ID A0A1V6RX36_9EURO Unreviewed; 302 AA.
AC A0A1V6RX36;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 08-NOV-2023, entry version 18.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENVUL_c018G04360 {ECO:0000313|EMBL:OQE06335.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE06335.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE06335.1}.
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DR EMBL; MDYP01000018; OQE06335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RX36; -.
DR STRING; 29845.A0A1V6RX36; -.
DR OrthoDB; 196930at2759; -.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:InterPro.
DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.3730.10; ProC C-terminal domain-like; 1.
DR HAMAP; MF_01925; P5C_reductase; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR InterPro; IPR029036; P5CR_dimer.
DR InterPro; IPR000304; Pyrroline-COOH_reductase.
DR NCBIfam; TIGR00112; proC; 1.
DR PANTHER; PTHR11645:SF27; HYPOTHETICAL PYRROLINE-5-CARBOXYLATE REDUCTASE (EUROFUNG); 1.
DR PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|PIRSR:PIRSR000193-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000191518}.
FT DOMAIN 8..114
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 189..288
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 11..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 71
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 302 AA; 32368 MW; 3017F0F05C5F87BD CRC64;
MDIQNGTLCI LGCGNLGIAI LDGLVNAPVE KSKELPFARY TACVRSESSE KRLFERFTQS
LDKISISRGN NVQAVQNADV IILGADPADI ETVLTQTGLR EALVDKLIIS IAAGWTRQKL
EVTLYGSETT TDNTAGRAWV VRTLPNIAAQ VSQSLTAIET SEPALPERYL QITTSIFEQI
GKAVHIDPRL MNATTAVGGS TPAFFAVICD AMIDAAVAVG LPRDLAHTMI FQSMQGTAMM
LQSGIHPALL KDQGTSPEGC TIGGLMVMEE AGVRGHVGRA LREAVTLARL METTPHVNDT
RH
//
