ID   ECDK_ASPRU              Reviewed;         332 AA.
AC   K0E3U5;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=2-oxoglutarate-dependent dioxygenase ecdK {ECO:0000303|PubMed:22998630};
DE            EC=1.14.-.- {ECO:0000305|PubMed:22998630};
DE   AltName: Full=Echinocandin B biosynthetic cluster protein K {ECO:0000303|PubMed:22998630};
GN   Name=ecdK {ECO:0000303|PubMed:22998630};
OS   Aspergillus rugulosus (Emericella rugulosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND BIOTECHNOLOGY.
RC   STRAIN=ATCC 58397 / NRRL 11440;
RX   PubMed=22998630; DOI=10.1021/ja307220z;
RA   Cacho R.A., Jiang W., Chooi Y.H., Walsh C.T., Tang Y.;
RT   "Identification and characterization of the echinocandin B biosynthetic
RT   gene cluster from Emericella rugulosa NRRL 11440.";
RL   J. Am. Chem. Soc. 134:16781-16790(2012).
CC   -!- FUNCTION: 2-oxoglutarate-dependent dioxygenase; part of the gene
CC       cluster that mediates the biosynthesis of echinocandin B, a fungal
CC       lipidated cyclic hexapeptide that acts as an antifungal agent
CC       (PubMed:22998630). Linoleoyl-AMP, produced by the fatty-acyl-AMP ligase
CC       ecdI, is transferred to the initiation carrier domain (T0) of ecdA
CC       (PubMed:22998630). The linoleoyl-S-phosphopantetheinyl-T0 is
CC       sequentially extended with L-ornithine, L-threonine, L-proline, L-
CC       homotyrosine, L-threonine, and 4R-methyl-L-proline to form the linear
CC       hexapeptide (PubMed:22998630). Thereafter, the terminal condensation
CC       (C7) performs macrocyclization of the NRPS product and the cyclic
CC       scaffold is released from ecdA (PubMed:22998630). All six of the amino
CC       acid residues are hydroxylated, including 4R,5R-dihydroxy-L-ornithine,
CC       4R-hydroxyl-L-proline, 3S,4S-dihydroxy-L-homotyrosine, and 3S-hydroxyl-
CC       4S-methyl-L-prolin (PubMed:22998630). In the pathway, all the
CC       hydroxylation reactions are proposed to occur following completion of
CC       the cyclic peptide, so the unhydroxylated precursor produced by ecdA
CC       will undergo six rounds of hydroxylation (PubMed:22998630). Five
CC       hydroxylase genes (ecdG, ecdH, ecdK, htyE and htyF) are embedded within
CC       the echinocandin B (ecd) and L-homotyrosine (hty) clusters
CC       (PubMed:22998630). {ECO:0000269|PubMed:22998630}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- PATHWAY: Antifungal biosynthesis. {ECO:0000305|PubMed:22998630}.
CC   -!- BIOTECHNOLOGY: Due to their effectiveness as antifungal agents,
CC       echinocandin derivatives can be used for the treatment of human
CC       invasive candidiasis (PubMed:22998630). {ECO:0000269|PubMed:22998630}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; JX421684; AFT91382.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0E3U5; -.
DR   SMR; K0E3U5; -.
DR   BioCyc; MetaCyc:MON-19240; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.330; -; 1.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..332
FT                   /note="2-oxoglutarate-dependent dioxygenase ecdK"
FT                   /id="PRO_0000443843"
FT   DOMAIN          178..294
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         206
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         208
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         266
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         285
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   332 AA;  37517 MW;  5EE5696FA5CB8AC9 CRC64;
     MSVLTLDFTK FHSGSEVERR AFGQALLDGF TTTGFVKLIN HGFSKEEMAD IFNWNQRFFD
     LPIDRKAAIR NDEGPKPQRG WSSLGAEKTG FLNPGGKLSL ARASNNDRQD AKEHFDIGPA
     EDEEFQNKWP EEQTLPGFQE TMNSYFDRSQ AITLELLEAL ALAMDVPKDT FVGLCHGHAS
     ELRLNHYPSI PVKTIEEGKT NRIWPHTDFG IITLLAQDDI GGLEIQDRNH PSDFLPVNRE
     DSTEFVVNIG DILERWTNGR LRAGLHQVTT PRSMQQKGNG TLPTRRSVAF FLKPHRQMSV
     ASISHFVPGN QSPRYEDMTA LAYQQLRTGI VY