ID D4LEM4_RUMC1 Unreviewed; 359 AA.
AC D4LEM4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Aspartate semialdehyde dehydrogenase {ECO:0000313|EMBL:CBL18069.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:CBL18069.1};
GN OrderedLocusNames=RUM_20430 {ECO:0000313|EMBL:CBL18069.1};
OS Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / KCTC 15320 /
OS 18P13).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL18069.1, ECO:0000313|Proteomes:UP000007054};
RN [1] {ECO:0000313|Proteomes:UP000007054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18848 / JCM 17042 / 18P13
RC {ECO:0000313|Proteomes:UP000007054};
RA Pajon A., Turner K., Parkhill J., Bernalier A.;
RT "The genome sequence of Ruminococcus sp. 18P13.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FP929052; CBL18069.1; -; Genomic_DNA.
DR RefSeq; WP_015558975.1; NZ_BBEP01000006.1.
DR AlphaFoldDB; D4LEM4; -.
DR STRING; 213810.RUM_20430; -.
DR GeneID; 83156707; -.
DR KEGG; rch:RUM_20430; -.
DR PATRIC; fig|213810.4.peg.1930; -.
DR HOGENOM; CLU_049966_1_0_9; -.
DR OrthoDB; 9805684at2; -.
DR BioCyc; RCHA213810:RUM_RS09910-MONOMER; -.
DR Proteomes; UP000007054; 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:CBL18069.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007054}.
FT DOMAIN 5..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 359 AA; 39950 MW; B2D915A91910BD0C CRC64;
MKQYNVGIIG ATGMVGQRFA TLLENHPWFR VKVLAASPRS AGKTYEEAVG SRWAMTTPMP
AAMKDMIMMD ATADIEKIAS QVDFVFCAVD MKKDEIKKLE EAYAKAECPV VSNNSANRFT
PDVPMVVPEI NPEHIEIIDA QRKRLGTKRG FIAVKSNCSI QSYVPALHPL RKYGLKHVLA
CTYQAISGAG KTFKTWPEMV DNLIPYIGGE EEKSEQEPLK VWGTIENNQI VKTATPSITT
QCLRVPVQDG HTAAVFVSFE NKPSKEEILQ CWKAFSGVPQ ELELPSAPKQ FLHYFEENDR
PQAKLDRNLE NGMAISIGRL REDTQYDYKF VCLSHNTLRG AAGGGVLLAE LLAAKGYFD
//
