ID   P5CR_KLULA              Reviewed;         285 AA.
AC   Q6CR99;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000303|PubMed:24912400};
DE            Short=P5C reductase {ECO:0000250|UniProtKB:P32263};
DE            Short=P5CR {ECO:0000250|UniProtKB:P32263};
DE            EC=1.5.1.2 {ECO:0000269|PubMed:24912400};
GN   Name=PRO3 {ECO:0000303|PubMed:24912400}; OrderedLocusNames=KLLA0D10736g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [2]
RP   CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=24912400; DOI=10.1111/mmi.12666;
RA   Romagnoli G., Verhoeven M.D., Mans R., Fleury Rey Y., Bel-Rhlid R.,
RA   van den Broek M., Seifar R.M., Ten Pierick A., Thompson M., Muller V.,
RA   Wahl S.A., Pronk J.T., Daran J.M.;
RT   "An alternative, arginase-independent pathway for arginine metabolism in
RT   Kluyveromyces lactis involves guanidinobutyrase as a key enzyme.";
RL   Mol. Microbiol. 93:369-389(2014).
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:0000269|PubMed:24912400};
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:0000269|PubMed:24912400};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC       from L-glutamate 5-semialdehyde: step 1/1.
CC       {ECO:0000305|PubMed:24912400}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P32263}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; CR382124; CAH00636.1; -; Genomic_DNA.
DR   RefSeq; XP_453540.1; XM_453540.1.
DR   AlphaFoldDB; Q6CR99; -.
DR   SMR; Q6CR99; -.
DR   STRING; 28985.XP_453540.1; -.
DR   EnsemblFungi; CAH00636; CAH00636; KLLA0_D10736g.
DR   GeneID; 2892904; -.
DR   KEGG; kla:KLLA0_D10736g; -.
DR   eggNOG; KOG3124; Eukaryota.
DR   HOGENOM; CLU_042344_1_2_1; -.
DR   InParanoid; Q6CR99; -.
DR   OMA; VVRVMTN; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
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   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   PANTHER; PTHR11645; PTHR11645; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00112; proC; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; NADP; Oxidoreductase; Proline biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..285
FT                   /note="Pyrroline-5-carboxylate reductase"
FT                   /id="PRO_0000432233"
SQ   SEQUENCE   285 AA;  30164 MW;  AEADD055F4ECC847 CRC64;
     MSRYTLAIVG CGVMGQALLS AIYNAPKASD EALQYYPSKI IACNDVPASA ELVEKLVSGF
     ETSPNGIEVE IATNDNERAV AEAKVIILGL KPHIVEPVLQ QIPNEDGSKL LISLAAGVTL
     NQLSQYYKKV SRVMTNTPAK YGYGTAIVSH STSVEPQDKA IVSELVSQVG KCLELPEKNM
     DAATALVGSG PAFVLLMLES MMEAGLKMGI PLKESRECAM KVLEGTAKMV EISGQSPGVL
     KHQVCTPGGT TIAGLCVMED KGVKSGIIRG IEEAARVSKE LGQKK