ID A0A136IS89_9PEZI Unreviewed; 450 AA.
AC A0A136IS89;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=glutamate-5-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013002};
DE EC=1.2.1.41 {ECO:0000256|ARBA:ARBA00013002};
GN ORFNames=Micbo1qcDRAFT_20816 {ECO:0000313|EMBL:KXJ87629.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ87629.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-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; KQ964261; KXJ87629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IS89; -.
DR STRING; 196109.A0A136IS89; -.
DR InParanoid; A0A136IS89; -.
DR OrthoDB; 314297at2759; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000070501; 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:UP000070501}.
FT DOMAIN 10..287
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 450 AA; 48117 MW; F5414A2B75E35455 CRC64;
MSLTNASPLE AAKSAKSASH ILATLPASAR NDALTAIHTA LSAARDDILA ANARDLEAAR
SAAASGELSQ SLVSRLDLGK KGKWEDMLKG ILDVRDLEDP VGKVTLRTRL DDGLEMTRVT
CPIGVLLIIF EARPEVIANI ASLAVKSGNS AILKGGKEST ESFVAISKVI SEALDKSEVP
NGAIQLVTTR DVIPQLLDLD QYIDLVVPRG SNELVRYIKS STKIPVLGHA DGLCSIFLEQ
SVDPTLAADV IVDSKTTYPA ACNSLETLLV QEAALESILP AIAEKLIAKE VTLKCDGRSK
AVLASKLPTD LAAKYLQDAT NVDFDTEFLS LTLAVKVVAD LGEAVQHINE HGSKHTDCIL
TSSEELAERF MASVDAAGVY WNASTRFADG MRYGFGTEVG ISTNKIHSRG PVGLEGLMIY
KYQIRGNGHI TAVYGEGKGQ KRFKHEKLPL
//
