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Database: UniProt
Entry: A0A1V6S593_9EURO
LinkDB: A0A1V6S593_9EURO
Original site: A0A1V6S593_9EURO 
ID   A0A1V6S593_9EURO        Unreviewed;       364 AA.
AC   A0A1V6S593;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Semialdehyde dehydrogenase NAD-binding domain-containing protein {ECO:0000259|SMART:SM00859};
GN   ORFNames=PENVUL_c007G09758 {ECO:0000313|EMBL:OQE09028.1};
OS   Penicillium vulpinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE09028.1, ECO:0000313|Proteomes:UP000191518};
RN   [1] {ECO:0000313|Proteomes:UP000191518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE09028.1}.
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DR   EMBL; MDYP01000007; OQE09028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6S593; -.
DR   STRING; 29845.A0A1V6S593; -.
DR   OrthoDB; 6339at2759; -.
DR   Proteomes; UP000191518; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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.
PE   4: Predicted;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191518}.
FT   DOMAIN          9..135
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        155
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ   SEQUENCE   364 AA;  39278 MW;  DCABC5F9FEDF48D5 CRC64;
     MAPVFPKKKC GVLGATGSVG QRFILLLADH PFLELHAVGA SERSANKKYK DAVNWKQSSP
     MSEKLSNLVM RDCKPEQFSD CDLVFSGLNS DVAGETEMAF IKAEIPVFSN AKNFRKDPIV
     PLVVPTVNPQ HLDLIPHQRE KFGLKKGFLV CNSNCAVIGI VIPFAALQAK FGPVEEVEVF
     TEQAVSGAGY PGVPTMDILD NVIPYISGEE DKLENEAQKI LGSLNASATG FDEQTGLRIG
     ATCTRVGVTD GHMAFVSLRF KNRQTPTAEQ VKEALREYKS EAQKLGAPSA PEPAIKVFDQ
     PDRPQPRLDR NISGGYTVSV GRVREGAPGG HFDIRFAALS HNTVIGAAGS SILNAEVAVI
     KGYI
//
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