ID A0A0P7B486_9HYPO Unreviewed; 302 AA.
AC A0A0P7B486;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-NOV-2023, entry version 19.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AK830_g5422 {ECO:0000313|EMBL:KPM41166.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM41166.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM41166.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM41166.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPM41166.1}.
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DR EMBL; LKCW01000070; KPM41166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7B486; -.
DR STRING; 78410.A0A0P7B486; -.
DR OrthoDB; 196930at2759; -.
DR Proteomes; UP000050424; 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:UP000050424}.
FT DOMAIN 9..111
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 188..287
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 12..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 68
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 302 AA; 32403 MW; 6FA2860ECCAD8ECE CRC64;
MSNLRDATLC VLGCGNLGRP ILQSLVAGNE DLPFTRFIAC VRSEKSHAAL TKQFAPHLEK
LAIYRSENVK AVQESKVIIL GADPADIESL LTQTGIRDAL ANKLLISVVA GWTRQKLETT
IYGSESSAEN REGRAWIVRT LPNIAALASE GLTAIETDNS EPVLPDEYLK LTTSIFERVG
RTVHIPPRLM NATTAVGGST PAFFAVICDA LIDASVAVGV PRDMAQTMIY QSMRGTATML
QSGIHPGVLK DQGTSPEGCT IGGLMVLEEG AVRGHLGRAL REAVTLARLM ETVEHVNDTR
TA
//
