ID A0A1L7X447_9HELO Unreviewed; 449 AA.
AC A0A1L7X447;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=glutamate-5-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013002};
DE EC=1.2.1.41 {ECO:0000256|ARBA:ARBA00013002};
GN ORFNames=PAC_09682 {ECO:0000313|EMBL:CZR59788.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR59788.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR59788.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR59788.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; FJOG01000014; CZR59788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7X447; -.
DR STRING; 576137.A0A1L7X447; -.
DR OrthoDB; 314297at2759; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000184330; Unassembled WGS sequence.
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:UP000184330}.
FT DOMAIN 10..286
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 449 AA; 47775 MW; 94540047C902C998 CRC64;
MSLTNALPAD AAKAAKSASH TLATLPASAR NDALTAIHKG LSGAKEEILA ANARDLELAR
KAADNGELSL SIVSRLDLGK KGKWEDMLKG ILDVRDLEDP VGKVTLRTKL DDGLTLERVT
CPIGVLLIIF EARPEVIANI ASLAIKSGNA AILKGGKEST ESFIAISTVI SAALESTAVP
NSAVQLVTTR DVIPQLLSQD KNIDLVIPRG SNELVRYIKS STKIPVLGHA DGICALYLEH
TADLPMAVKV IVDSKTAYPA ACNSAEVLLV EEAALETVLP PVAQALLEQG VSLRCDPASK
KALSSKLDSH SATILQDAED VDFDTEHLSL VLPIKTVKSV EEAIIHINIH GSHHTDVILT
SSSELAEQFM AGVDSAGVFW NTSTRMADGM RFGFGTEVGI STNKIHARGP VGLEGLMIYK
YKIRGGGQVS AEYGEAEGQK RFKHEQLPF
//
