ECDI_ASPRU
ID ECDI_ASPRU Reviewed; 559 AA.
AC K0E2F3;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Fatty-acyl-AMP ligase ecdI {ECO:0000303|PubMed:22998630};
DE EC=6.2.1.- {ECO:0000305|PubMed:22998630};
DE AltName: Full=Echinocandin B biosynthetic cluster protein I {ECO:0000303|PubMed:22998630};
GN Name=ecdI {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: Fatty-acyl-AMP ligase; part of the gene cluster that mediates
CC 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 -!- PATHWAY: Antifungal biosynthesis. {ECO:0000269|PubMed:22998630}.
CC -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC the substrate recognition, and are sufficient to confer the substrate
CC specificity. {ECO:0000250|UniProtKB:Q42524}.
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 ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX421684; AFT91380.1; -; Genomic_DNA.
DR AlphaFoldDB; K0E2F3; -.
DR SMR; K0E2F3; -.
DR BioCyc; MetaCyc:MON-19232; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Ligase; Nucleotide-binding.
FT CHAIN 1..559
FT /note="Fatty-acyl-AMP ligase ecdI"
FT /id="PRO_0000443832"
FT REGION 278..348
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 349..411
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 207..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 348..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 559 AA; 60785 MW; 5C497D7FC2A205C1 CRC64;
MVFTSPAWCS QLASTIPETK LVGDFVLEGN GTESGDKPLL VCAETGKSYN IGVLENRVDL
LARSLMRVFG WSPNEGAPED KVVGICSFNA MDFVPLSWAI HRVGGICLVL HPTSSAAELQ
SLMRQASCKA LFTCRDLLPT CRAVLEALKL ESSRLFLLEL PADEQTTQAQ PVSVSQLIAD
GESLPPVDKV ALQDGESKHR VAYLCPTSGT SGYQKLAQIT HKNITSNILQ AVTLDGFATR
TAPEVALGIL PLSHAYGLVA FSTLLYRRDT VILHARFDMP AALRSIQQYR IQRLYVVPAI
VAALVNNPIL FKLADLSSVQ SLIVGSAPLS KELVGALKRV RPEWDLLAGY GLTEAAVFVS
CTSKHSIFPG SVGSLLPHVE ARLVGDDGAE IQDYDVAGEL FLRSPSIMKG YLVDDATDSG
AFDADGWLIT GDVASFRKGP DGEEHLFIVD RKKDIMKVKG IQVAPAEIET RLLSHPAVDE
AAVFGINDAE AGERPFAFVV RSKMVNVDLD EKALRQSIHS HIQETLSEPF WLRDNIKFVE
SIPKGHSGKA LKFKLKELI
