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Database: UniProt
Entry: Q59134_ACTPL
LinkDB: Q59134_ACTPL
Original site: Q59134_ACTPL 
ID   Q59134_ACTPL            Unreviewed;        61 AA.
AC   Q59134;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:CAA67770.1};
DE            EC=1.2.1.11 {ECO:0000313|EMBL:CAA67770.1};
DE   Flags: Fragment;
GN   Name=asd {ECO:0000313|EMBL:CAA67770.1};
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715 {ECO:0000313|EMBL:CAA67770.1};
RN   [1] {ECO:0000313|EMBL:CAA67770.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1421 {ECO:0000313|EMBL:CAA67770.1};
RX   PubMed=8945543;
RA   Langford P.R., Loynds B.M., Kroll J.S.;
RT   "Cloning and molecular characterization of Cu,Zn superoxide dismutase from
RT   Actinobacillus pleuropneumoniae.";
RL   Infect. Immun. 64:5035-5041(1996).
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DR   EMBL; X99396; CAA67770.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59134; -.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:CAA67770.1}.
FT   DOMAIN          3..49
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01118"
FT   NON_TER         61
FT                   /evidence="ECO:0000313|EMBL:CAA67770.1"
SQ   SEQUENCE   61 AA;  6682 MW;  8BDA67FE267310AA CRC64;
     MQNVGFIGWR GMVGSVLMDR MVQENDFANI NPIFFTTSQA GQKAPVFAGK DAGELKNAFD
     I
//
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