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Database: UniProt
Entry: R9AN44_WALI9
LinkDB: R9AN44_WALI9
Original site: R9AN44_WALI9 
ID   R9AN44_WALI9            Unreviewed;       307 AA.
AC   R9AN44;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|RuleBase:RU003903};
DE            EC=1.5.1.2 {ECO:0000256|RuleBase:RU003903};
GN   ORFNames=J056_003104 {ECO:0000313|EMBL:EOR03647.1};
OS   Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR03647.1, ECO:0000313|Proteomes:UP000014064};
RN   [1] {ECO:0000313|Proteomes:UP000014064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX   PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA   Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT   "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT   ichthyophaga: haloadaptations present and absent.";
RL   BMC Genomics 14:617-617(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC         NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC         Evidence={ECO:0000256|RuleBase:RU003903};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC       from L-glutamate 5-semialdehyde: step 1/1.
CC       {ECO:0000256|RuleBase:RU003903}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|RuleBase:RU003903}.
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DR   EMBL; KE007226; EOR03647.1; -; Genomic_DNA.
DR   RefSeq; XP_009266683.1; XM_009268408.1.
DR   AlphaFoldDB; R9AN44; -.
DR   STRING; 1299270.R9AN44; -.
DR   GeneID; 20376056; -.
DR   KEGG; wic:J056_003104; -.
DR   eggNOG; KOG3124; Eukaryota.
DR   HOGENOM; CLU_042344_1_1_1; -.
DR   OMA; YYFIESL; -.
DR   OrthoDB; 196930at2759; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000014064; Unassembled WGS sequence.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
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.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003903};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000193-1};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003903};
KW   Proline biosynthesis {ECO:0000256|RuleBase:RU003903};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014064}.
FT   DOMAIN          64..135
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          198..300
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         92
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   307 AA;  32253 MW;  428EEAF94D11216F CRC64;
     MGVAVLSGVI DGLNTRNSMS TSQLNTDDAS GTSTPIDISS SQAIMEAKES CLPSKFLCTV
     NRSESAKSLR KTFDLLGDAG KQVNILQGGG VNVDAVRDSD VVLLCAKPQM AHTILNEPGM
     QEALANKLLI SILAGVTITQ IHSWVPKSTK VVRAMPNTPC KIREGMTVVS ALPTDWVFEK
     ELILAIFRSI GRCRFLEEKH FDACTALCGS GPAFAVTVLE AMADGGVMMG LPRAEAVELA
     AQSMQGIARM VLETGVHPAA LKDSVTTPGG CTIAGLLALE DGKVRSTMAR TIQVATSHAS
     GLGQAKK
//
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