ID A0A099TXI5_9HELI Unreviewed; 345 AA.
AC A0A099TXI5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:STQ86170.1};
GN ORFNames=LS73_008935 {ECO:0000313|EMBL:TLD98404.1}, NCTC12714_00972
GN {ECO:0000313|EMBL:STQ86170.1};
OS Helicobacter muridarum.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=216 {ECO:0000313|EMBL:STQ86170.1, ECO:0000313|Proteomes:UP000255139};
RN [1] {ECO:0000313|EMBL:TLD98404.1, ECO:0000313|Proteomes:UP000029922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST1 {ECO:0000313|EMBL:TLD98404.1,
RC ECO:0000313|Proteomes:UP000029922};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
RN [2] {ECO:0000313|EMBL:STQ86170.1, ECO:0000313|Proteomes:UP000255139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12714 {ECO:0000313|EMBL:STQ86170.1,
RC ECO:0000313|Proteomes:UP000255139};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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|HAMAP-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; UGJE01000002; STQ86170.1; -; Genomic_DNA.
DR EMBL; JRPD02000031; TLD98404.1; -; Genomic_DNA.
DR RefSeq; WP_034559746.1; NZ_UGJE01000002.1.
DR AlphaFoldDB; A0A099TXI5; -.
DR STRING; 216.LS73_10335; -.
DR OrthoDB; 9805684at2; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000029922; Unassembled WGS sequence.
DR Proteomes; UP000255139; 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; IPR012080; Asp_semialdehyde_DH.
DR InterPro; IPR005986; Asp_semialdehyde_DH_beta.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR NCBIfam; TIGR01296; asd_B; 1.
DR PANTHER; PTHR46278:SF2; 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:STQ86170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000255139};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697, ECO:0000256|HAMAP-
KW Rule:MF_02121}.
FT DOMAIN 13..130
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 139
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121,
FT ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121,
FT ECO:0000256|PIRSR:PIRSR000148-1"
FT BINDING 20..23
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 48..49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 110
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 169..170
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
FT BINDING 326
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02121"
SQ SEQUENCE 345 AA; 38716 MW; E70B9FADF1D365AD CRC64;
MLLDSKKSQK KYVVGIVGAS GAVGEELLLV LEQRNFPVER LVPLASKRSV GKSVNFCGEK
YPILETNAEV FSKENIEIAF FSAGSSISEL YANDAANAGA LVIDNTSFFR MQDDIALVVP
EVNPNDIRKD ARIIANPNCS TIQMVHVLDP LHREFEIDRV DVSTYQAVSG AGKRGMEELV
LQMQKFFAFE IDSAKSEVFQ HRIALNLIPH IDIFLDNDYT KEEMKMINES KKIMHADFEL
AATCVRVPIL RSHSESITIR FKREASAKRA REILQSADGV IVVDNPKDNL YPMPIIATDK
DDTFVGRIRE DNFDKRILHL FCVADQVRVG AATNAVRIAE KWINL
//
