ID R8WVH3_9ENTR Unreviewed; 337 AA.
AC R8WVH3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=USG-1 protein {ECO:0000313|EMBL:EOQ48764.1};
GN ORFNames=WC7_03009 {ECO:0000313|EMBL:EOQ48764.1};
OS Citrobacter sp. KTE151.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=1169322 {ECO:0000313|EMBL:EOQ48764.1, ECO:0000313|Proteomes:UP000014006};
RN [1] {ECO:0000313|EMBL:EOQ48764.1, ECO:0000313|Proteomes:UP000014006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTE151 {ECO:0000313|EMBL:EOQ48764.1,
RC ECO:0000313|Proteomes:UP000014006};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Nielsen K.L., Frimodt-Moller N., Andersen P.S., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Escherichia coli KTE151.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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:EOQ48764.1}.
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; ASQK01000005; EOQ48764.1; -; Genomic_DNA.
DR RefSeq; WP_016153862.1; NZ_KB976064.1.
DR AlphaFoldDB; R8WVH3; -.
DR PATRIC; fig|1169322.3.peg.3006; -.
DR HOGENOM; CLU_049966_0_1_6; -.
DR Proteomes; UP000014006; Unassembled WGS sequence.
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;
FT DOMAIN 6..121
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
SQ SEQUENCE 337 AA; 36357 MW; 85ADA978255A8571 CRC64;
MSEGWNIAIL GATGAVGEAL LDTLAERQFP VGEIYALARN ESAGEHLRFN GKSVLVQDVV
DFDWTQAQLA FFVAGAEATA AWVEEATNAG CLVIDSSGLF ALEPDVPLVV PDVNPLVLAD
YRNRNVIAVP SSLTSQLLSA LKPLIDDGGL SRITVTNIIS ASAHGKKAVD ALAGQSAKLL
NGIPIDDDDF FGRQLAFNML PLLPDREGSV REERRIVDEV RKIMQDDGLL ISASIVQSPV
FYGHAQMVNF EALRPLAAEE ARDAFSRGED VVLSEETYIP TQVGDASGTP HLSVGCVHND
YGMPEQVQFW SVADNVRFGG ALMAVKIAEK LVQEYLY
//