ID E5ETF2_9VIBR Unreviewed; 230 AA.
AC E5ETF2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Putative aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:ADQ56129.1};
DE Flags: Fragment;
GN Name=asd {ECO:0000313|EMBL:ADQ56129.1};
OS Vibrio sp. K0606-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=593508 {ECO:0000313|EMBL:ADQ56129.1};
RN [1] {ECO:0000313|EMBL:ADQ56129.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K0606-41 {ECO:0000313|EMBL:ADQ56129.1};
RX PubMed=21075874; DOI=10.1128/AEM.02062-10;
RA Keymer D.P., Boehm A.B.;
RT "Recombination shapes the structure of an environmental Vibrio cholerae
RT population.";
RL Appl. Environ. Microbiol. 77:537-544(2011).
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HM009542; ADQ56129.1; -; Genomic_DNA.
DR AlphaFoldDB; E5ETF2; -.
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 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;
FT DOMAIN 2..117
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADQ56129.1"
FT NON_TER 230
FT /evidence="ECO:0000313|EMBL:ADQ56129.1"
SQ SEQUENCE 230 AA; 25447 MW; 189DDB54259CF385 CRC64;
YNVAILGATG AVGETILDVL QERKFPVGEI FLLASERSEG KTYRFNGKTV RVQNVEEFDW
SQAHIALFSA GGELSEKWAP IAADEGVIVI DNTSHFRYEY DIPLVVPEVN PEAIAEFRNR
NIIANPNCST IQMLVALKPI HDAVGIERIN VSTYQSVSGA GKAGIDELAG QTAKLLNGLP
ADKKQFSQQI AFNCIPQIDQ MMENGYTKEE MKMVWETQKI FNDPSITVNP
//
