ID   PUT2_AGABI              Reviewed;         546 AA.
AC   P78568;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 112.
DE   RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase;
DE            Short=P5C dehydrogenase;
DE            EC=1.2.1.88;
DE   AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
GN   Name=pruA;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Horst H39;
RX   PubMed=8979339; DOI=10.1128/aem.63.1.57-62.1997;
RA   Schaap P.J., Mueller Y., Sonnenberg A.S.M., van Griensven L.J.L.D.,
RA   Visser J.;
RT   "The Agaricus bisporus pruA gene encodes a cytosolic delta 1-pyrroline-5-
RT   carboxylate dehydrogenase which is expressed in fruit bodies but not in
RT   gill tissue.";
RL   Appl. Environ. Microbiol. 63:57-62(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate 5-semialdehyde + NAD(+) + H2O = L-glutamate + NADH
CC         + 2 H(+); Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58066; EC=1.2.1.88;
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X95584; CAA64836.1; -; Genomic_DNA.
DR   AlphaFoldDB; P78568; -.
DR   SMR; P78568; -.
DR   UniPathway; UPA00261; UER00374.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:TreeGrafter.
DR   GO; GO:0003842; F:L-glutamate gamma-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd07123; ALDH_F4-17_P5CDH; 1.
DR   FunFam; 3.40.605.10:FF:000006; 1-pyrroline-5-carboxylate dehydrogenase; 1.
DR   FunFam; 3.40.309.10:FF:000005; 1-pyrroline-5-carboxylate dehydrogenase 1; 1.
DR   Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR005931; P5CDH/ALDH4A1.
DR   InterPro; IPR050485; Proline_metab_enzyme.
DR   NCBIfam; TIGR01236; D1pyr5carbox1; 1.
DR   PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase; Proline metabolism.
FT   CHAIN           1..546
FT                   /note="Delta-1-pyrroline-5-carboxylate dehydrogenase"
FT                   /id="PRO_0000056501"
FT   ACT_SITE        297
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        331
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         279..284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            195
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   546 AA;  59757 MW;  6B795E09AC242945 CRC64;
     MATAQLATFK IPPVSNEPML SYAPGSPERA GLQAALAEMQ SQLPFEVPCI INGQEVRTNN
     IQKQPMPHDH ARHLCTFHEG SPELVEKATC GALQAKDGWE TMPWNDRAAI FLKAADLASG
     KYRYKLMAAT MLGQGKNTWQ AEIDAAAELA DFFRFGVSYV EELYAQQPPK NAPGCWNRTE
     YRPLEGFVLA VSPFNFTAIG GNLPGSPALV GNVVVWKPAP AATYSNYLVF KILSEAGVPP
     GVIQFIPGGA EIVQAAIQSP NFRSLHFTGS TNVFKSLWKD ISSNLDKYKV YPRIVGETGG
     KNWHVIHKSA EVRNAVLQSV RGAFEYQGQK CSALSRLYVS RSVWENGFKT QYLEEIAKIK
     VGPCLDWNNY MGPVIGRRAY DNITGFIKKA KEEGGEVLIG GSGDDSKGFF IQPTVILTKV
     PRSTTMVGEI FGPVVTAYVF EDSDYEKTLE LIDTTSIYGL TGAIFASERQ ALLTATNRSR
     NAAGNIYYNE KCTGAVVGQQ PFGGARGSGT NDKAGSISIF YRFVSARSIK ENFVGLEDFH
     YPSNLV
//