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Database: UniProt
Entry: A0A1V9ZHX8_9STRA
LinkDB: A0A1V9ZHX8_9STRA
Original site: A0A1V9ZHX8_9STRA 
ID   A0A1V9ZHX8_9STRA        Unreviewed;       346 AA.
AC   A0A1V9ZHX8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Delta-1-pyrroline-5-carboxylate reductase {ECO:0000313|EMBL:OQR97589.1};
GN   ORFNames=ACHHYP_10178 {ECO:0000313|EMBL:OQR97589.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR97589.1, ECO:0000313|Proteomes:UP000243579};
RN   [1] {ECO:0000313|EMBL:OQR97589.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR97589.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
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:OQR97589.1}.
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DR   EMBL; JNBR01000100; OQR97589.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9ZHX8; -.
DR   STRING; 1202772.A0A1V9ZHX8; -.
DR   OrthoDB; 196930at2759; -.
DR   Proteomes; UP000243579; 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   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:UP000243579}.
FT   DOMAIN          74..169
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          233..337
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
SQ   SEQUENCE   346 AA;  37367 MW;  3740FB3DC9E04794 CRC64;
     MFRVATSVLR RRSRVVGAAF ASSLVDSSAA CTLRHRSHSA VLEKYAPIYT KTVKHEIEDE
     DEDMGPAATL NVNRVAFIGG GNMAEAIITG MMTQELLPPS QILVSAPSPE TRDKFAQMHV
     ETVDKNKKAL VGADVVIVAV KPQVLKQAVF EDLKKYLDPN ALVISIVAGV TIDAFKHELG
     RDTCIVRSMP NTPAMIGEGI TVWTQSSNVS DVQHDLTKKI LGAFGKQVFV DDEKNLDMAT
     ALSGSGPAYF FLVAEAMIDA GVHMGFGRNV AQKLVQQTML GSALYMQSSG LHPVVLRNNI
     TSPGGTTAAA MYQAEKNGFR AVIADSIWAA YERSKELGAQ AKKRDQ
//
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