ID L0MVF3_9ENTR Unreviewed; 368 AA.
AC L0MVF3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN Name=asd {ECO:0000313|EMBL:AGC03845.1};
GN ORFNames=BCHRO640_611 {ECO:0000313|EMBL:AGC03845.1};
OS Candidatus Blochmannia chromaiodes str. 640.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=1240471 {ECO:0000313|EMBL:AGC03845.1, ECO:0000313|Proteomes:UP000011067};
RN [1] {ECO:0000313|EMBL:AGC03845.1, ECO:0000313|Proteomes:UP000011067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=640 {ECO:0000313|EMBL:AGC03845.1,
RC ECO:0000313|Proteomes:UP000011067};
RX PubMed=23475937; DOI=10.1093/gbe/evt033;
RA Williams L.E., Wernegreen J.J.;
RT "Sequence context of indel mutations and their effect on protein evolution
RT in a bacterial endosymbiont.";
RL Genome Biol. Evol. 5:599-605(2013).
CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
CC semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-
CC 4-phosphate. {ECO:0000256|ARBA:ARBA00002492}.
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; CP003903; AGC03845.1; -; Genomic_DNA.
DR RefSeq; WP_015344813.1; NC_020075.1.
DR AlphaFoldDB; L0MVF3; -.
DR KEGG; bchr:BCHRO640_611; -.
DR PATRIC; fig|1240471.4.peg.571; -.
DR HOGENOM; CLU_066397_0_0_6; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000011067; 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:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
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; IPR011534; Asp_ADH_gamma-type.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR NCBIfam; TIGR01745; asd_gamma; 1.
DR PANTHER; PTHR46278:SF4; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 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;
FT DOMAIN 3..123
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 136
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 368 AA; 41096 MW; 9B2F4D75C6B2ABC4 CRC64;
MKNIGFVGWR GMVGSVLMNR MKEENDFNYF HSIFLSTSQI GEHAPNIQAS QELLLQDACN
IDLLDSLDII ITCQGSAYSK IIYPKLRKIG WTGYWIDSAS FLRMNDDAII VLDPVNQVLI
KQSINNGIKT FVGGNCTVSL MLMSLGGLFA HNLIEWVFAS TYQAASGCGA RAMRELLIQM
GQVYNIVTDL LTSPSMAILD IEHIITKFSK TDSLLVDCFK VPLIGNVIPW IGDDMYNGQT
QEEWKGQAET NKILNTSKII TVDSLCVRVG ALRCHSQAFV LKLKKDICLK EIEELLQSHN
KWVEVISNDV TQSLNKLTPV MVSGTLKIPI GRLRKLHAGN KYISAFSVGD QLLWGAAEPL
RRILRQLL
//
