ORYD_ASPOR
ID ORYD_ASPOR Reviewed; 240 AA.
AC P9WEZ5; Q2TXE9;
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=Histidinol dehydrogenase homolog oryD {ECO:0000303|PubMed:30104550};
DE EC=1.1.-.- {ECO:0000305|PubMed:30104550};
DE AltName: Full=Oryzines biosynthesis cluster protein D {ECO:0000303|PubMed:30104550};
GN Name=oryD {ECO:0000303|PubMed:30104550}; ORFNames=AO090010000172;
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: Histidinol dehydrogenase homolog; part of the gene cluster
CC that mediates the biosynthesis of oryzines, natural products with an
CC unusual maleidride backbone (PubMed:30104550). The two subunits of the
CC fungal fatty acid synthase oryfasA and oryfasB probably form octenoic
CC acid (Probable). This fatty acid is most likely activated by the acyl-
CC CoA ligase oryP to give octenyl-CoA before the citrate synthase-like
CC protein oryE catalyzes condensation with oxaloacetate to form
CC tricarboxylic acid (Probable). The next steps of the pathways are
CC conjectural, but a favorite possible route has been proposed, beginning
CC with decarboxylation and concomitant dehydration by the decarboxylase
CC oryM, followed by tautomerization, which may lead to the production of
CC a 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P06988};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P06988};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30104550}.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE66074.1; Type=Erroneous gene model prediction; Note=The predicted gene AO090010000172 has been split into 2 genes: oryC and oryD.; Evidence={ECO:0000305|PubMed:30104550};
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DR EMBL; AP007175; BAE66074.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P9WEZ5; -.
DR SMR; P9WEZ5; -.
DR EnsemblFungi; BAE66074; BAE66074; AO090010000172.
DR Proteomes; UP000006564; Chromosome 8.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR012131; Hstdl_DH.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 3: Inferred from homology;
KW Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..240
FT /note="Histidinol dehydrogenase homolog oryD"
FT /id="PRO_0000450490"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988"
SQ SEQUENCE 240 AA; 26079 MW; 3C899D4BF2CAC9A4 CRC64;
MPVGTEAIRK VDFLAGTGNR FVAEGKRQLF GEVGIDLFAG PTESLVLADE TADPFTVATD
LISQAGHGPD TPAVLITTCP KVGRETIEIV NKLLSATDLS TPDVAKVSWD AFGEVIIVDT
LKELWELGDH YASEQVQVFT KDPRDALDKM SNYGALFLGE NTCVSYGDKV IGKNHVLLTR
TTARYTGGLW VGKYLKTCTY QEVTSPESSG KLGRLCGRAA RPERFEAHAR SGDLQANRHM
