ID A0A0D5NNY0_9BACL Unreviewed; 347 AA.
AC A0A0D5NNY0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:AJY76870.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:AJY76870.1};
GN ORFNames=VN24_22800 {ECO:0000313|EMBL:AJY76870.1};
OS Paenibacillus beijingensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY76870.1, ECO:0000313|Proteomes:UP000032633};
RN [1] {ECO:0000313|EMBL:AJY76870.1, ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY76870.1,
RC ECO:0000313|Proteomes:UP000032633};
RX PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA Kwak Y., Shin J.H.;
RT "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT 24997(T)), a novel rhizobacterium from jujube garden soil.";
RL J. Biotechnol. 206:75-76(2015).
RN [2] {ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011058; AJY76870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D5NNY0; -.
DR STRING; 1126833.VN24_22800; -.
DR KEGG; pbj:VN24_22800; -.
DR PATRIC; fig|1126833.4.peg.5013; -.
DR HOGENOM; CLU_049966_1_0_9; -.
DR Proteomes; UP000032633; 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:AJY76870.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032633}.
FT DOMAIN 1..124
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 144
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 347 AA; 38235 MW; F81E59A833488DB2 CRC64;
MVGQRFVQLL DQHPWFKVTA IAASAGSAGK TYEESVQGRW KLQGPIPEEV KNIVVQDASK
VEEVAGGVDF IFCAVDMKKN EIQALEEAYA KTGTPVISNN SAHRWTPDIP MVIPEINPGH
IEVIAAQRKR LGTATGFIAV KPNCSIQSYV PALHALLDYK PTKVVASTYQ AISGAGKNFT
DWPEMLDNVI PYIGGEEEKS EQEPLRIWGT IENGEIIKAS APLITTQCIR VPVTDGHLAT
VFASFENTPS KEEILDRWLN FKGRPQELGL PSAPKQFITY FEEENRPQTK LDRDIERGMG
VSVGRLREDS IYDFKFVGLS HNTLRGAAGG AVLIAELLKA EGYIQAK
//
