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Database: UniProt
Entry: A0A139ACB6_GONPJ
LinkDB: A0A139ACB6_GONPJ
Original site: A0A139ACB6_GONPJ 
ID   A0A139ACB6_GONPJ        Unreviewed;       286 AA.
AC   A0A139ACB6;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Pyrroline-5-carboxylate reductase {ECO:0000313|EMBL:KXS14410.1};
GN   ORFNames=M427DRAFT_33104 {ECO:0000313|EMBL:KXS14410.1};
OS   Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC   Gonapodyaceae; Gonapodya.
OX   NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS14410.1, ECO:0000313|Proteomes:UP000070544};
RN   [1] {ECO:0000313|EMBL:KXS14410.1, ECO:0000313|Proteomes:UP000070544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL478 {ECO:0000313|EMBL:KXS14410.1,
RC   ECO:0000313|Proteomes:UP000070544};
RX   PubMed=25977457; DOI=10.1093/gbe/evv090;
RA   Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA   Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA   Spatafora J.W., Berbee M.L.;
RT   "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT   Walls of Algal Ancestors of Land Plants.";
RL   Genome Biol. Evol. 7:1590-1601(2015).
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525}.
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DR   EMBL; KQ965769; KXS14410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139ACB6; -.
DR   STRING; 1344416.A0A139ACB6; -.
DR   OMA; AKQTCLG; -.
DR   OrthoDB; 196930at2759; -.
DR   Proteomes; UP000070544; 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; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR   PANTHER; PTHR11645:SF0; PYRROLINE-5-CARBOXYLATE REDUCTASE 3; 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|ARBA:ARBA00022857};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070544}.
FT   DOMAIN          5..106
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          171..278
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
SQ   SEQUENCE   286 AA;  29695 MW;  8B8746379D494303 CRC64;
     MAQKRLAFVG GGNMASSIIG GLVNAGYPSN HITVFEPNAD LARSLQTQFG TLNASSNDQA
     VLGHPSGGPA DVVLFCVKPQ VMQVVAKGVA GAVQKVKPLV VSIAAGIRSV DLERWLGGTL
     AIVRVMPNTP ALLLEGASGL VANGAVTPEQ KEFSVTLLKT VSKSVEWVDS EHMIDVTTGL
     SGSGPAYFFL LLEVMEDAAV KLGMPRETAR ALAAQTCIGA GRMALEEGKK GVDCAELRRR
     VTSPGGTTAA GLTVLEDGGF RTMVESCVNA ATHRGTEMGE LFGKDT
//
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