ID   CHYM_PENRW              Reviewed;         392 AA.
AC   B6HLP7;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Oxidoreductase chyM {ECO:0000303|PubMed:29196288};
DE            EC=1.-.-.- {ECO:0000269|PubMed:29196288};
DE   AltName: Full=Chrysogine biosynthesis cluster protein M {ECO:0000303|PubMed:29196288};
GN   Name=chyM {ECO:0000303|PubMed:29196288}; ORFNames=Pc21g12610;
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: Oxidoreductase; part of the gene cluster that mediates the
CC       biosynthesis of the yellow pigment chrysogine (PubMed:29196288). the
CC       NRPS chyA mediates the condensation of anthranilic acid and alanine
CC       into the intermediate 2-(2-aminopropanamido)benzoic acid
CC       (PubMed:29196288). The remainder of the pathway is highly branched
CC       yielding at least 13 chrysogine-related compounds (PubMed:29196288).
CC       The malonyl transferase chyE converts 2-(2-aminopropanamido)benzoic
CC       acid and 2-(2-aminopropanamido)benzamidine into 2-(2-(2-
CC       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   -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:29196288}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of N-
CC       pyruvoylanthranilamide ans downstream compounds and accumulates 2-(2-
CC       aminopropanamido)benzoic acid and 2-(2-((4-amino-1-carboxy-4-
CC       oxobutyl)amino)propanamido)benzoic acid (PubMed:29196288).
CC       {ECO:0000269|PubMed:29196288}.
CC   -!- SIMILARITY: Belongs to the asaB hydroxylase/desaturase family.
CC       {ECO:0000305}.
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DR   EMBL; AM920436; CAP96158.1; -; Genomic_DNA.
DR   RefSeq; XP_002568288.1; XM_002568242.1.
DR   AlphaFoldDB; B6HLP7; -.
DR   SMR; B6HLP7; -.
DR   EnsemblFungi; CAP96158; CAP96158; PCH_Pc21g12610.
DR   GeneID; 8306447; -.
DR   KEGG; pcs:Pc21g12610; -.
DR   VEuPathDB; FungiDB:PCH_Pc21g12610; -.
DR   eggNOG; ENOG502SKC4; Eukaryota.
DR   HOGENOM; CLU_042688_4_1_1; -.
DR   OMA; SIWRPLK; -.
DR   OrthoDB; 867824at2759; -.
DR   BioCyc; PCHR:PC21G12610-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c21.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR044053; AsaB-like.
DR   PANTHER; PTHR34598; PTHR34598; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..392
FT                   /note="Oxidoreductase chyM"
FT                   /id="PRO_0000443349"
SQ   SEQUENCE   392 AA;  43818 MW;  818B9FAF5272D16C CRC64;
     MGSITPSLHR GKFRYLTRGA KPAQSKEAYL LPPLSEFGDV LALPLVDMKP SLDLGDDSPY
     KLSVHGFTAR RHHSALHAAP YERRSWNDEH LLREIYFPEV QELVQKVTGC KKVVVSAAVL
     RNELYTEGDP ASATQTEQNG QDAVKKDMSE LFPPIVGNSP TDGICPAPKV HLDLTPKGAR
     YHIRKYHREV TSAAEQVIEA ENRLLESGVQ WDDLKDYYQG KESDDGVPRF ALFSIWRPLK
     PVHRDPLALA SCASFPESDY VPSEQLEPMD HQISAHLSRI IDPNAPKLSV ENERQVQGGT
     CQTYGYLAYG PRDKEQKAHG WHFVSEQQPS DVLIIQLFDN EMEAHARAPQ EGTNKMSNLG
     VGGAIHSAFE LEGQDIDAEA RESIEVRCAA FW