ID F2JMY3_CELLD Unreviewed; 364 AA.
AC F2JMY3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:ADZ85898.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:ADZ85898.1};
GN OrderedLocusNames=Clole_4226 {ECO:0000313|EMBL:ADZ85898.1};
OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS RHM5) (Clostridium lentocellum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ85898.1, ECO:0000313|Proteomes:UP000008467};
RN [1] {ECO:0000313|EMBL:ADZ85898.1, ECO:0000313|Proteomes:UP000008467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC {ECO:0000313|Proteomes:UP000008467};
RX PubMed=21398547; DOI=10.1128/JB.00239-11;
RG US DOE Joint Genome Institute;
RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA Angert E.R., Currie C.R.;
RT "Complete genome sequence of the cellulose-degrading bacterium
RT Cellulosilyticum lentocellum.";
RL J. Bacteriol. 193:2357-2358(2011).
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DR EMBL; CP002582; ADZ85898.1; -; Genomic_DNA.
DR AlphaFoldDB; F2JMY3; -.
DR STRING; 642492.Clole_4226; -.
DR KEGG; cle:Clole_4226; -.
DR eggNOG; COG0136; Bacteria.
DR HOGENOM; CLU_049966_1_0_9; -.
DR Proteomes; UP000008467; 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:ADZ85898.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008467}.
FT DOMAIN 7..139
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 159
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 364 AA; 40289 MW; DF9BF1DA78CA250C CRC64;
MMEKKLKVGI VGGTGMVGQR FLALLENHPY FDVKVIAASS RSAGQTYEKA VEGRWKMSTS
IPETVKNLIV LDAAKVEEVA SQVDFIFCAV DMKKDEIKAL EEAYAKTETP VVSNNSAHRW
TPDVPMVIPE INDEHLKVIE AQRKRLGTTK GFIAVKPNCS IQSYVPMLSA LLDYEPTTVV
ASTYQAISGA GKTFKEWPEM IDNVIPYIGG EEEKSEQEPL RIWGKVENDA IVKATSPVIT
TQCIRVPVLD GHLATVFVSF KKKPTKEQIL EAWKNYKGKP QELNLPSAPK QFITYFEEDN
RPQTGLDRNT EKGMGVCVGR LREDTVYDYK FVGLSHNTVR GAAGGAVLIA ELLAAEGYIT
SKEA
//
