ID A0A087DJ61_9BIFI Unreviewed; 364 AA.
AC A0A087DJ61;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KFI95561.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:KFI95561.1};
GN ORFNames=BSCA_0593 {ECO:0000313|EMBL:KFI95561.1};
OS Bifidobacterium scardovii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI95561.1, ECO:0000313|Proteomes:UP000029033};
RN [1] {ECO:0000313|EMBL:KFI95561.1, ECO:0000313|Proteomes:UP000029033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI95561.1,
RC ECO:0000313|Proteomes:UP000029033};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KFI95561.1}.
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DR EMBL; JGZO01000002; KFI95561.1; -; Genomic_DNA.
DR RefSeq; WP_033517207.1; NZ_JGZO01000002.1.
DR AlphaFoldDB; A0A087DJ61; -.
DR STRING; 158787.BSCA_0593; -.
DR GeneID; 85166735; -.
DR eggNOG; COG0136; Bacteria.
DR OrthoDB; 9805684at2; -.
DR Proteomes; UP000029033; 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:0050661; F:NADP 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; IPR005676; Asp_semi-ald_DH_pep-lack.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR NCBIfam; TIGR00978; asd_EA; 1.
DR PANTHER; PTHR46718; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR46718:SF1; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 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 4: Predicted;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KFI95561.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029033}.
FT DOMAIN 6..138
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 158
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 364 AA; 40449 MW; 3381B3BB7955CB5E CRC64;
MSEKLKVGIL GATGMVGQRF LTLLENHPWF EVVTLAASAH SAGKTYEEAV GDRWKMETPM
PEYAKHMVVV DGDDAEAVAA NVDFMFSAVN MPKDQIRAIE ERYAKTETPV VSNNSAHRWT
PDVPMVVPEI NPEHFAVIEH QRKRLGTTRG FIAVKPNCSI QAYTPALAAW KEFEPREVVV
STYQAISGAG KTFKDWPEMM GNIIPFISGE EAKSEKEPLK VFGHVDAEKG EIVPFDGPLR
ITSQCIRVPV LNGHTATVFL NFGKKATKEE LIDRLVNYTS ETARLELPHA PKQFIQYLTE
DDRPQVKLDV DYEGGMGVSI GRLREDSIFD WKFVGLAHNT LRGAAGGALE CAEMLKALGY
ITKK
//
