ID   PFMAA_PESFW             Reviewed;        1283 AA.
AC   W3X7R6;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=5-oxoprolinase PfmaA {ECO:0000303|PubMed:28517364};
DE            EC=3.5.2.9 {ECO:0000305|PubMed:28517364};
DE   AltName: Full=Conidial pigment biosynthesis cluster protein A {ECO:0000303|PubMed:28517364};
GN   Name=PfmaA {ECO:0000303|PubMed:28517364}; ORFNames=PFICI_07097;
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: 5-oxoprolinase; part of the gene cluster that mediates the
CC       biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green
CC       pigment forming a dark layer in the conidial wall that protects the
CC       conidia from UV radiations (PubMed:28517364). The first step of the
CC       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=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate +
CC         phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216; EC=3.5.2.9;
CC         Evidence={ECO:0000305|PubMed:28517364};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28273}.
CC   -!- DISRUPTION PHENOTYPE: Does not affect the production of scytalone.
CC       {ECO:0000269|PubMed:28517364}.
CC   -!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}.
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DR   EMBL; KI912112; ETS82095.1; -; Genomic_DNA.
DR   RefSeq; XP_007833869.1; XM_007835678.1.
DR   AlphaFoldDB; W3X7R6; -.
DR   SMR; W3X7R6; -.
DR   STRING; 1229662.W3X7R6; -.
DR   EnsemblFungi; ETS82095; ETS82095; PFICI_07097.
DR   GeneID; 19272110; -.
DR   KEGG; pfy:PFICI_07097; -.
DR   eggNOG; KOG1939; Eukaryota.
DR   HOGENOM; CLU_002157_0_0_1; -.
DR   OMA; CRIGTTI; -.
DR   OrthoDB; 62698at2759; -.
DR   Proteomes; UP000030651; Unassembled WGS sequence.
DR   GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR008040; Hydant_A_N.
DR   InterPro; IPR002821; Hydantoinase_A.
DR   InterPro; IPR003692; Hydantoinase_B.
DR   InterPro; IPR045079; Oxoprolinase_fam.
DR   PANTHER; PTHR11365; PTHR11365; 1.
DR   Pfam; PF05378; Hydant_A_N; 1.
DR   Pfam; PF01968; Hydantoinase_A; 1.
DR   Pfam; PF02538; Hydantoinase_B; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Melanin biosynthesis; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1283
FT                   /note="5-oxoprolinase PfmaA"
FT                   /id="PRO_0000445349"
FT   REGION          1256..1283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1268..1283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1283 AA;  139396 MW;  4028AE6D4C02A095 CRC64;
     MTADIRVSID RGGTFCDVIA HVEGREPIIF KLLSVDPANY QDAPTEGIRR VLEIVEGKKI
     PVGEKLDGTR IASCRLGTTV ATNALLEGKY EKFALVTTKG FEDVCVIGDQ SRPKLFDLKV
     KKAEALHDTV IGVDERVTIE DYDLNPYPLD KSASLNDPDL VRTPSGEIIR ILARVNEETV
     REQLLALRDA GYNSVAISFM HSYIFPDHED QVAKIAREVG FTYVTTSAET RPVLKYLNRS
     TSCCSEACLY PVIRRYIENF ESGFRVLPRR VDFMCSDGGL KQSQKFRGNE ALLSGPAGGV
     VGIATSCYDV EQKIPIIGFD MGGTSTDVSR FDGKYDYLSE TVIADRTISM PMLNISTVAA
     GGGSILFARS GLLVVGPESA GAHPGPACYR KGGPLTVTDA NLFLGRLVVS SFPSIFGENA
     DQPLDQDVVT AKFQEITADF NSQTSQNLTA EEVALGFLDV ANEAMSRPIR NTTEARGFAP
     EKHNLVSFGG AGGQHACAIA SKLGIKRVLI HKWSSLLSAH GISQADLQYE SFEPLSLDFG
     MDLNGFIKER LSLLREKVAA GLLAQGAQES TLRFDESLVM KYFGTDTTIT VTTPDDLDYG
     AAFEALHLRE FAFKLNRKIV IDSVNVRGTG SAVTLATEEP PLKALARVKS VATTAQTTEE
     QKVYINGSWR KVPIYRLDQL SKGCAVSGPA MIIDKTQTIF VEPRFNAYIL PDHVILEESN
     VEDTVTRQAV SAEEINPLLL SVFAHRFMSI AEQMGNTLQR TSVSSSIKER LDFSCAIFSR
     EGKLVANAPH IPIHLGSMQM AIRYQHEAWK GKLKPGDALV TNHPLSGGTH LPDLTVVSPV
     FVNGDVAFYV ASRGHHTDIG GKGIAAMMPE SKELWEEGIS IKTMKIVSGG EFLEDEIRAA
     FDKAGSFPGC SPTRRIADNL SDLKAQIASN QRGIILLGNL CEEFTLPVVC TYMEGIQANA
     EFAVRRFLKQ LAKKHPEPLT AIDYFDDGTP IKIKIIIDPE TGGAVYDFSG TGPQQWGNYN
     CPISITHSAI IYTLRCLVDV DIPLNEGCLT PIDIRVPYGS MLNPSPAVAI CGSTLASQRV
     IDTILRAFRR CAASQGCASS FSWGMGGRDP ETGKVLPGWN YGESLGGGVG ALPGYHGESA
     INVHSTNTRN TDPEVVEKRT AVLVTKYAVR KGSGGRGQWR GGDGVTREIQ ARIPLKFSIL
     SDRRVYRPYG MEGGEAGHRG QNYVFKFNQE GTGFEQINLG GKAVVVLNPG EKMQINTPGG
     GAWGKPEGDA DGYREEDQAG DGI