ID F9XDF7_ZYMTI Unreviewed; 458 AA.
AC F9XDF7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=glutamate-5-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013002};
DE EC=1.2.1.41 {ECO:0000256|ARBA:ARBA00013002};
DE Flags: Fragment;
GN ORFNames=MYCGRDRAFT_60015 {ECO:0000313|EMBL:EGP86488.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP86488.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP86488.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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; CM001201; EGP86488.1; -; Genomic_DNA.
DR RefSeq; XP_003851512.1; XM_003851464.1.
DR AlphaFoldDB; F9XDF7; -.
DR STRING; 336722.F9XDF7; -.
DR EnsemblFungi; Mycgr3T60015; Mycgr3P60015; Mycgr3G60015.
DR GeneID; 13402199; -.
DR KEGG; ztr:MYCGRDRAFT_60015; -.
DR eggNOG; KOG4165; Eukaryota.
DR HOGENOM; CLU_030231_0_1_1; -.
DR InParanoid; F9XDF7; -.
DR OMA; QYPAVCN; -.
DR OrthoDB; 314297at2759; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000008062; Chromosome 6.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
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; 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.
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:UP000008062}.
FT DOMAIN 6..288
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 458
FT /evidence="ECO:0000313|EMBL:EGP86488.1"
SQ SEQUENCE 458 AA; 48458 MW; 48DFC6B9D6F607D7 CRC64;
MSLTNASPEE AARAAKTSSR TLATLSESSR NKALDAIYDA LSAAREDILA ANAVDLENAK
KAAADGALNP SIFKRLDLSR KGKFDDMLQG IKDVRGLPDP VGRVDLRTEL DAGLILQRQT
CPIGVLLIIF EARPEVIANI ASLAIKSANA AILKGGKEST ESFKAIASTI STALSSTDVP
NDAIQLVTTR DAVDPLLTLS QYIDLVIPRG SNDLVSHCQK KAHMPVLGHA DGLCSLYIHS
DANAQMCIDV VVDSKTDYPA ACNAVETLLV HEDVLSTILP GVATALQAKG VTLRCDQQSL
TALTSTLDPA ASSLLQPSTD QDYATEFLDL ILAIRTIPSS SSSDQPNTSV DAAITHINTH
GSHHTDAILT SSEQTANRFL SSVDAACKFW NASTRFCDGM RFGFGTEVGI STNKVHARGP
VGLEGLTIHE YRVVGKGHCA GAYGGAGGRA YTHRKLPL
//
