CHYH_PENRW
ID CHYH_PENRW Reviewed; 500 AA.
AC B6HLP5;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=FAD-linked oxidoreductase chyH {ECO:0000303|PubMed:29196288};
DE EC=1.-.-.- {ECO:0000269|PubMed:29196288};
DE AltName: Full=Chrysogine biosynthesis cluster protein H {ECO:0000303|PubMed:29196288};
DE Flags: Precursor;
GN Name=chyH {ECO:0000303|PubMed:29196288}; ORFNames=Pc21g12590;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29196288; DOI=10.1128/aem.02246-17;
RA Viggiano A., Salo O., Ali H., Szymanski W., Lankhorst P.P., Nygaard Y.,
RA Bovenberg R.A.L., Driessen A.J.M.;
RT "Elucidation of the biosynthetic pathway for the production of the pigment
RT chrysogine by Penicillium chrysogenum.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
CC -!- FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of the yellow pigment chrysogine
CC (PubMed:29196288). the NRPS chyA mediates the condensation of
CC anthranilic acid and alanine into the intermediate 2-(2-
CC aminopropanamido)benzoic acid (PubMed:29196288). The remainder of the
CC pathway is highly branched yielding at least 13 chrysogine-related
CC compounds (PubMed:29196288). The malonyl transferase chyE converts 2-
CC (2-aminopropanamido)benzoic acid and 2-(2-aminopropanamido)benzamidine
CC into 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 3-((1-((2-
CC carbamoylphenyl)amino)-1-oxopropan-2-yl)amino)-3-oxopropanoic acid,
CC respectively (PubMed:29196288). ChyD is an amidase, being responsible
CC for the amidation of the carboxylic acid moiety of 2-(2-
CC aminopropanamido)benzoic acid, 2-(2-(2-
CC carboxyacetamido)propanamido)benzoic acid and 2-(2-((4-amino-1-carboxy-
CC 4-oxobutyl)amino)propanamido)benzoic acid (PubMed:29196288). ChyC is
CC involved in the same reactions as ChyD, but plays a more minor role in
CC the amidation reactions compared to chyD (PubMed:29196288). The
CC oxidoreductases chyH and chyM are involved in oxidation reactions that
CC form N-pyruvoylanthranilamide from 2-(2-aminopropanamido)benzamidine
CC and (1-((2-carbamoylphenyl)amino)-1-oxopropan-2-yl)glutamine,
CC respectively (PubMed:29196288). N-pyruvoylanthranilamide is further
CC converted via two further branches in the pathway, yielding chrysogine
CC and additional chrysogine-related coumpounds (PubMed:29196288).
CC Chrysogine is likely formed by a spontaneous ring closure from N-
CC pyruvoylanthranilamide (PubMed:29196288).
CC {ECO:0000269|PubMed:29196288}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q5BEJ5};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:29196288}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of N-
CC pyruvoylanthranilamide ans downstream compounds (PubMed:29196288).
CC {ECO:0000269|PubMed:29196288}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AM920436; CAP96156.1; -; Genomic_DNA.
DR RefSeq; XP_002568286.1; XM_002568240.1.
DR AlphaFoldDB; B6HLP5; -.
DR SMR; B6HLP5; -.
DR EnsemblFungi; CAP96156; CAP96156; PCH_Pc21g12590.
DR GeneID; 8306445; -.
DR KEGG; pcs:Pc21g12590; -.
DR VEuPathDB; FungiDB:PCH_Pc21g12590; -.
DR eggNOG; ENOG502SJ3M; Eukaryota.
DR HOGENOM; CLU_018354_0_1_1; -.
DR OMA; PLISYMP; -.
DR OrthoDB; 350817at2759; -.
DR BioCyc; PCHR:PC21G12590-MON; -.
DR Proteomes; UP000000724; Contig Pc00c21.
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; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..500
FT /note="FAD-linked oxidoreductase chyH"
FT /id="PRO_5002845783"
FT DOMAIN 65..235
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 500 AA; 54521 MW; D997F90665B7A823 CRC64;
MRLQAVTAVA AWAVASACQS LPGTRTIWSR DADYKELSEK LSPSAKAYYP GSDEFEKANT
RWSNLEVPTV NIVIVPGNEN DVVETVKFAN KKGLPFLAWN SAHGAMTTLG QMDSGIEIYL
DQLSGVEIAE DGKTVTIAGG TKSKLVTDTL WAAGKQTVTG ACECVGYIGP ALGGGHGWLQ
GRHGTIGDQF ESANIVLANG TLTSIDSSSD LWWAIKGAGH NFGIVTSVTS KTYDIEHKDW
AIEILTFSGS KVVELYEAVN THLLKNGTQP TDLINWSYWV NVPSADANNP VIQILIIQEG
VNTVDSAYTT PFHSLSPITK EAHSGSYTDL AKWVGITTTD EPCQKTGAMN PRFPIYLETY
NPQAQKKAFE LFSDAIRGDS IFNGSLFAFD GYSTQGVRAI DEKSTAFAFR NQNVLTAPLI
SYMPDGPELD EKVAKLGNQL RQILHEGTGR EHIPAYVNYA NGDEGPEQWY GSESWRQSKL
QSLKKKYDPN GMFSFYGPIA
