ID D8M613_BLAHO Unreviewed; 275 AA.
AC D8M613;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSBLH_T00003451001 {ECO:0000313|EMBL:CBK23612.2};
OS Blastocystis hominis.
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=12968 {ECO:0000313|EMBL:CBK23612.2};
RN [1] {ECO:0000313|EMBL:CBK23612.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore isolate B {ECO:0000313|EMBL:CBK23612.2};
RA Wincker P.;
RT "Sequencing and annotation of the Blastocystis hominis genome.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525}.
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DR EMBL; FN668661; CBK23612.2; -; Genomic_DNA.
DR RefSeq; XP_012897660.1; XM_013042206.1.
DR AlphaFoldDB; D8M613; -.
DR EnsemblProtists; CBK23612; CBK23612; GSBLH_T00003451001.
DR GeneID; 24920550; -.
DR InParanoid; D8M613; -.
DR OMA; VVRVMTN; -.
DR OrthoDB; 196930at2759; -.
DR Proteomes; UP000008312; 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; 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:UP000008312}.
FT DOMAIN 7..101
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 167..269
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 71..74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 275 AA; 29686 MW; 33AF92CADB85057F CRC64;
MLDAYHIGFI GGGVMATTMI SGFLQTETFA KDHIHVFDIS EDRTNYFKSV GIIVNDGITP
LVDACDIIVF AVKPDVLLTL LHSPLSMGEY YDRKKLFISI ACGIKIAQIR DRIHPKTCGI
VRLLPNTPCG VLKGICCYTL GPNTDEETDK LMKNMFGKLG ETLKIPECYM DAVVALAGSG
PAIIYMLIEA LADGGVKSGL PRDLAMNLAA YTVRGAAEMV IQTNRHPAEL KDQVCSPGGT
SIAGVEYLEK KGFRGNVLGA VYAAFCRGKD IGNTE
//
