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Database: UniProt
Entry: W1DIE5_KLEPN
LinkDB: W1DIE5_KLEPN
Original site: W1DIE5_KLEPN 
ID   W1DIE5_KLEPN            Unreviewed;       337 AA.
AC   W1DIE5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:CDL08415.1};
DE            EC=1.2.1.11 {ECO:0000313|EMBL:CDL08415.1};
OS   Klebsiella pneumoniae IS43.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1432552 {ECO:0000313|EMBL:CDL08415.1, ECO:0000313|Proteomes:UP000019183};
RN   [1] {ECO:0000313|EMBL:CDL08415.1, ECO:0000313|Proteomes:UP000019183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IS43 {ECO:0000313|EMBL:CDL08415.1,
RC   ECO:0000313|Proteomes:UP000019183};
RA   Barisic I., Mitteregger D., Hirschl A.M., Noehammer C., Wiesinger-Mayr H.;
RT   "Antibiotic resistance diversity of beta-lactamase producers in the General
RT   Hospital Vienna.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:CDL08415.1}.
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DR   EMBL; CBWK010000196; CDL08415.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1DIE5; -.
DR   eggNOG; COG0136; Bacteria.
DR   Proteomes; UP000019183; Unassembled WGS sequence.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; 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   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   PANTHER; PTHR46278:SF2; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   PIRSF; PIRSF000148; ASA_dh; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:CDL08415.1}.
FT   DOMAIN          6..121
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
SQ   SEQUENCE   337 AA;  36294 MW;  A6B50C73BDD77082 CRC64;
     MSEGWNIAVL GATGAVGEAL LETLAERQFP VGEIFALARN DSAGEHLRFG GKSVIVKDAA
     EFDWTQAQLA FFAAGVEASA AYVEEATNAG CLVIDLSGLF ALEPDVPLVV PDVNPFVLGD
     YRNRNLIAVP NSLTSQLLTA LKPLIDQGGL SRISVTNLLS ASGQGKKAVD ALAGQSAKLL
     NGIPIDEDDF FGRQLAFNML PLLPDREGSV REERRIVDEA RKILQDDGLM ISASVVQSPV
     FYGHAQMVSF EAMRPLAAEE ARDAFTRGED IELSEEGEFP TQVGDASGNA RLSIGCVHND
     YGMPEQIQFW SVADNVRFGG ALMAVKIAEK LIEEYLY
//
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