CHYC_PENRW
ID CHYC_PENRW Reviewed; 258 AA.
AC B6HLP6;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Short-chain dehydrogenase chyC {ECO:0000305};
DE EC=1.1.1.- {ECO:0000269|PubMed:29196288};
DE AltName: Full=Chrysogine biosynthesis cluster protein C {ECO:0000303|PubMed:29196288};
GN Name=chyC {ECO:0000303|PubMed:29196288}; ORFNames=Pc21g12600;
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: Short-chain dehydrogenase; 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 -!- DISRUPTION PHENOTYPE: Accumulates 2-(2-aminopropanamido)benzoic acid,
CC 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 2-(2-((4-amino-1-
CC carboxy-4-oxobutyl)amino)propanamido)benzoic acid, but downstream
CC compounds are still produced in low amount (PubMed:29196288).
CC {ECO:0000269|PubMed:29196288}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AM920436; CAP96157.1; -; Genomic_DNA.
DR RefSeq; XP_002568287.1; XM_002568241.1.
DR AlphaFoldDB; B6HLP6; -.
DR SMR; B6HLP6; -.
DR STRING; 1108849.XP_002568287.1; -.
DR EnsemblFungi; CAP96157; CAP96157; PCH_Pc21g12600.
DR GeneID; 8306446; -.
DR KEGG; pcs:Pc21g12600; -.
DR VEuPathDB; FungiDB:PCH_Pc21g12600; -.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_44_5_1; -.
DR OMA; RNHTVYL; -.
DR OrthoDB; 1032903at2759; -.
DR BioCyc; PCHR:PC21G12600-MON; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..258
FT /note="Short-chain dehydrogenase chyC"
FT /id="PRO_0000443346"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 5..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 31..32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 77..79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 154..158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 185..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 258 AA; 28245 MW; B5D92960DE356B25 CRC64;
MARILITGST DGFGLEAARQ LVDRKHVVYL HARSQERAEE VKTKCPGAAG VLVADLTSVA
ETRKLAEEAN AIGTFDAIIL NAGLLYGPFR KTDYGVPAMP FVNVLAPYIL SCLLEQPKRL
IFIASILHKE AKTDLKDIFW LERGEKEFQD FPAYCDSKFH VMLLANAVAK RFKGTSVTSV
HPGYVATKLG GSGATDKMED GVETYVMLAE GDYDQSLTGV YFVPKKQIGE PLPETTQEDL
QETVVKACED ITGIKLPA
