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POXH_PENO1
ID   POXH_PENO1              Reviewed;         385 AA.
AC   S7ZK59;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Trans-enoyl reductase poxH {ECO:0000303|PubMed:28365998};
DE            EC=1.-.-.- {ECO:0000305|PubMed:28365998};
DE   AltName: Full=Oxaleimides biosynthesis cluster protein H {ECO:0000303|PubMed:28365998};
GN   Name=poxH {ECO:0000303|PubMed:28365998}; ORFNames=PDE_04020;
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302;
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
RN   [2]
RP   FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=28365998; DOI=10.1021/jacs.7b02432;
RA   Sato M., Dander J.E., Sato C., Hung Y.S., Gao S.S., Tang M.C., Hang L.,
RA   Winter J.M., Garg N.K., Watanabe K., Tang Y.;
RT   "Collaborative Biosynthesis of Maleimide- and Succinimide-Containing
RT   Natural Products by Fungal Polyketide Megasynthases.";
RL   J. Am. Chem. Soc. 139:5317-5320(2017).
RN   [3]
RP   FUNCTION.
RX   PubMed=32039410; DOI=10.1039/c9cc09590j;
RA   Hantke V., Skellam E.J., Cox R.J.;
RT   "Evidence for enzyme catalysed intramolecular [4+2] Diels-Alder cyclization
RT   during the biosynthesis of pyrichalasin H.";
RL   Chem. Commun. (Camb.) 56:2925-2928(2020).
CC   -!- FUNCTION: Trans-enoyl reductase; part of the gene cluster that mediates
CC       the biosynthesis of oxaleimides, cytotoxic compounds containing an
CC       unusual disubstituted succinimide moiety (PubMed:28365998). The first
CC       step of the pathway is provided by the HR-PKS poxF that serves in a new
CC       mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing
CC       the olefin containing amino acid substrate via the synthesis of an ACP-
CC       bound dec-4-enoate (PubMed:28365998). The cytochrome P450 monooxygenase
CC       poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound
CC       2-hydroxydec-4-enoyl-ACP thioester, which may be prone to spontaneous
CC       hydrolysis to yield 2-hydroxydec-4-enoic acid due to increased
CC       electrophilicity of the carbonyl (PubMed:28365998). 2-hydroxydec-4-
CC       enoic acid can then be further oxidized by poxM to yield the alpha-
CC       ketoacid 2-oxodec-4-enoicacid, which is reductively aminated by the
CC       aminotransferase poxL to yield (S,E)-2-aminodec-4-enoic acid
CC       (PubMed:28365998). The Hybrid PKS-NRPS synthetase poxE then performs
CC       condensation between the octaketide product of its PKS modules and the
CC       amino group of (S,E)-2-aminodec-4-enoic acid which is activated and
CC       incorporated by the adenylation domain (PubMed:28365998). The resulting
CC       aminoacyl product can be cyclized by the Diels-Alderase PoxQ and
CC       reductively released by the reductive (R) domain of poxE to yield an
CC       aldehyde intermediate (PubMed:28365998) (Probable). The released
CC       aldehyde is then substrate for a Knoevenagel condensation by the
CC       hydrolyase poxO followed by an oxidation at the 5-position of the
CC       pyrrolidone ring (PubMed:28365998). The presence of the olefin from the
CC       amino acid building block allows for migration of the substituted allyl
CC       group to occur (PubMed:28365998). This allylic transposition reaction
CC       takes place in a conjugate addition, semipinacol-like fashion to yield
CC       a succinimide intermediate (PubMed:28365998). Iterative two-electron
CC       oxidations of the C7 methyl of the succinimide intermediate to the
CC       carboxylic acid can be catalyzed by one of two remaining cytochrome
CC       P450 monooxygenasess poxC or poxD to yield oxaleimide A
CC       (PubMed:28365998). Subsequent oxidation yields the maleimide scaffold
CC       oxaleimide I (PubMed:28365998). Both oxaleimide A and oxaleimide I can
CC       undergo oxidative modifications in the decalin ring to yield the series
CC       of products oxaleimides B to H (PubMed:28365998).
CC       {ECO:0000269|PubMed:28365998, ECO:0000305|PubMed:32039410}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:28365998}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9Y7D0}.
CC   -!- INDUCTION: Expression is positively regulated by the oxaleimides
CC       biosynthesis cluster-specific transcription factor poxB.
CC       {ECO:0000269|PubMed:28365998}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; KB644411; EPS29071.1; -; Genomic_DNA.
DR   SMR; S7ZK59; -.
DR   STRING; 933388.S7ZK59; -.
DR   EnsemblFungi; EPS29071; EPS29071; PDE_04020.
DR   eggNOG; KOG1198; Eukaryota.
DR   HOGENOM; CLU_026673_3_3_1; -.
DR   OrthoDB; 727365at2759; -.
DR   PhylomeDB; S7ZK59; -.
DR   Proteomes; UP000019376; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NADP; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Trans-enoyl reductase poxH"
FT                   /id="PRO_0000453758"
FT   BINDING         64..67
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         156..163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         199..202
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         223..226
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         241
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         289..290
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
FT   BINDING         309..313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         372..373
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y7D0"
SQ   SEQUENCE   385 AA;  41833 MW;  176794C3FA9B5F66 CRC64;
     MSTTTTMRAW TYMQSGLPSQ TIVLDDEAPS PSAAELGPDE LLIAVNYVAM NSGFTTLMRS
     LPPQPYSLPH IYNRQKRLGV PEFEFSGRIL AVGSAIPSTR PDLQPSTLVL GCCAAKRVFI
     EGKGALAERV IAPAAQLIPL RPLSTVTTQD DESPGPDPAA PPISLLEASG LSACGCTAVQ
     VLDLTKLVAG DKLFVNGGST SVGMLIIQVA RQVLGQTGTI IASGTDATLI RSVGADDVID
     YTAQRPLHEF LRTHHAGRPF DAIIDCVGVA ELYTHCEPYL APGKLFINLG AMTAKPTFWG
     LLSFVWNQHM APLWPVVLGG VPRSYQFYSA RPNRETLGRV MRLVERGELR MVVDSVWEMR
     DAKMAYKRME SKRAKGKIIV RVQEE
 
 
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