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Database: UniProt
Entry: X4ZLL4_9BACL
LinkDB: X4ZLL4_9BACL
Original site: X4ZLL4_9BACL 
ID   X4ZLL4_9BACL            Unreviewed;       361 AA.
AC   X4ZLL4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:AHV98157.1};
DE            EC=1.2.1.11 {ECO:0000313|EMBL:AHV98157.1};
GN   ORFNames=PSAB_16250 {ECO:0000313|EMBL:AHV98157.1};
OS   Paenibacillus sabinae T27.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV98157.1, ECO:0000313|Proteomes:UP000019772};
RN   [1] {ECO:0000313|EMBL:AHV98157.1, ECO:0000313|Proteomes:UP000019772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T27 {ECO:0000313|EMBL:AHV98157.1,
RC   ECO:0000313|Proteomes:UP000019772};
RX   PubMed=24651173;
RA   Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA   Chen X., Cheng Q., Chen S., Li J.;
RT   "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing Paenibacillus
RT   spp.: Organization, Evolution and Expression of the Nitrogen Fixation
RT   Genes.";
RL   PLoS Genet. 10:E1004231-E1004231(2014).
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DR   EMBL; CP004078; AHV98157.1; -; Genomic_DNA.
DR   RefSeq; WP_025335654.1; NZ_CP004078.1.
DR   AlphaFoldDB; X4ZLL4; -.
DR   STRING; 1268072.PSAB_16250; -.
DR   KEGG; psab:PSAB_16250; -.
DR   PATRIC; fig|1268072.3.peg.3359; -.
DR   eggNOG; COG0136; Bacteria.
DR   HOGENOM; CLU_049966_1_0_9; -.
DR   OrthoDB; 9805684at2; -.
DR   Proteomes; UP000019772; Chromosome.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP 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; 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   ECO:0000313|EMBL:AHV98157.1}.
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        251
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ   SEQUENCE   361 AA;  39764 MW;  38257D66B45BF2B6 CRC64;
     MTEKLRAGIV GGTGMVGQRF IALLENHPWF QVTAIAASAN SAGKTYEESV KGRWKLSTPM
     PESVKHIPVQ DASRVEEVAA GVDLIFCAVD MKKNEIQALE EAYAKAGVPV ISNNSAHRWT
     PDVPMVVPEI NPEHLEVIAA QRKRLGTETG FIAVKPNCSI QSYVPMLNAL RGFKPTQVVA
     STYQAISGAG KTFTDWPEML DNVIPYIGGE EEKSEQEPLR IWGTVEDGQI VKASAPHITT
     QCIRVPVTDG HLATVFVSFE NKPSKEDILE SWKNYKGRPQ ELELPSAPKQ FITYFEEENR
     PQTNLDRDIE NGMGISAGRL REDSLYDFKF VGLSHNTLRG AAGGAVLIAE LLKAEGYITK
     R
//
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