v1
    Checksum:i0FE6A251BEB5E233
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D16098 Genomic DNA. Translation: BAA03672.1.
    PIRiS51594.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D16098 Genomic DNA. Translation: BAA03672.1.
    PIRiS51594.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y46X-ray1.83A/B/C1-397[»]
    2Y5NX-ray1.62A/B1-397[»]
    2Y5ZX-ray2.06A/B/C1-397[»]
    2Y98X-ray1.65A1-397[»]
    2YCAX-ray1.80A1-397[»]
    2YGXX-ray2.39A/B/C/D1-397[»]
    3ZSNX-ray1.90A/B/C1-397[»]
    4AW3X-ray2.05A/B1-397[»]
    ProteinModelPortaliQ59523.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA01019.
    BioCyciMetaCyc:MONOMER-18369.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    IPR017972. Cyt_P450_CS.
    [Graphical view]
    PfamiPF00067. p450. 2 hits.
    [Graphical view]
    PRINTSiPR00359. BP450.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Characterization and expression of a P-450-like mycinamicin biosynthesis gene using a novel Micromonospora-Escherichia coli shuttle cosmid vector."
      Inouye M., Takada Y., Muto N., Horinouchi S., Beppu T.
      Mol. Gen. Genet. 245:456-464(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: A11725Imported.
    2. "Functional analysis of MycCI and MycG, cytochrome P450 enzymes involved in biosynthesis of mycinamicin macrolide antibiotics."
      Anzai Y., Li S., Chaulagain M.R., Kinoshita K., Kato F., Montgomery J., Sherman D.H.
      Chem. Biol. 15:950-959(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
    3. "Function of cytochrome P450 enzymes MycCI and MycG in Micromonospora griseorubida, a producer of the macrolide antibiotic mycinamicin."
      Anzai Y., Tsukada S., Sakai A., Masuda R., Harada C., Domeki A., Li S., Kinoshita K., Sherman D.H., Kato F.
      Antimicrob. Agents Chemother. 56:3648-3656(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, PATHWAY.
      Strain: A11725.
    4. "Substrate recognition by the multifunctional cytochrome P450 MycG in mycinamicin hydroxylation and epoxidation reactions."
      Li S., Tietz D.R., Rutaganira F.U., Kells P.M., Anzai Y., Kato F., Pochapsky T.C., Sherman D.H., Podust L.M.
      J. Biol. Chem. 287:37880-37890(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-286 AND VAL-286 IN COMPLEXES WITH HEME; MYCINAMICIN III; MYCINAMICIN IV AND MYCINAMICIN V, COFACTOR, MUTAGENESIS OF PHE-286.

    Entry informationi

    Entry nameiMYCG_MICGR
    AccessioniPrimary (citable) accession number: Q59523
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 11, 2015
    Last sequence update: November 1, 1996
    Last modified: January 20, 2016
    This is version 75 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

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.