CHYE_PENRW
ID CHYE_PENRW Reviewed; 238 AA.
AC B6HLP3;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Glutamine amidotransferase-like protein chyE {ECO:0000305};
DE EC=3.-.-.- {ECO:0000269|PubMed:29196288};
DE AltName: Full=Chrysogine biosynthesis cluster protein E {ECO:0000303|PubMed:29196288};
DE AltName: Full=Malonyl transferase chyE {ECO:0000303|PubMed:29196288};
GN Name=chyE {ECO:0000303|PubMed:29196288}; ORFNames=Pc21g12570;
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: Glutamine amidotransferase-like protein; part of the gene
CC cluster that 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 -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:29196288}.
CC -!- DISRUPTION PHENOTYPE: Affects the production of 2-(2-(2-
CC carboxyacetamido)propanamido)benzoic acid and downstream compounds and
CC accumulates 2-(2-aminopropanamido)benzoic acid (PubMed:29196288).
CC {ECO:0000269|PubMed:29196288}.
CC -!- SIMILARITY: Belongs to the peptidase C26 family. {ECO:0000305}.
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DR EMBL; AM920436; CAP96154.1; -; Genomic_DNA.
DR RefSeq; XP_002568284.1; XM_002568238.1.
DR AlphaFoldDB; B6HLP3; -.
DR SMR; B6HLP3; -.
DR STRING; 1108849.XP_002568284.1; -.
DR EnsemblFungi; CAP96154; CAP96154; PCH_Pc21g12570.
DR GeneID; 8306443; -.
DR KEGG; pcs:Pc21g12570; -.
DR VEuPathDB; FungiDB:PCH_Pc21g12570; -.
DR eggNOG; KOG3179; Eukaryota.
DR HOGENOM; CLU_054974_0_0_1; -.
DR OMA; QGHPEMD; -.
DR OrthoDB; 1450344at2759; -.
DR BioCyc; PCHR:PC21G12570-MON; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01741; GATase1_1; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR044992; ChyE-like.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR PANTHER; PTHR42695; PTHR42695; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase; Hydrolase; Reference proteome.
FT CHAIN 1..238
FT /note="Glutamine amidotransferase-like protein chyE"
FT /id="PRO_0000443348"
FT DOMAIN 8..238
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 238 AA; 26279 MW; E0A5DD8AC33DB187 CRC64;
MDSVSNLKIA VLINTPPDET DFQSVVRECF REAFASIAPT GEVDFYDPVV ERKFPDASRY
DLVVLSGGKI DAACSDPWVL GVLDYVRITA RDLPKTKILA VCWGHQAVSR AFGGQVRPVP
AGEITAIEDI RLTDAGMKFF PFAATSGSYR AIELHSGEVY TPPPGFISLA ENQECFINDT
NNVLTFQAHP EISHELASKL ILEEDKKHSR NSSAEVLGID RPTEGLKLLE RVLQWLSE
