ID T2SKZ3_HELPX Unreviewed; 209 AA.
AC T2SKZ3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|ARBA:ARBA00012086};
DE EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086};
DE Flags: Fragment;
GN ORFNames=L932_02670 {ECO:0000313|EMBL:EQD93401.1};
OS Helicobacter pylori PZ5026.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1337392 {ECO:0000313|EMBL:EQD93401.1, ECO:0000313|Proteomes:UP000015722};
RN [1] {ECO:0000313|EMBL:EQD93401.1, ECO:0000313|Proteomes:UP000015722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PZ5026 {ECO:0000313|EMBL:EQD93401.1,
RC ECO:0000313|Proteomes:UP000015722};
RX PubMed=24051318;
RA Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.;
RT "Draft Genome Sequences of Helicobacter pylori Strains Isolated from
RT Regions of Low and High Gastric Cancer Risk in Colombia.";
RL Genome Announc. 1:e00736-13(2013).
CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC {ECO:0000256|ARBA:ARBA00003294}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-
CC hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O;
CC Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000594};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC {ECO:0000256|ARBA:ARBA00005120}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQD93401.1}.
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DR EMBL; ASYT01000088; EQD93401.1; -; Genomic_DNA.
DR RefSeq; WP_021173175.1; NZ_ASYT01000088.1.
DR AlphaFoldDB; T2SKZ3; -.
DR PATRIC; fig|1337392.3.peg.538; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000015722; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd00950; DHDPS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00418; DapA; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005263; DapA.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR NCBIfam; TIGR00674; dapA; 1.
DR PANTHER; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EQD93401.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EQD93401.1"
SQ SEQUENCE 209 AA; 23385 MW; 63811390C7A249D1 CRC64;
SLSLAKFAQK IGADAILCVS PYYNRPTQQG LFEHYKTIAQ SVEIPVMLYD VPSRTGVSIE
VPTALKLFRE VPNIKAIKEA SGSLKRVTEL HYYEKDFKIF SGEDSLNHSI MFSGGCGVIS
VTGNLMPNLI SQMVNCTLNL EYQQALEIQN KLFNLHQALF VETNPIPIKM AMHLAGLIEN
PSYRLPLVPP SKETIKLLEK TLQQYEVIA
//
