DHAS_SALTY
ID DHAS_SALTY Reviewed; 368 AA.
AC P0A1F8; O30706;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE Short=ASA dehydrogenase;
DE Short=ASADH;
DE EC=1.2.1.11;
DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase;
GN Name=asd; OrderedLocusNames=STM3539;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Galan J., Antoine G., Curtiss R. III;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP DISRUPTION PHENOTYPE, AND BIOTECHNOLOGY.
RX PubMed=2227450; DOI=10.1016/0378-1119(90)90464-3;
RA Galan J.E., Nakayama K., Curtiss R. III;
RT "Cloning and characterization of the asd gene of Salmonella typhimurium:
RT use in stable maintenance of recombinant plasmids in Salmonella vaccine
RT strains.";
RL Gene 94:29-35(1990).
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:0000250}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 2/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have an obligate
CC requirement for diaminopimelic acid (DAP) and undergo lysis in
CC environments deprived of DAP. {ECO:0000269|PubMed:2227450}.
CC -!- BIOTECHNOLOGY: Vaccine strains for Salmonella typhimurium were
CC successfully produced using strains with mutations in the asd gene.
CC {ECO:0000269|PubMed:2227450}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB69392.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF015781; AAB69392.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL22399.1; -; Genomic_DNA.
DR RefSeq; NP_462440.1; NC_003197.2.
DR RefSeq; WP_000799940.1; NC_003197.2.
DR AlphaFoldDB; P0A1F8; -.
DR SMR; P0A1F8; -.
DR STRING; 99287.STM3539; -.
DR PaxDb; P0A1F8; -.
DR EnsemblBacteria; AAL22399; AAL22399; STM3539.
DR GeneID; 1255062; -.
DR KEGG; stm:STM3539; -.
DR PATRIC; fig|99287.12.peg.3741; -.
DR HOGENOM; CLU_066397_0_0_6; -.
DR OMA; MFDVPDE; -.
DR PhylomeDB; P0A1F8; -.
DR BioCyc; SENT99287:STM3539-MON; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02121; ASADH; 1.
DR InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR InterPro; IPR011534; Asp_ADH_gamma-type.
DR InterPro; IPR012080; Asp_semialdehyde_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR PANTHER; PTHR46278:SF4; PTHR46278:SF4; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01745; asd_gamma; 1.
DR PROSITE; PS01103; ASD; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Diaminopimelate biosynthesis; Lysine biosynthesis;
KW Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome;
KW Threonine biosynthesis.
FT CHAIN 1..368
FT /note="Aspartate-semialdehyde dehydrogenase"
FT /id="PRO_0000141373"
FT ACT_SITE 136
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 10..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 37..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 136
FT /note="S-cysteinyl cysteine; in inhibited form"
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 40136 MW; 08BFB3E98029A677 CRC64;
MKNVGFIGWR GMVGSVLMQR MVEERDFDAI RPVFFSTSQF GQAAPTFGDT STGTLQDAFD
LDALKALDII VTCQGGDYTN EIYPKLRESG WQGYWIDAAS TLRMKDDAII ILDPVNQDVI
TDGLNNGVKT FVGGNCTVSL MLMSLGGLFA HNLVDWVSVA TYQAASGGGA RHMRELLTQM
GQLYGHVADE LATPSSAILD IERKVTALTR SGELPVDNFG VPLAGSLIPW IDKQLDNGQS
REEWKGQAET NKILNTASVI PVDGLCVRVG ALRCHSQAFT IKLKKEVSIP TVEELLAAHN
PWAKVVPNDR DITMRELTPA AVTGTLTTPV GRLRKLNMGP EFLSAFTVGD QLLWGAAEPL
RRMLRQLA
