CHYD_PENRW
ID CHYD_PENRW Reviewed; 672 AA.
AC B6HLP8;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Amidase chyE {ECO:0000305};
DE EC=3.-.-.- {ECO:0000269|PubMed:29196288};
DE AltName: Full=Chrysogine biosynthesis cluster protein D {ECO:0000303|PubMed:29196288};
GN Name=chyD {ECO:0000303|PubMed:29196288}; ORFNames=Pc21g12620;
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: Amidase; 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: Leads to a depletion of most chrysogine-related
CC metabolites with accumulation of only 2-(2-aminopropanamido)benzoic
CC acid, 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 2-(2-((4-
CC amino-1-carboxy-4-oxobutyl)amino)propanamido)benzoic acid
CC (PubMed:29196288). {ECO:0000269|PubMed:29196288}.
CC -!- SIMILARITY: Belongs to the asparagine synthetase family. {ECO:0000305}.
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DR EMBL; AM920436; CAP96159.1; -; Genomic_DNA.
DR RefSeq; XP_002568289.1; XM_002568243.1.
DR AlphaFoldDB; B6HLP8; -.
DR SMR; B6HLP8; -.
DR STRING; 1108849.XP_002568289.1; -.
DR EnsemblFungi; CAP96159; CAP96159; PCH_Pc21g12620.
DR GeneID; 8306448; -.
DR KEGG; pcs:Pc21g12620; -.
DR VEuPathDB; FungiDB:PCH_Pc21g12620; -.
DR eggNOG; KOG0571; Eukaryota.
DR HOGENOM; CLU_014658_1_0_1; -.
DR OMA; LYRPKMG; -.
DR OrthoDB; 1142572at2759; -.
DR BioCyc; PCHR:PC21G12620-MON; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006529; P:asparagine biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01991; Asn_Synthase_B_C; 1.
DR CDD; cd00712; AsnB; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR006426; Asn_synth_AEB.
DR InterPro; IPR001962; Asn_synthase.
DR InterPro; IPR033738; AsnB_N.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00733; Asn_synthase; 1.
DR Pfam; PF13537; GATase_7; 1.
DR PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01536; asn_synth_AEB; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..672
FT /note="Amidase chyE"
FT /id="PRO_0000443347"
FT DOMAIN 2..219
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 250..639
FT /note="Asparagine synthetase"
FT /evidence="ECO:0000255"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
SQ SEQUENCE 672 AA; 75951 MW; 1CF8ADA9B46E840C CRC64;
MCGISAFLCH PGKASSNEQA NAQTRHVVDE LEHSLDLVGH RGPDARGHID ILTIGLGHVR
LSIIDLSLSG NQPFHDQDNS IHAVVNGELY DHEYYRDQLA SEFQFVGTSD CEIVIALYKH
YGLSFISHLR GEFAFVLWDA NRQLLIAARD RYGIKSLYYT VVQGKLLVAT EIKSFLAFGL
QPEWCVRTLR DQSWRIESRT FFKGVHRVLP GHYLISRPNE REEQKPYWDL EYPDKLSHDA
RSEEEIVQGV RKRLLEAVKI RLKADVPVAI YLSGGIDSSS VAGMVADLMR QGTKLGNESN
SVPSNMKCFT VQFDEDSGAD ESAIARRTAN WLGVDIHLVK MDEEALASRF EDAVWHSEIP
LPDLNGMGRL ALAEAVHAQG IKVVITGEGS DEHFAGYDAF RADLLSEPDH SWPALQLPET
DRQKALAMAA KQVKYGIFGE YSETVPDATK RMLNHSHVTS TIARVGSLPF SNWTTSYGND
LPETSLIEGF DGRVRDNITK RWHPLHTAQY LFTKSFMPHF ILRYNGDNID MVNQVESRCP
FLDHHLTEYV NNVPPSLKLK YLPEEKSFRE KYILREAVKP YVTDEIYNIS KKAYMGPRKF
WPGGPLHRKI KQLVTKENVE SLGFVDWNAT QEAVEKAFTK QDPMGLRRTI TVAQFIVLGK
RFGVKPAGAL PN
