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Database: UniProt
Entry: A0A2P6MP79_9EUKA
LinkDB: A0A2P6MP79_9EUKA
Original site: A0A2P6MP79_9EUKA 
ID   A0A2P6MP79_9EUKA        Unreviewed;       231 AA.
AC   A0A2P6MP79;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PROFUN_02494 {ECO:0000313|EMBL:PRP73485.1};
OS   Planoprotostelium fungivorum.
OC   Eukaryota; Amoebozoa; Evosea; Variosea; Cavosteliida; Cavosteliaceae;
OC   Planoprotostelium.
OX   NCBI_TaxID=1890364 {ECO:0000313|EMBL:PRP73485.1, ECO:0000313|Proteomes:UP000241769};
RN   [1] {ECO:0000313|EMBL:PRP73485.1, ECO:0000313|Proteomes:UP000241769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jena {ECO:0000313|EMBL:PRP73485.1,
RC   ECO:0000313|Proteomes:UP000241769};
RX   PubMed=29378020; DOI=10.1093/gbe/evy011;
RA   Hillmann F., Forbes G., Novohradska S., Ferling I., Riege K., Groth M.,
RA   Westermann M., Marz M., Spaller T., Winckler T., Schaap P., Glockner G.;
RT   "Multiple Roots of Fruiting Body Formation in Amoebozoa.";
RL   Genome Biol. Evol. 10:591-606(2018).
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:PRP73485.1}.
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DR   EMBL; MDYQ01000599; PRP73485.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P6MP79; -.
DR   STRING; 1890364.A0A2P6MP79; -.
DR   InParanoid; A0A2P6MP79; -.
DR   Proteomes; UP000241769; 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   PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR   PANTHER; PTHR11645:SF0; 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|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000193-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241769}.
FT   DOMAIN          9..105
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          174..220
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         13..18
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         60
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         73..76
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   231 AA;  24440 MW;  3F8CB7E96EA23491 CRC64;
     MSTSLEKIKI SFIGGGNMAA AIIGGLLSKN ISADNIYVSE PWDVNRQKMA AMGVKTTTCN
     KQASNDADII IIAVKPQVTK DVCEELGAAW TDRQSLPLII SISAGITLSS ISQWFSVNGN
     EAPHIVRVMP NTPALVGEGA SGLYADANVT GDEKELATAL MSTVSKATEW VDREELLDVV
     TALSGSGPAY FFDFVEHMIS SATSLGLSEE QATRLAKQTC FAPMAPPTPL S
//
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