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
//