ECDG_ASPRU
ID ECDG_ASPRU Reviewed; 338 AA.
AC K0E678;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase ecdG {ECO:0000303|PubMed:22998630};
DE EC=1.14.-.- {ECO:0000305|PubMed:22998630};
DE AltName: Full=Echinocandin B biosynthetic cluster protein G {ECO:0000303|PubMed:22998630};
GN Name=ecdG {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; AFT91379.1; -; Genomic_DNA.
DR AlphaFoldDB; K0E678; -.
DR SMR; K0E678; -.
DR BioCyc; MetaCyc:MON-19238; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
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 PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..338
FT /note="2-oxoglutarate-dependent dioxygenase ecdG"
FT /id="PRO_0000443830"
FT DOMAIN 165..273
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 249
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 264
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 338 AA; 37905 MW; 63189488EA3D2A60 CRC64;
MASISYDGLL RGAAKDIQTL TEASLVHGYF NLELDCPEGK QLREDVLFLE SFTKEIFDTP
SPQKTIYDFK KLGRFRTTGF KPLGIEEGAK GKSDGFEMFM LPQNELLLPS HQDKLQSPSA
VFSHRATLTR CMSNYDAASQ LILRRITESL NLDNALLAAH NPSEPSVTNL GFLRYPPQPA
TSENCGHIAH TDVGTLTILA ATQRGLQVIN SETQDWTFVD PHPQNEFLLV QFGDCLKFLS
GGRVVPSIHR VIPSDNPEER EGTKYTLAYF VRPNEEAVIK DDRGEEWVYG DYHCRKFGAF
ARPLKEGDRD RMPDRPVGEY DMINIRKFKG LADGVSAA
