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Database: UniProt
Entry: A0A0G1TD98_9BACT
LinkDB: A0A0G1TD98_9BACT
Original site: A0A0G1TD98_9BACT 
ID   A0A0G1TD98_9BACT        Unreviewed;        95 AA.
AC   A0A0G1TD98;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KKU79807.1};
DE   Flags: Fragment;
GN   ORFNames=UY05_C0021G0006 {ECO:0000313|EMBL:KKU79807.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWA2_47_7.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619058 {ECO:0000313|EMBL:KKU79807.1, ECO:0000313|Proteomes:UP000034737};
RN   [1] {ECO:0000313|EMBL:KKU79807.1, ECO:0000313|Proteomes:UP000034737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKU79807.1}.
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DR   EMBL; LCON01000021; KKU79807.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1TD98; -.
DR   Proteomes; UP000034737; Unassembled WGS sequence.
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:SF2; 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;
FT   DOMAIN          4..95
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   NON_TER         95
FT                   /evidence="ECO:0000313|EMBL:KKU79807.1"
SQ   SEQUENCE   95 AA;  10033 MW;  E3DE149EF0478850 CRC64;
     MSKNVAIIGA TGAVGKEIIH CLDALKFPVQ KLRLVASEKS TGKKCDTPFG SITLEVAGED
     VFKESDVAIF SAGGDISKEL APMAKRHNCL VIDNS
//
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