ID C5DG37_LACTC Unreviewed; 457 AA.
AC C5DG37;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=glutamate-5-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013002};
DE EC=1.2.1.41 {ECO:0000256|ARBA:ARBA00013002};
GN OrderedLocusNames=KLTH0D02134g {ECO:0000313|EMBL:CAR22379.1};
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR22379.1, ECO:0000313|Proteomes:UP000002036};
RN [1] {ECO:0000313|EMBL:CAR22379.1, ECO:0000313|Proteomes:UP000002036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC {ECO:0000313|Proteomes:UP000002036};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-
CC glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00000979};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004985}.
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DR EMBL; CU928168; CAR22379.1; -; Genomic_DNA.
DR RefSeq; XP_002552817.1; XM_002552771.1.
DR AlphaFoldDB; C5DG37; -.
DR STRING; 559295.C5DG37; -.
DR GeneID; 8295037; -.
DR KEGG; lth:KLTH0D02134g; -.
DR eggNOG; KOG4165; Eukaryota.
DR HOGENOM; CLU_030231_0_1_1; -.
DR InParanoid; C5DG37; -.
DR OMA; QYPAVCN; -.
DR OrthoDB; 314297at2759; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000002036; Chromosome D.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR HAMAP; MF_00412; ProA; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR020593; G-glutamylP_reductase_CS.
DR InterPro; IPR012134; Glu-5-SA_DH.
DR InterPro; IPR000965; GPR_dom.
DR NCBIfam; TIGR00407; proA; 1.
DR PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF000151; GPR; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS01223; PROA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000002036}.
FT DOMAIN 5..267
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 457 AA; 49968 MW; 0D4C8394DB43F744 CRC64;
MSSTAEIIAK NARLGGNTLK TISNENRSRL LYKIHDGLKA NAKSIKEANQ LDLQKAKEDS
LADSLYKRLD LFKGDKFDTM LIGIKDVAEL EDPVGKVRLA RQLDENLDLY QVTAPVGALL
VIFESRPEVI ANITSLAIKS GNAAILKGGK ESVHTFREIS RIINTVISEN EESTGIPASV
IQLIETRQDV SDLLQQDLYI DLVVPRGSNE LVRKIKSSTK IPVLGHADGI CSIYLDSEAD
LAISKRITID AKTSYPAGCN AVETILVNPE MPKWWEVLEN LSKVGGVTLH VSADVKASYL
DFLKQSGAQD DDAQGKIVDA DESKDFDREF LSLDCAVKFV HSTEDAIAHI NQHSSKHTDA
IITENKAKAE LFMKGVDSSG VYWNASTRFA DGFRYGFGTE VGISTSKIHA RGPVGLDGLV
SYQYQLRGNG QVASDYIGSG GKKAFIHKNL DISNLRL
//
