ID X0PQT7_9LACO Unreviewed; 363 AA.
AC X0PQT7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KRM32558.1};
GN ORFNames=FC83_GL000425 {ECO:0000313|EMBL:KRM32558.1};
OS Agrilactobacillus composti DSM 18527 = JCM 14202.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Agrilactobacillus.
OX NCBI_TaxID=1423734 {ECO:0000313|EMBL:KRM32558.1, ECO:0000313|Proteomes:UP000051236};
RN [1] {ECO:0000313|EMBL:KRM32558.1, ECO:0000313|Proteomes:UP000051236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18527 {ECO:0000313|EMBL:KRM32558.1,
RC ECO:0000313|Proteomes:UP000051236};
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:KRM32558.1}.
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DR EMBL; AZGA01000070; KRM32558.1; -; Genomic_DNA.
DR RefSeq; WP_035453047.1; NZ_BAMK01000013.1.
DR AlphaFoldDB; X0PQT7; -.
DR STRING; 1423734.FC83_GL000425; -.
DR PATRIC; fig|1423734.3.peg.426; -.
DR eggNOG; COG0136; Bacteria.
DR OrthoDB; 9805684at2; -.
DR Proteomes; UP000051236; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051236}.
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; 40525 MW; F359D92744BAF776 CRC64;
MDEKLKVGII GATGMVGQRY ISLLENHPWF EVTTVAASPH SAGKTYEEAV NGRWRMDTPI
PEAVKNLTIL DVNDIDKVAS QVDFVFSAVN MSKDAIKKIE TEYAQTETPV VSNNSAHRWT
PDVPMVVPEI NPDHTDIIKY QRERLGTKRG FIAVKPNCSI QSYTPALSAW QQFEPYEVVA
TTYQAISGAG KTFEDWPEMK GNIIPYISGE EEKSEKEPLR IWGSIDPEKK AIVPATTPVI
TTQCVRVPIL YGHTAAAFVK FRQNPTKQEL IDALTSYHGI PQEQNLPSAP KQFIQYMTED
DRPQVQLDVN FENGMGISIG RLREDTVYDW KFIGLSHNTA RGAAGGAILL AELLKAQDYI
AKK
//
