ID   MPPO_STRHY              Reviewed;         341 AA.
AC   Q643C1;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Enduracididine beta-hydroxylase;
DE            EC=1.14.11.40;
DE   AltName: Full=Mannopeptimycin biosynthesis protein O;
GN   Name=mppO;
OS   Streptomyces hygroscopicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=1912;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 30439;
RX   PubMed=16723579; DOI=10.1128/aac.01545-05;
RA   Magarvey N.A., Haltli B., He M., Greenstein M., Hucul J.A.;
RT   "Biosynthetic pathway for mannopeptimycins, lipoglycopeptide antibiotics
RT   active against drug-resistant gram-positive pathogens.";
RL   Antimicrob. Agents Chemother. 50:2167-2177(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=NRRL 30439;
RX   PubMed=16298295; DOI=10.1016/j.chembiol.2005.09.013;
RA   Haltli B., Tan Y., Magarvey N.A., Wagenaar M., Yin X., Greenstein M.,
RA   Hucul J.A., Zabriskie T.M.;
RT   "Investigating beta-hydroxyenduracididine formation in the biosynthesis of
RT   the mannopeptimycins.";
RL   Chem. Biol. 12:1163-1168(2005).
CC   -!- FUNCTION: Hydroxylates the beta carbon of free L-enduracididine to
CC       produce (3S)-3-hydroxy-L-enduracididine in biosynthesis of the
CC       nonproteinogenic amino acid beta-hydroxyenduracididine, a component of
CC       antibiotic mannopeptimycin. {ECO:0000269|PubMed:16298295}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-enduracididine + O2 = (3S)-3-hydroxy-L-
CC         enduracididine + CO2 + succinate; Xref=Rhea:RHEA:36603,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:73936, ChEBI:CHEBI:73937;
CC         EC=1.14.11.40; Evidence={ECO:0000269|PubMed:16298295};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:16298295}.
CC   -!- DISRUPTION PHENOTYPE: Cells produce dideoxy-mannopeptimycins.
CC       {ECO:0000269|PubMed:16298295}.
CC   -!- SIMILARITY: Belongs to the clavaminate synthase family. {ECO:0000305}.
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DR   EMBL; AY735112; AAU34208.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q643C1; -.
DR   SMR; Q643C1; -.
DR   KEGG; ag:AAU34208; -.
DR   BRENDA; 1.14.11.40; 6043.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.130.10; -; 1.
DR   InterPro; IPR014503; Clavaminate_syn-like.
DR   InterPro; IPR042098; TauD-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   Pfam; PF02668; TauD; 1.
DR   PIRSF; PIRSF019543; Clavaminate_syn; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..341
FT                   /note="Enduracididine beta-hydroxylase"
FT                   /id="PRO_0000423988"
FT   REGION          203..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         146
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  38548 MW;  41FD91395A9D5345 CRC64;
     MLTLHLQDDD VAAIDAVADE LSRRYDSVES TEFQAESRLY ADELPRRVRR ALHEYRSTEK
     SGILVVTGLP VDDSALGATP ADRRHKPVPS TSLRQDIAFY LIANLLGDPI GWATQQDGFI
     MHDVYPVQGF EHEQIGWGSE ETLTWHTEDA FHPLRTDYLG LMCLRNPDGV ETTACDIADV
     EIDDETRETL SQERFRILPD DAHRIHGKAP GDESARESAL RERSRQRVAS ALESPDPVAV
     LFGDRDDPYL RIDPHYMQGV QGETEQRALE TIGAAIDDAM SGVVLSPGDI VFIDNYRVVH
     GRKPFRARFD GTDRWLRRLN IARDLRKSRE ARLAATTRVI Y