ID P5CR_LOPAR Reviewed; 320 AA.
AC Q12740;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Pyrroline-5-carboxylate reductase;
DE Short=P5C reductase;
DE Short=P5CR;
DE EC=1.5.1.2;
GN Name=P5CR;
OS Lophium arboricola (Zalerion arboricola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Mytilinidiales; Mytilinidiaceae; Lophium.
OX NCBI_TaxID=42465;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 20868 / MF5171;
RX PubMed=8654976; DOI=10.1016/0378-1119(96)00107-2;
RA Kelly R., Register E.;
RT "Isolation and sequence analysis of the cDNA encoding delta 1-pyrroline-5-
RT carboxylate reductase from Zalerion arboricola.";
RL Gene 172:149-153(1996).
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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U33266; AAC49320.1; -; mRNA.
DR PIR; JC4830; JC4830.
DR AlphaFoldDB; Q12740; -.
DR SMR; Q12740; -.
DR UniPathway; UPA00098; UER00361.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; NADP; Oxidoreductase; Proline biosynthesis.
FT CHAIN 1..320
FT /note="Pyrroline-5-carboxylate reductase"
FT /id="PRO_0000187329"
SQ SEQUENCE 320 AA; 32975 MW; 90F0ADC59F0AE7F2 CRC64;
MASTAKEGSE LTLAVIGCGT MGIAILSGIL ASLDEIHAPN SQSSETDETP SKLPTKFIAC
VRSPKGAEKI KKALSPYKTP VKIIQSDNVT ACREADVVLL GCKPYMAEGI LGEEGMVDAL
KGKLLISILA GVPAEQIYGY MYGKTPVNPE KEGLCQVVRA MPNTASGIRE SMTVIATSSP
PLSATTSSLI TWIFKRIGDV VQLPAATMDA STALCGSGPA FFALILEAAI DGAVAMGLPR
AEAQRMAAQT MKGAAGLVLS GEHPALLKDK VTTPGGCTIG GLMVLEEGGV RGTVARAVRE
ATVVASQLGK GVQGVNGTRF
//
