PUT2_AGABI
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 03-AUG-2022, entry version 101.
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; 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=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, 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:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR CDD; cd07123; ALDH_F4-17_P5CDH; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01236; D1pyr5carbox1; 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
