ALT4_ALTSO
ID ALT4_ALTSO Reviewed; 482 AA.
AC Q5KTN0;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=FAD-linked oxidoreductase alt4 {ECO:0000303|PubMed:16356847};
DE EC=1.-.-.- {ECO:0000305|PubMed:16356847};
DE AltName: Full=Alternapyrone biosynthesis cluster protein 4 {ECO:0000303|PubMed:16356847};
GN Name=alt4 {ECO:0000303|PubMed:16356847};
OS Alternaria solani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Porri.
OX NCBI_TaxID=48100;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=584;
RX PubMed=16356847; DOI=10.1016/j.chembiol.2005.09.015;
RA Fujii I., Yoshida N., Shimomaki S., Oikawa H., Ebizuka Y.;
RT "An iterative type I polyketide synthase PKSN catalyzes synthesis of the
RT decaketide alternapyrone with regio-specific octa-methylation.";
RL Chem. Biol. 12:1301-1309(2005).
CC -!- FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of alternapyrone derivatives
CC (PubMed:16356847). Alternapyrone is a decaketide with octa-methylation
CC from methionine on every C2 unit except the third unit
CC (PubMed:16356847). All the domains in the polyketide synthase alt5 are
CC apparently involved in alternapyrone synthesis, that is, the 8 CMeT, 7
CC KR, 7 DH, and 4 ER reactions in the 9 KS-mediated condensation steps
CC required for alternapyrone synthesis (PubMed:16356847). the
CC alternapyrone produced by alt5 might be intensively modified by
CC cytochrome P450 monooxygenases alt1, alt2 and alt3 and FAD-dependent
CC oxidoreductase alt4 present in the alt gene cluster (PubMed:16356847).
CC {ECO:0000269|PubMed:16356847}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:16356847};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:16356847}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB120221; BAD83683.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5KTN0; -.
DR SMR; Q5KTN0; -.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..482
FT /note="FAD-linked oxidoreductase alt4"
FT /id="PRO_0000444927"
FT DOMAIN 53..211
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ SEQUENCE 482 AA; 55503 MW; ED1E9E68D4095BCC CRC64;
MDIQQGGNDL ISLAATIRTE LQQKLSSKAR IHLPFDEDRT EFDKANLRFT QYERPTYLAI
VDPVCEDDVI EAVKYARGKG IPFTPRGGHH SVTTTMGRFQ NGICINMRPL NQMRWYAEKR
HVTIGGGAIT DEFVRFVHDL GMEVTFGAGL GRLQGKYGFL NDNMVSCKLV LADGSTVIAS
KDSHPDLFWA LRGAGHNFGI ALEATFQVYP QAHGGIHHTW DLEYTLDQCD EVFRTLNSVY
ESMPAELAIF ILWLRQSSGR KHIILVNLVW SGPAAGADPY VQRFESLQPV LNSGRKSVPW
PELPFSTYKE INKLFCNPEI WLRGPYKMMG AACVERFDLK TTREFFESVK SLSEEWEDRG
WFSAMFECLP DQRVREISDD ATAFPWRAGS NHFLMLNATP KRMEDRKVFE DHLNYWKRRF
IETSGYGRLQ QYVSYGNGTS TMKDPPEALY GYEPWRLEKL RNLKQKYDPD NVFRWYQPLL
EP
