ID A0A0T7RTS7_SALET Unreviewed; 368 AA.
AC A0A0T7RTS7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120, ECO:0000256|HAMAP-Rule:MF_02121};
DE Short=ASA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
DE Short=ASADH {ECO:0000256|HAMAP-Rule:MF_02121};
DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120, ECO:0000256|HAMAP-Rule:MF_02121};
DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
GN Name=asd {ECO:0000256|HAMAP-Rule:MF_02121,
GN ECO:0000313|EMBL:SUE45642.1};
GN ORFNames=B7N00_17495 {ECO:0000313|EMBL:EDG5018742.1}, B7N01_10810
GN {ECO:0000313|EMBL:EDG4994915.1}, B7N35_03535
GN {ECO:0000313|EMBL:EDG5125102.1}, B7N72_07570
GN {ECO:0000313|EMBL:EDG5369963.1}, B7N78_06560
GN {ECO:0000313|EMBL:EDG5279438.1}, B7N80_01400
GN {ECO:0000313|EMBL:EDG5287045.1}, B7N84_12000
GN {ECO:0000313|EMBL:EDG5267056.1}, DRU31_07355
GN {ECO:0000313|EMBL:EBS2452142.1}, E0916_12465
GN {ECO:0000313|EMBL:ECF1446762.1}, EJV93_15130
GN {ECO:0000313|EMBL:ECA2722520.1}, ERS008202_01218
GN {ECO:0000313|EMBL:CNT85501.1}, EWC73_02995
GN {ECO:0000313|EMBL:ECE8535194.1}, G0B02_04090
GN {ECO:0000313|EMBL:HAC6378315.1}, G0D18_07420
GN {ECO:0000313|EMBL:HAC6680492.1}, G2206_10555
GN {ECO:0000313|EMBL:HAE0435200.1}, NCTC5754_00424
GN {ECO:0000313|EMBL:SUE45642.1};
OS Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE45642.1, ECO:0000313|Proteomes:UP000254190};
RN [1] {ECO:0000313|EMBL:CNT85501.1, ECO:0000313|Proteomes:UP000039541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3476 {ECO:0000313|EMBL:CNT85501.1,
RC ECO:0000313|Proteomes:UP000039541};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HAC6378315.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6378315.1}, M123
RC {ECO:0000313|EMBL:HAC6680492.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0435200.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:SUE45642.1, ECO:0000313|Proteomes:UP000254190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE45642.1,
RC ECO:0000313|Proteomes:UP000254190};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:HAC6378315.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6378315.1}, M123
RC {ECO:0000313|EMBL:HAC6680492.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0435200.1};
RG NCBI Pathogen Detection Project;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:ECE8535194.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=136768 {ECO:0000313|EMBL:EDG4994915.1}, 138330
RC {ECO:0000313|EMBL:EDG5287045.1}, 143652
RC {ECO:0000313|EMBL:EDG5369963.1}, 273631
RC {ECO:0000313|EMBL:EDG5018742.1}, 330535
RC {ECO:0000313|EMBL:EDG5267056.1}, 333944
RC {ECO:0000313|EMBL:EDG5279438.1}, 337042
RC {ECO:0000313|EMBL:EDG5125102.1}, 387147
RC {ECO:0000313|EMBL:EBS2452142.1}, 470200
RC {ECO:0000313|EMBL:ECE8535194.1}, 598023
RC {ECO:0000313|EMBL:ECA2722520.1}, and 692616
RC {ECO:0000313|EMBL:ECF1446762.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|HAMAP-
CC Rule:MF_02121}.
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, ECO:0000256|HAMAP-
CC Rule:MF_02121};
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, ECO:0000256|HAMAP-Rule:MF_02121}.
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, ECO:0000256|HAMAP-Rule:MF_02121}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097,
CC ECO:0000256|HAMAP-Rule:MF_02121}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_02121}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010584, ECO:0000256|HAMAP-Rule:MF_02121}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}.
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DR EMBL; CQPC01000011; CNT85501.1; -; Genomic_DNA.
DR EMBL; AAGUWJ010000004; EBS2452142.1; -; Genomic_DNA.
DR EMBL; AAHTVM010000007; ECA2722520.1; -; Genomic_DNA.
DR EMBL; AAIJHK010000002; ECE8535194.1; -; Genomic_DNA.
DR EMBL; AAIKGE010000006; ECF1446762.1; -; Genomic_DNA.
DR EMBL; AAMEJW010000009; EDG4994915.1; -; Genomic_DNA.
DR EMBL; AAMEJY010000013; EDG5018742.1; -; Genomic_DNA.
DR EMBL; AAMEKY010000002; EDG5125102.1; -; Genomic_DNA.
DR EMBL; AAMEMC010000005; EDG5267056.1; -; Genomic_DNA.
DR EMBL; AAMEMH010000003; EDG5279438.1; -; Genomic_DNA.
DR EMBL; AAMEML010000001; EDG5287045.1; -; Genomic_DNA.
DR EMBL; AAMEMP010000005; EDG5369963.1; -; Genomic_DNA.
DR EMBL; DAAMEZ010000002; HAC6378315.1; -; Genomic_DNA.
DR EMBL; DAAMHM010000004; HAC6680492.1; -; Genomic_DNA.
DR EMBL; DAAQQK010000009; HAE0435200.1; -; Genomic_DNA.
DR EMBL; UGVQ01000002; SUE45642.1; -; Genomic_DNA.
DR RefSeq; WP_000799940.1; NZ_WFIN01000005.1.
DR AlphaFoldDB; A0A0T7RTS7; -.
DR SMR; A0A0T7RTS7; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000039541; Unassembled WGS sequence.
DR Proteomes; UP000254190; Unassembled WGS sequence.
DR Proteomes; UP000839929; Unassembled WGS sequence.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 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;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW ECO:0000256|HAMAP-Rule:MF_02121};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW Rule:MF_02121};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_02121}; NADP {ECO:0000256|HAMAP-Rule:MF_02121};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121,
KW ECO:0000313|EMBL:SUE45642.1};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP-
KW Rule:MF_02121}.
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|HAMAP-Rule:MF_02121,
FT ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121,
FT ECO:0000256|PIRSR:PIRSR000148-1"
FT BINDING 10..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 37..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 103
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 166..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 245
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
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
//
