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Database: UniProt
Entry: U2B0K4_9PSED
LinkDB: U2B0K4_9PSED
Original site: U2B0K4_9PSED 
ID   U2B0K4_9PSED            Unreviewed;       336 AA.
AC   U2B0K4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:ERI50637.1};
DE            EC=1.2.1.11 {ECO:0000313|EMBL:ERI50637.1};
GN   ORFNames=N878_08235 {ECO:0000313|EMBL:ERI50637.1};
OS   Pseudomonas sp. EGD-AK9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1386078 {ECO:0000313|EMBL:ERI50637.1, ECO:0000313|Proteomes:UP000016488};
RN   [1] {ECO:0000313|EMBL:ERI50637.1, ECO:0000313|Proteomes:UP000016488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EGD-Ak9 {ECO:0000313|Proteomes:UP000016488};
RA   Kapley A., Sagarkar S., Bhardwaj P., Qureshi A., Khardenavis A.,
RA   Purohit H.J.;
RT   "Indian agricultural soil isolates capable of pesticide degradation.";
RL   Submitted (AUG-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:ERI50637.1}.
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DR   EMBL; AVOF01000551; ERI50637.1; -; Genomic_DNA.
DR   RefSeq; WP_021445393.1; NZ_AVOF01000551.1.
DR   AlphaFoldDB; U2B0K4; -.
DR   PATRIC; fig|1386078.3.peg.3735; -.
DR   OrthoDB; 9805684at2; -.
DR   Proteomes; UP000016488; Unassembled WGS sequence.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; 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:0000313|EMBL:ERI50637.1}.
FT   DOMAIN          6..120
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
SQ   SEQUENCE   336 AA;  35394 MW;  F164CCB9995F2C40 CRC64;
     MSQSFNIALV GATGSIGEAL VELLEERDFP VKELHLLASS ESAGQSLSFR GRQVRVRSLD
     AFDFAQVQLA FFAAGADVTR AQHERVLAAG CSLIDLSAAL PLSQAPCVLP EAGLDGLPAR
     HAPWLLSSPT PCAVATALVL TALRPLLQPR QVQLTAMLAA STLGRSGVQE LARQTAELLN
     GRPLEPKGLD RQVAFNLLAQ VGALDEQGHA ELEKRLASEL QQLLGVPDLP VSATCALAPV
     FFGDSLALGV QVDGEVDVAA VSRLLEAAPG IELVEAGDYP TAVGDAVGQD QVYVGRVRSG
     VSDPRQLNLW IASDNVRKGA ALNAVQIAEL LIKHYL
//
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