ID F4LQ69_TREBD Unreviewed; 368 AA.
AC F4LQ69;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN OrderedLocusNames=Trebr_0648 {ECO:0000313|EMBL:AEE16090.1};
OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE16090.1, ECO:0000313|Proteomes:UP000006546};
RN [1] {ECO:0000313|Proteomes:UP000006546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC {ECO:0000313|Proteomes:UP000006546};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Treponema brennaborense DSM 12168.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-
CC L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001636};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00005076}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00005021}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584}.
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DR EMBL; CP002696; AEE16090.1; -; Genomic_DNA.
DR RefSeq; WP_013757809.1; NC_015500.1.
DR AlphaFoldDB; F4LQ69; -.
DR STRING; 906968.Trebr_0648; -.
DR KEGG; tbe:Trebr_0648; -.
DR eggNOG; COG0136; Bacteria.
DR HOGENOM; CLU_049966_1_0_12; -.
DR OrthoDB; 9805684at2; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000006546; 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:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000319; Asp-semialdehyde_DH_CS.
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.
DR PROSITE; PS01103; ASD; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEE16090.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546}.
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 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 368 AA; 40128 MW; A08BD932E9C43009 CRC64;
MCAHKIAVGV LGATGMVGQR YIYLLKDHPW FEVTYVAASP RSAGKKYREA VESRWLIGSD
VPAGVADLVV QDANDAKLAL GACKFVFSAL EMDKDAIKAL EAAYAAEGIP VVSNASANRW
TDDVPMLIPE INPHHLSVIA EQKKHRGWDK GFIAVKPNCS LQSYMMPIFA LQQAGYPVKR
MIVTTLQATS GAGYPGVPSF DMIDNIVPYI GGEEEKTERE VLKILGTVKD GKIENAAGPL
VAAHCNRVPV IDGHTACVSL EFDLPENKKP SLEEIERVWT AFTALPQELA LPSAPVQPII
VRHEPNRPQP RRDRENDKGM AVTIGRLRTC PVFDIRFVAL SHNTKRGAAL GGILNAELLK
AKGFFDAL
//
