ID A0A1I5YRS1_9FIRM Unreviewed; 361 AA.
AC A0A1I5YRS1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:SFQ46745.1};
GN ORFNames=SAMN04487928_1544 {ECO:0000313|EMBL:SFQ46745.1};
OS Butyrivibrio proteoclasticus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=43305 {ECO:0000313|EMBL:SFQ46745.1, ECO:0000313|Proteomes:UP000182624};
RN [1] {ECO:0000313|Proteomes:UP000182624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P18 {ECO:0000313|Proteomes:UP000182624};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOXO01000054; SFQ46745.1; -; Genomic_DNA.
DR RefSeq; WP_074892087.1; NZ_FOXO01000054.1.
DR AlphaFoldDB; A0A1I5YRS1; -.
DR eggNOG; COG0136; Bacteria.
DR OrthoDB; 9805684at2; -.
DR Proteomes; UP000182624; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP 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 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}.
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 251
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 361 AA; 40212 MW; CA3DBB89652FDBF7 CRC64;
MSDKLKVAVL GGTGMVGQRF IDIINNHPWF EVTTIAASPR SAGQTYEEAV GKRWKMDNPI
PESVKNIVVK DVTDVKGVSE DVDFVLSAVN MSKDEIKHIE EEYAKTETPV VSNNSAHRWT
PDVPMIIPEI NPEHMDVIEF QKKRLGTTNG FIAVKPNCSI QSYTPALTAW KEYEPYEVVA
TTYQAISGAG KNFEEWPEMV GNVIPFISGE EEKSEKEPLR IWGKIENGVI VPADDVKITC
QCIRIPVLYG HTAAAFVKFR KEVSKEELIE KLVNFSGLPQ KLQLPSAPKQ FIQYMQDDNR
PQVALDVNYE GGMGVSIGRL REDTIYDYKF VGLSHNTLRG AAGGAVECAE LLKASGYINK
K
//
