ECDH_ASPRU
ID ECDH_ASPRU Reviewed; 503 AA.
AC K0E684;
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=Cytochrome P450 monooxygenase ecdH {ECO:0000303|PubMed:22998630};
DE EC=1.-.-.- {ECO:0000305|PubMed:22998630};
DE AltName: Full=Echinocandin B biosynthetic cluster protein H {ECO:0000303|PubMed:22998630};
GN Name=ecdH {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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of echinocandin B, a fungal lipidated cyclic
CC hexapeptide that acts as an antifungal agent (PubMed:22998630).
CC Linoleoyl-AMP, produced by the fatty-acyl-AMP ligase ecdI, is
CC 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=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Antifungal biosynthesis. {ECO:0000305|PubMed:22998630}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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 cytochrome P450 family. {ECO:0000305}.
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DR EMBL; JX421684; AFT91389.1; -; Genomic_DNA.
DR AlphaFoldDB; K0E684; -.
DR SMR; K0E684; -.
DR BioCyc; MetaCyc:MON-19239; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..503
FT /note="Cytochrome P450 monooxygenase ecdH"
FT /id="PRO_0000443831"
FT TRANSMEM 8..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 449
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 503 AA; 56635 MW; ECBB1A4FD90A23A9 CRC64;
MEFPLYTTTL LCGVISSTLL LLLLNKLTTW EHIVPSKVPW IDRRSEPFGY LRAKCRSFFN
MKENITEAYY AFNKEGRAAA LAIAFGRPQI ILPPKYIRWI IDQPESVLSI DPIHNEFHAF
VRDGLVGDHL VQEVLRRELA GHLAHLTREM NEEIADSVES VLGVSKEWAT VPLRDSMRII
IARISNRLFV GKELCRNEDY IRNAVGLGMA VMPQTLVQDL LPQLLKGPLS FATKLFTRIT
LAGLSGHLSP VVRQRIQDVQ TAEKDQLPLE LLTWMAQRAL QRGESATSIE EKLIARIAMA
NLASIETTTN TITKCMEDMT ALSNETGGYL ELMRQEAHTV LEACNYSPIK ADLEKLVHIE
NALKESLRLA VVFPGLIRQV TSRTGVTLDD GTHLPHGARI SVAAYAIHRD DANWTDAARY
DPSRHEKASL PMSRGSEQLL SFGLGKRACP GRFFVTDELK LLFAHILTKY EFKVIKPPVT
KVGLLKELTM RGPQEQLVIR RVK
