ID   PFMAB_PESFW             Reviewed;         281 AA.
AC   W3XA95;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Proline iminopeptidase PfmaB {ECO:0000303|PubMed:28517364};
DE            Short=PIP {ECO:0000303|PubMed:28517364};
DE            EC=3.4.11.5 {ECO:0000305|PubMed:28517364};
DE   AltName: Full=Conidial pigment biosynthesis cluster protein B {ECO:0000303|PubMed:28517364};
GN   Name=PfmaB {ECO:0000303|PubMed:28517364}; ORFNames=PFICI_07098;
OS   Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX   NCBI_TaxID=1229662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W106-1 / CGMCC3.15140;
RX   PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA   Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA   Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT   "Genomic and transcriptomic analysis of the endophytic fungus
RT   Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT   of natural products.";
RL   BMC Genomics 16:28-28(2015).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28517364; DOI=10.1111/mmi.13711;
RA   Zhang P., Wang X., Fan A., Zheng Y., Liu X., Wang S., Zou H., Oakley B.R.,
RA   Keller N.P., Yin W.B.;
RT   "A cryptic pigment biosynthetic pathway uncovered by heterologous
RT   expression is essential for conidial development in Pestalotiopsis fici.";
RL   Mol. Microbiol. 105:469-483(2017).
RN   [3]
RP   FUNCTION.
RX   PubMed=31116900; DOI=10.1111/mmi.14281;
RA   Zhang P., Zhou S., Wang G., An Z., Liu X., Li K., Yin W.B.;
RT   "Two transcription factors cooperatively regulate DHN melanin biosynthesis
RT   and development in Pestalotiopsis fici.";
RL   Mol. Microbiol. 112:649-666(2019).
CC   -!- FUNCTION: Proline iminopeptidase; part of the gene cluster that
CC       mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a
CC       bluish-green pigment forming a dark layer in the conidial wall that
CC       protects the conidia from UV radiations (PubMed:28517364). The first
CC       step of the pathway is the production of the pentaketide 1,3,6,8-
CC       tetrahydroxynaphthalene (1,3,6,8-THN or T4HN) by the polyketide
CC       synthase PfmaE though condensation of acetyl-CoA with malonyl-CoA. T4HN
CC       is not stable and easily oxidizes into the stable form flaviolin
CC       (PubMed:28517364). T4HN is also substrate of the hydroxynaphthalene
CC       reductase PfmaG to yield scytalone (PubMed:28517364). The scytalone
CC       dehydratase PfmaJ then reduces scytalone to 1,3,8-THN
CC       (PubMed:31116900). 1,3,8-THN is then substrate of the
CC       hydroxynaphthalene reductase PfmaI to yield vermelone (Probable).
CC       Vermelone is further converted by the multicopper oxidase PfmaD to 1,8-
CC       DHN (Probable). Finally the laccase PFICI_06862 transforms 1,8-DHN to
CC       DHN-melanin (Probable). The roles of the 5-oxoprolinase PfmaA and the
CC       proline iminopeptidase PfmaB within the cluster have not been
CC       elucidated yet (Probable). {ECO:0000269|PubMed:28517364,
CC       ECO:0000269|PubMed:31116900, ECO:0000305|PubMed:28517364,
CC       ECO:0000305|PubMed:31116900}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC         Evidence={ECO:0000305|PubMed:28517364};
CC   -!- DISRUPTION PHENOTYPE: Does not affect the production of scytalone.
CC       {ECO:0000269|PubMed:28517364}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; KI912112; ETS82096.1; -; Genomic_DNA.
DR   RefSeq; XP_007833870.1; XM_007835679.1.
DR   AlphaFoldDB; W3XA95; -.
DR   SMR; W3XA95; -.
DR   STRING; 1229662.W3XA95; -.
DR   EnsemblFungi; ETS82096; ETS82096; PFICI_07098.
DR   GeneID; 19272111; -.
DR   KEGG; pfy:PFICI_07098; -.
DR   eggNOG; ENOG502QPPY; Eukaryota.
DR   HOGENOM; CLU_020336_50_0_1; -.
DR   OMA; KDWICPP; -.
DR   OrthoDB; 1061420at2759; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Melanin biosynthesis; Protease;
KW   Reference proteome.
FT   CHAIN           1..281
FT                   /note="Proline iminopeptidase PfmaB"
FT                   /id="PRO_0000445350"
FT   DOMAIN          23..267
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   281 AA;  31682 MW;  BB69B3B3C7088DD9 CRC64;
     MVEFVEINGA QLAYRICGPE DAPLVITLHG GRGMGNHQSD FKAFSPLGDS YRILSFDYRG
     HGQSSRTKPY TFEQIVDDID GMRARFAGPE KQVIILGGSF GGFLAQQYAI KYASHVSHLI
     LRGTAPSHHH EEGAIKTLEQ RLSKVPSFSI EMLKDKVFGA FDSDLEFRMV HLVMSPLYSE
     SFDANAALQS CLNNVYNAES HNDLYSEKEK YFDYTKDLHR ITAKTLVVVG DKDWICPPEN
     SKFIAKEIKD AELFLVENAN HSVHVEKNDL VVKKIRSHLE K