ID Q9F0T9_NEIEL Unreviewed; 117 AA.
AC Q9F0T9;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Aspartate b-semialdehyde dehydrogenase {ECO:0000313|EMBL:AAG34297.1};
DE Flags: Fragment;
OS Neisseria elongata.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=495 {ECO:0000313|EMBL:AAG34297.1};
RN [1] {ECO:0000313|EMBL:AAG34297.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 25295 {ECO:0000313|EMBL:AAG34297.1};
RA Lansac N., Picard F.J., Menard C., Ouellette M., Roy P.H., Bergeron M.G.;
RT "PCR-based assays specific for Neisseria spp. and Neisseria meningitidis.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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DR EMBL; AF205570; AAG34297.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F0T9; -.
DR GO; GO:0051287; F:NAD 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 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 PANTHER; PTHR46278:SF4; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..115
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAG34297.1"
FT NON_TER 117
FT /evidence="ECO:0000313|EMBL:AAG34297.1"
SQ SEQUENCE 117 AA; 12871 MW; 7A86B13C3706E0D6 CRC64;
WRGMVGSVLM QRMKEENDFA HIPEAFFFTT SNVGGAAPDF GQAAKTLLDA NDVAELAKMD
IIVTCQGGDY TKSVFQPLRD SGWNGYWIDA ASSLRMKDDA IIVLDPVNRN VIDNGLK
//