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
//