ORYP_ASPOR
ID ORYP_ASPOR Reviewed; 546 AA.
AC P9WEZ0;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Acyl-CoA ligase oryP {ECO:0000303|PubMed:30104550};
DE EC=6.2.-.- {ECO:0000305|PubMed:30104550};
DE AltName: Full=Oryzines biosynthesis cluster protein P {ECO:0000303|PubMed:30104550};
GN Name=oryP {ECO:0000303|PubMed:30104550};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=30104550; DOI=10.3390/jof4030096;
RA Wasil Z., Kuhnert E., Simpson T.J., Cox R.J.;
RT "Oryzines A & B, maleidride congeners from Aspergillus oryzae and their
RT putative biosynthesis.";
RL J. Fungi 4:0-0(2018).
CC -!- FUNCTION: Acyl-CoA ligase; part of the gene cluster that mediates the
CC biosynthesis of oryzines, natural products with an unusual maleidride
CC backbone (PubMed:30104550). The two subunits of the fungal fatty acid
CC synthase oryfasA and oryfasB probably form octenoic acid (Probable).
CC This fatty acid is most likely activated by the acyl-CoA ligase oryP to
CC give octenyl-CoA before the citrate synthase-like protein oryE
CC catalyzes condensation with oxaloacetate to form tricarboxylic acid
CC (Probable). The next steps of the pathways are conjectural, but a
CC favorite possible route has been proposed, beginning with
CC decarboxylation and concomitant dehydration by the decarboxylase oryM,
CC followed by tautomerization, which may lead to the production of a
CC diene intermediate (Probable). Reduction of this diene intermediate
CC could give the known metabolite piliformic acid (Probable). On the
CC pathway to oryzine B and oryzine A, however, hydroxylation of the diene
CC by the alpha-ketoglutarate-dependent dioxygenase oryG and lactonisation
CC by the lactonohydrolases oryH or oryL could give oryzine B directly
CC (Probable). Finally, enoyl reduction by the dehydrogenase oryD would
CC then convert oryzine B into oryzine A (Probable).
CC {ECO:0000269|PubMed:30104550, ECO:0000305|PubMed:30104550}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30104550}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AP007175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P9WEZ0; -.
DR SMR; P9WEZ0; -.
DR Proteomes; UP000006564; Chromosome 8.
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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..546
FT /note="Acyl-CoA ligase oryP"
FT /id="PRO_0000450496"
FT BINDING 166..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 300..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 412..414
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 482..484
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ SEQUENCE 546 AA; 60919 MW; E95AFACB53D8F129 CRC64;
MILPADPIFS QLLLIARNSP DEVVIDDRNL HVQAGYSHLL HDAVQLAQQL RDSLSQGPST
VGSAFIGILA PTSYESTVAS LAILAVGAAG ASLEELAYTL KQCSATCVLV GSQHQQTKLA
TQLQEQTGIL KLAIPVLSPG RPPIESYTLD EDSIPSDDLP AFLFFTSGTT GAPKGVLHAR
RYLYAKFSVQ QSELTDELCL IYDSICWSTC FISVLLHILR GERVELHELD ARYDLIWDRF
RDCEITKIHF SPTSWYTMMK VFQERISKLP EPSVQAYIRG AQYIRTPITL GGILPVPVKQ
FWLNLRGGRP IKVIYGSTEA GLLTVADPEA SASEEASIGS PAPNVTVKLS DGDSGELLVK
APTLLLQYLN SPELTASCFD SEGFYKTGDL VERQGKNFIF RGRYKADFFK FWDHKIPRLH
VESCLSSLPY IEEAHILPVA DARCDNRVAA LVRLRQDHTC VTLQSIRKDL STMLPVYQMP
TLLRILGKGD EVPRTFSEKV AMKKTVERFF PRWNNDHFMD DSIEVLGIKE ILQFDTTGPL
ELVELW
