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Database: UniProt
Entry: A0A1W1UMP8_9PAST
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Original site: A0A1W1UMP8_9PAST 
ID   A0A1W1UMP8_9PAST        Unreviewed;       325 AA.
AC   A0A1W1UMP8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:SMB81984.1};
GN   ORFNames=SAMN05660772_01968 {ECO:0000313|EMBL:SMB81984.1};
OS   Pasteurella testudinis DSM 23072.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=1122938 {ECO:0000313|EMBL:SMB81984.1, ECO:0000313|Proteomes:UP000192408};
RN   [1] {ECO:0000313|EMBL:SMB81984.1, ECO:0000313|Proteomes:UP000192408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23072 {ECO:0000313|EMBL:SMB81984.1,
RC   ECO:0000313|Proteomes:UP000192408};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; FWWV01000008; SMB81984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W1UMP8; -.
DR   STRING; 1122938.SAMN05660772_01968; -.
DR   Proteomes; UP000192408; 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   PIRSF; PIRSF000148; ASA_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;
FT   DOMAIN          50..118
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01118"
SQ   SEQUENCE   325 AA;  36081 MW;  AB8126F1BEE33AB0 CRC64;
     MQTDLNIVIA AEFELAEKIA ELLEQSILPT AKLSVAEIYP FNEEQGLRFH NRSVEQQNIE
     EVDWSDKQYL FFAGEAKHAP YVARAADSGC VVIDLAAVCA TLADVPLIVP GFNDSQLAEL
     RNRNIVSLAD PQISQLVLTC GEILVGGEIN RLLVTSMLPA SYVNAEQVKK LAGQTARLLN
     GISLDDGEPR LAFDVAPFKG NSSERLLRQF QKIIPNSEIQ LLIHQVQSAV FYGLAQQVTA
     LSDYQSDSAH WQTVWQQNPL LALHQDEIIT PVSNGEKYQE QDSIHLSDVI VLENGIQFWS
     VCDEQRFSLA LLAIKLAESA YQQGY
//
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