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 27-MAR-2024, entry version 114.
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; 284590.Q6CR99; -.
DR PaxDb; 284590-Q6CR99; -.
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: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 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
//
