ID A0A0J9X9I0_GEOCN Unreviewed; 287 AA.
AC A0A0J9X9I0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|RuleBase:RU003903};
DE EC=1.5.1.2 {ECO:0000256|RuleBase:RU003903};
GN ORFNames=BN980_GECA05s02012g {ECO:0000313|EMBL:CDO53457.1};
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO53457.1, ECO:0000313|Proteomes:UP000242525};
RN [1] {ECO:0000313|EMBL:CDO53457.1, ECO:0000313|Proteomes:UP000242525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO53457.1,
RC ECO:0000313|Proteomes:UP000242525};
RA Casaregola S.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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; CCBN010000005; CDO53457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9X9I0; -.
DR STRING; 1173061.A0A0J9X9I0; -.
DR OrthoDB; 196930at2759; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000242525; 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}.
FT DOMAIN 12..119
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 181..281
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 16..21
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 287 AA; 29711 MW; F34B316B0DEE275F CRC64;
MPAPQVLKPG YTIGVIACGT MGTAVLNAIV TATTASDSKD VKTPLPGKFL TSVNSQKSVD
RLNGIFGDKV SVSIGNNDKI VSSSDLIILG CKPFLADDIL SSIDKELFRG KTVISLLAGK
TIEQLTTLTG ATVARAMTNT PSKIGAGMTV VSLPKVDIDE TVRDSISWIF NNTGRCLFMD
EKFMDVATAL CGSGPAFCFL MIEALSDGAV KMGMPYPVAQ ECAAQVLHGA AQMVLEGNHP
AVLRNAVCTP GGTTIGGLSV LEDKGVRGSV ASAVVEAANI ATALSKK
//
