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Database: UniProt
Entry: A0A672Y9J2_9TELE
LinkDB: A0A672Y9J2_9TELE
Original site: A0A672Y9J2_9TELE 
ID   A0A672Y9J2_9TELE        Unreviewed;       310 AA.
AC   A0A672Y9J2;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|ARBA:ARBA00012855, ECO:0000256|RuleBase:RU003903};
DE            EC=1.5.1.2 {ECO:0000256|ARBA:ARBA00012855, ECO:0000256|RuleBase:RU003903};
GN   Name=LOC115426152 {ECO:0000313|Ensembl:ENSSORP00005000504.1};
OS   Sphaeramia orbicularis (orbiculate cardinalfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX   NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005000504.1, ECO:0000313|Proteomes:UP000472271};
RN   [1] {ECO:0000313|Ensembl:ENSSORP00005000504.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000593};
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|ARBA:ARBA00000723,
CC         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|ARBA:ARBA00005205, 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   AlphaFoldDB; A0A672Y9J2; -.
DR   Ensembl; ENSSORT00005000529.1; ENSSORP00005000504.1; ENSSORG00005000308.1.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000472271; Unplaced.
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:SF63; 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|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU003903};
KW   NADP {ECO:0000256|PIRSR:PIRSR000193-1, ECO:0000256|RuleBase:RU003903};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003903};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650,
KW   ECO:0000256|RuleBase:RU003903};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472271}.
FT   DOMAIN          3..98
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          164..268
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         6..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         34
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         56
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         69..72
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         95..97
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   310 AA;  32742 MW;  72FA78403898D88F CRC64;
     MSVGFIGAGQ LAHALVKGFT AAGVIATQRI TASSPDTDLP TVAGLRKMGV TMTTSNKETV
     NKSDVLFLAV KPHIIPFVLD EIGPDIEDRH LIVSCAAGVT ISSIEKKLLQ YRSAPKVMRC
     MTNTPVVVRE GATVYATGTH AEVEDGKLLE QLMASVGFCT EVEEDLIDAV TGLSGSGPAY
     AFTALDALAD GGVKMGLPRR LAVRLGAQAL LGAAKMLLDS EQHPGQLKDN VCSPGGATIH
     ALHVLESGGF RSLLINAVEA SCIRTRELQF LADQERISPA AIKKTTLDKV LQQAGLSLFN
     TRTPGIKKKN
//
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