ID CHYA_PENRW Reviewed; 2382 AA.
AC B6HLP9;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Nonribosomal peptide synthase chyA {ECO:0000303|PubMed:29196288};
DE Short=NRPS chyA {ECO:0000303|PubMed:29196288};
DE EC=2.3.2.- {ECO:0000269|PubMed:29196288};
DE AltName: Full=Chrysogine biosynthesis cluster protein A {ECO:0000303|PubMed:29196288};
GN Name=chyA {ECO:0000303|PubMed:29196288}; ORFNames=Pc21g12630;
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, DOMAIN, 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: Nonribosomal peptide synthase; 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 -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:29196288}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module. Each module is responsible for the recognition (via the A
CC domain) and incorporation of a single amino acid into the growing
CC peptide product. Thus, an NRP synthetase is generally composed of one
CC or more modules and can terminate in a thioesterase domain (TE) that
CC releases the newly synthesized peptide from the enzyme. Occasionally,
CC epimerase (E) domains (responsible for L- to D-amino acid conversion)
CC are present within the NRP synthetase. ChyA has the following
CC architecture: A-T-C-A-T-C. {ECO:0000305|PubMed:29196288}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of chrysogine and 13 other
CC chrysogine-related compounds (PubMed:29196288).
CC {ECO:0000269|PubMed:29196288}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; AM920436; CAP96160.1; -; Genomic_DNA.
DR RefSeq; XP_002568290.1; XM_002568244.1.
DR AlphaFoldDB; B6HLP9; -.
DR SMR; B6HLP9; -.
DR STRING; 500485.B6HLP9; -.
DR GeneID; 8306449; -.
DR KEGG; pcs:Pc21g12630; -.
DR VEuPathDB; FungiDB:PCH_Pc21g12630; -.
DR eggNOG; KOG1176; Eukaryota.
DR eggNOG; KOG1178; Eukaryota.
DR HOGENOM; CLU_000022_60_2_1; -.
DR OMA; FQIAPEM; -.
DR OrthoDB; 2209130at2759; -.
DR BioCyc; PCHR:PC21G12630-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c21.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd05918; A_NRPS_SidN3_like; 2.
DR CDD; cd19542; CT_NRPS-like; 1.
DR CDD; cd19545; FUM14_C_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..2382
FT /note="Nonribosomal peptide synthase chyA"
FT /id="PRO_0000443345"
FT DOMAIN 745..821
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1833..1909
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 204..607
FT /note="Adenylation 1"
FT /evidence="ECO:0000255"
FT REGION 857..1269
FT /note="Condensation 1"
FT /evidence="ECO:0000255"
FT REGION 1294..1687
FT /note="Adenylation 2"
FT /evidence="ECO:0000255"
FT REGION 1967..2373
FT /note="Condensation 2"
FT /evidence="ECO:0000255"
FT MOD_RES 782
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1870
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2382 AA; 260769 MW; 582DAC279F7F88E7 CRC64;
MAAPSISPLF APQMGVQRDF QDSEMQIATV NFPCTGQSNT SLANWLQQEE KSHLQLLQAA
WSISLRSYTG SNDVLFSCLN TKDTAALGAN SVVYVDEGNE DKYGSARRGN LREFDLAICF
SKQNEANCPV IGIHHKPSVI STDFATMIAA TVAKAIEEIV LHVDSLIASL DICSDADINC
ISRWNSPSDD GIPSAQCIHH IISQKCATQP ESIAVSAWDG RLTYAELDGL SSSLAIRLQH
LGVCQEIFVP LIFDKSKWAV IALLSVLKAG GAYFFLNPSN PIQYNLGLCS SLSPEVALCS
PRHSTLAKSF AGTAIPVGEE HCELPESLPV DEKTPPCTAE TTPSNAMYIT FTSGTTGVPK
GITTEHSAFY SMAMANGKAL QVGPATRMLQ FASYTFDVSN RDMLITLMFG GCICIPSELD
RLNDLSGFIN RQSVNLASLT PSLASTLNPA LCPSLQGLVL GGESMNDSHI SAWANHVRLF
NAYGVSESAG IAALASDIQA DYSPGNIGFG SGSTLWVVTI DQPDKLAPIG ALGEMVIEGP
SVARGYLGDK KRTEEQFTST SKWKNRIRAQ LSESRSSKRA FHTGDLVRYN LDGSLNFLGR
KDHQVKIHGQ RLELTAIEHH IAACLEVAES GFLHVAVVTA KNEGNGSVKL LAFLGLYTSR
GSDSPSQLVS KKLEDVEALK VALRQHLLLC LPAFMVPVDF IFVQHMPLTT SGKINRLLLQ
EAAGHALLDD QKRNIDTSDL NGNQTPTTQN QRILIQSWAK ALGIKSESIM RNDCFFRRGG
DSIAAIKMAA SLRQQELIIS VSDVFKFSTF SDMASVLVKD HRPLQTAMLA PFSLIDNSQT
VLDAVMEELG TGIDQIEDVY PCTHMQQGLI ALTAQQPHSY IGRYTWQLAE MLDVEKFKNA
WESAWLHNPI LRTRIVQIPD GVFQVVVKTD MPWNTVTDIS RGGDGKELRE IDISNGPLIQ
FYLSKESFRL DIHHSLFDEW SLGLIMGQVE RAYAGGGLRM QPFSPFVQHL LHERDTSLED
FWRQEFSGLQ AEHFPAIASR PLSVEHPTEK VVLEHSVQLE TGFSTKYTIS SIVRLAWAIV
LWHQTGSEDV VFGATVSGRN ANIDGIDQLS GPTLATLPVR IKLAASQPIH EGLSQVQGQF
VNMMVHEQAG LPRIRQVGRE AAEACNFQNL LVVQPYEEQT ESHMFKASAN SASSSENAKS
FASYPMVLIC RPEKSGISMK AAFDPAILTP AAGHSILKQM SHVIQQLVTS DSTCIAAVSL
VPPEDMATLR QWNHSLPNGV NTCIHARIQE LCIGQPDTLA IHSQNLDLTY GQLDNYSDQF
AQNLIGSGVK QGDFVPLFLE RSPWVPVIML AVLKTGAAFV LLDLSHPMQR LRTMCSMIDA
RIVVTSKEHA DRSGNLLLPV IIFDPEAHAQ NVSKQATAPE LKPLTAVTTP DAPACVVFSS
GSTGLPKGIV LPHSALTTSA AVMREYGMLG PKSRVFHFAS FAFDISIGEI LFTLAAGACV
CVPHEEERKG NPAKAAGDLK VTWALLTPSV INLFDPSDVP TLEVLGSAGE PLTPQIVDTW
AHRVKLYGMY APAECTVISH IGRILPDTHH SNIGKSHGGV SWVVDPSDHN RLVPIGTVGE
LIVEGPTVSS GYLNDPAKTN EVFITSPSWL DEVRSHSGKM YKTGDLVRQT SEGSLEFVGR
KDDQVKLHGQ RLEVGEVEHC ITSSCTAIKT ATVECIKIRE QNSRVSLVAF ICPQTDEDWG
QSLNDPSSEV GDLELISPPR DQFYSMIESL ETSLRELLPA YMVPSFFVPL ADVPLSLSGK
VNRRLLRDQS TSWPMKRLGL YQLRRKSIPA EEVPVSIHGR KVQEIVGQAL NLDPKSIPMN
SNFFGLGGDS ISAMQVSMLA RRRGIRLTVA DIFTQQTLSG LSLKCATENG DASQASKSRS
LGRELPGSNI KSLHRCEIPR DKLPRQLPQE IADNIVEAMP ATEFQTMTLH NFYSRYLWIS
LPERVNQEHL LNACDQLVQK HSVLRTVFYT NDDKSVVQLT LRKVPVNFVH YSNIENLEKH
CADDSLAMGV PINSVPGFEV QLVTLRDSGM YLILRLPHAQ FDGVSLDIIC SDLSAAYSGD
SLPPCAQFSD HIRHVWEKRI PESYNAWREV LGNVPMTSLN NKYLRNWGSA SEMGSPNMGT
DPDQPKVVTA MAETLPISPP PNITLATLVK LAWAITLSRL FTSIEEDDGA SDDVVFGQVV
HGRGLGISHE DRIVGPCLNI IPVRVHLPPR SNKLDLLGQV QQQHIQTMSV ENLELGEITR
NCTSWKAGTK FGSFIRFQNF TNNDDSTCSF DGSACETGLY SLPNRPSNTA NVLVVPHGPT
LSITMTISNQ VLDRGSADFV AGYFSDVIES LASEETVCEY LE
//
