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Database: UniProt
Entry: A0A1C6NGR1_9NEIS
LinkDB: A0A1C6NGR1_9NEIS
Original site: A0A1C6NGR1_9NEIS 
ID   A0A1C6NGR1_9NEIS        Unreviewed;       337 AA.
AC   A0A1C6NGR1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:SCK29957.1};
GN   ORFNames=PSELUDRAFT_3708 {ECO:0000313|EMBL:SCK29957.1};
OS   Vogesella sp. LIG4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1192162 {ECO:0000313|EMBL:SCK29957.1, ECO:0000313|Proteomes:UP000198213};
RN   [1] {ECO:0000313|EMBL:SCK29957.1, ECO:0000313|Proteomes:UP000198213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LIG4 {ECO:0000313|Proteomes:UP000198213};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; LT607802; SCK29957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6NGR1; -.
DR   OrthoDB; 9805684at2; -.
DR   Proteomes; UP000198213; Chromosome i.
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   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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   PANTHER; PTHR46278:SF2; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198213}.
FT   DOMAIN          6..121
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        132
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT   ACT_SITE        244
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ   SEQUENCE   337 AA;  35925 MW;  5C5A077BE0162030 CRC64;
     MSEAIRVAVV GATNLVGQAV LELLAERELP IERVYALDVA DKEGESAYYG NLELDVLAVE
     EFDFANVALV IFVAGTALSR QYVQAARAAG AAVVDFSAAY RQADDVPLYA PRINDKQLDD
     LGEAPLVSIP NCTVTPLAQA LATLQAAGLQ RVSVTTFQSV SGSGQAALEE LASQTTALFS
     QRDAEMEVFP KRIAFNVLPL IGSVDEQGVS EEELSVEQEV RKLLAQPALV IEASCVRVPV
     FFGHGWAVSV ESADALSADK ARELFAAAGL QVVDDPAGDM PYVTPLEASG NEAVWVSRVR
     RQGRALQFWL AADNIRAAIA HNCVATAAAL MKRGYFA
//
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