ID A0A2T4GLH8_FUSCU Unreviewed; 364 AA.
AC A0A2T4GLH8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN ORFNames=FCULG_00002201 {ECO:0000313|EMBL:PTD04409.1}, HYE67_000578
GN {ECO:0000313|EMBL:QPC58347.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD04409.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD04409.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD04409.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QPC58347.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Class2-1B {ECO:0000313|EMBL:QPC58347.1};
RA Yuan Z.;
RT "The chromosome-scale genome resource for two endophytic Fusarium species:
RT F. culmorum and F. pseudograminearum.";
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-
CC L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001636};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00005076}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00005021}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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DR EMBL; PVEM01000012; PTD04409.1; -; Genomic_DNA.
DR EMBL; CP064747; QPC58347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4GLH8; -.
DR OMA; CEEEMKM; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000241587; Unassembled WGS sequence.
DR Proteomes; UP000663297; Chromosome 1.
DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR NCBIfam; TIGR00978; asd_EA; 1.
DR PANTHER; PTHR46718; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR46718:SF1; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR PIRSF; PIRSF000148; ASA_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01103; ASD; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000241587}.
FT DOMAIN 9..134
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT REGION 290..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 251
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 364 AA; 39041 MW; 5313A72E78B13468 CRC64;
MASQFPTKKC GVLGATGSVG QRFILLLAQH PYLTLHAIGA SSRSAGKKYK DAVRWKQASP
MGEIADMVVR ECKAEEFQDC DVVFSGLDSD VAGDIEMAFI KADIPVFSNA KNYRRDPLVP
LVVPTVNLPH LDLIPHQRSV HKLNKGFLVC NSNCAVIGLV GPFAALQAAF GPISTVSIVT
LQAVSGAGYP GVSSMDVIDN IVPFISGEED KLETEARKIL GRLDDNGTAF IDQEGLRVSA
TCNRVPVMDG HTACVSLSFE RKPSPSAEEV RKALRDYKCE AQALGCPSAP EPAIKVFGDD
EPDRPQPRLD RDLGRGYTVS VGRVREDEAG IFDIKFTALS HNTVIGAAGS SILNAEAAIL
KGYI
//
