ID A0A0R1V7Q9_9LACO Unreviewed; 363 AA.
AC A0A0R1V7Q9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KRL99045.1};
GN ORFNames=FD50_GL000317 {ECO:0000313|EMBL:KRL99045.1};
OS Liquorilactobacillus satsumensis DSM 16230 = JCM 12392.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423801 {ECO:0000313|EMBL:KRL99045.1, ECO:0000313|Proteomes:UP000051166};
RN [1] {ECO:0000313|EMBL:KRL99045.1, ECO:0000313|Proteomes:UP000051166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16230 {ECO:0000313|EMBL:KRL99045.1,
RC ECO:0000313|Proteomes:UP000051166};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRL99045.1}.
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DR EMBL; AZFQ01000034; KRL99045.1; -; Genomic_DNA.
DR RefSeq; WP_056960498.1; NZ_AZFQ01000034.1.
DR AlphaFoldDB; A0A0R1V7Q9; -.
DR STRING; 1423801.FD50_GL000317; -.
DR PATRIC; fig|1423801.4.peg.323; -.
DR OrthoDB; 9805684at2; -.
DR Proteomes; UP000051166; 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 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 363 AA; 40012 MW; E3E88DF230B433F3 CRC64;
MSKKLKVGIL GATGMVGQRY VTLLADHPWF EVVLVAASPH SAGKTYAEAV AGRWKMSVPI
PAKVKELSVL DVNQVNLIAE QVDFVFSAVN MAKDQIRKIE EEYAKTETPV VSNNSAHRWT
PDVPMIVPEI NPEHTEVIKY QRQRLGTSRG FIAVKPNCSI QSYAPALSAW QQFEPTQVIA
TTYQAISGAG KNFEDAPEIL NNVIPFIGGE EEKSEKEPLK IWGRVDPTDG VIIPATTPVI
TSQCLRVPVL YGHTAAAFVN FKQKVTKEEL ISALESFRGV PQELQLPSAP QQFIQYLTAD
DRPQVRYDVN FEHGMGISIG RLRPDKIFDW KFVGLSHNTA RGAAGGAILC AELLKSQGYI
TAK
//
