ID Q5FGN4_EHRRG Unreviewed; 88 AA.
AC Q5FGN4;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:CAI28347.1};
GN Name=asd {ECO:0000313|EMBL:CAI28347.1};
GN OrderedLocusNames=ERGA_CDS_08950 {ECO:0000313|EMBL:CAI28347.1};
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409 {ECO:0000313|EMBL:CAI28347.1, ECO:0000313|Proteomes:UP000000533};
RN [1] {ECO:0000313|EMBL:CAI28347.1, ECO:0000313|Proteomes:UP000000533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel {ECO:0000313|EMBL:CAI28347.1,
RC ECO:0000313|Proteomes:UP000000533};
RX PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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DR EMBL; CR925677; CAI28347.1; -; Genomic_DNA.
DR RefSeq; WP_011255942.1; NC_006831.1.
DR AlphaFoldDB; Q5FGN4; -.
DR KEGG; erg:ERGA_CDS_08950; -.
DR HOGENOM; CLU_2464183_0_0_5; -.
DR OrthoDB; 9805684at2; -.
DR Proteomes; UP000000533; Chromosome.
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 SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
FT DOMAIN 7..85
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01118"
SQ SEQUENCE 88 AA; 9496 MW; 141680330CD64D6E CRC64;
MVYKNIKIAV VDATGNVGRV ILNVLLDSKI FFNSNVVALA SKKSVGKKLS YGDAILEAQD
LGSYDFYGID IAIFSAESSI SQQYATIN
//
