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Database: UniProt
Entry: A0A1R1XY67_9FUNG
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ID   A0A1R1XY67_9FUNG        Unreviewed;       360 AA.
AC   A0A1R1XY67;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE            EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN   ORFNames=AYI70_g4601 {ECO:0000313|EMBL:OMJ19631.1};
OS   Smittium culicis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ19631.1, ECO:0000313|Proteomes:UP000187283};
RN   [1] {ECO:0000313|EMBL:OMJ19631.1, ECO:0000313|Proteomes:UP000187283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSMNP {ECO:0000313|EMBL:OMJ19631.1,
RC   ECO:0000313|Proteomes:UP000187283};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OMJ19631.1}.
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DR   EMBL; LSSN01001439; OMJ19631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1XY67; -.
DR   STRING; 133412.A0A1R1XY67; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000187283; Unassembled WGS sequence.
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:UP000187283}.
FT   DOMAIN          8..134
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
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   360 AA;  38964 MW;  C072596276A74163 CRC64;
     MSTKKVMRAG ILGATGTVGQ RFICLLSSNP RFEIHVLGAS DRSAGRPYSQ ATNWKLSDRL
     PENVASMIVK SCNPSEFEGC DLIFSGLDAS VATEIEKSFM EGNFPVFSNA KNYRMFDTVP
     LVIPTANPEH FAVIGQQRKE FNLNRGYIIT NSNCSVTGIA VVLKALQLTF GKISKVMVTT
     MQAISGAGYP GVASLDIMDN VVPHIGGEEE KIEQELGKIL GSASTDNTSI LSDDQLKVSA
     MCNRVAVIDG HTSSVSIEFA SGQKPSIQEI KTCLSEYRCM AQQLGCHSAP KQAIIVHENQ
     DRPQPRLDRM NENGMAVSIG RIRECPILDF KFTILVHNTI LGAAGASMLN AELASEMGLI
//
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