DAPA_SALTY
ID DAPA_SALTY Reviewed; 292 AA.
AC Q8ZN71;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418};
DE Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418};
DE EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418};
GN Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418}; OrderedLocusNames=STM2489;
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 [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).
CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-
CC 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O; Xref=Rhea:RHEA:34171,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00418};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00418}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP-
CC Rule:MF_00418}.
CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate synthase
CC (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was
CC shown in E.coli that the product of the enzymatic reaction is not
CC dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-
CC dipicolinic acid (HTPA), and that the consecutive dehydration reaction
CC leading to DHDP is not spontaneous but catalyzed by DapB.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL21383.1; -; Genomic_DNA.
DR RefSeq; NP_461424.1; NC_003197.2.
DR RefSeq; WP_000494020.1; NC_003197.2.
DR PDB; 3G0S; X-ray; 1.85 A; A/B=1-292.
DR PDBsum; 3G0S; -.
DR AlphaFoldDB; Q8ZN71; -.
DR SMR; Q8ZN71; -.
DR STRING; 99287.STM2489; -.
DR PaxDb; Q8ZN71; -.
DR EnsemblBacteria; AAL21383; AAL21383; STM2489.
DR GeneID; 1254011; -.
DR KEGG; stm:STM2489; -.
DR PATRIC; fig|99287.12.peg.2627; -.
DR HOGENOM; CLU_049343_7_1_6; -.
DR OMA; GMDACVP; -.
DR PhylomeDB; Q8ZN71; -.
DR BioCyc; SENT99287:STM2489-MON; -.
DR UniPathway; UPA00034; UER00017.
DR EvolutionaryTrace; Q8ZN71; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IBA:GO_Central.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd00950; DHDPS; 1.
DR Gene3D; 3.20.20.70; -; 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 InterPro; IPR020624; Schiff_base-form_aldolases_CS.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR TIGRFAMs; TIGR00674; dapA; 1.
DR PROSITE; PS00665; DHDPS_1; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lyase; Lysine biosynthesis;
KW Reference proteome; Schiff base.
FT CHAIN 1..292
FT /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT /id="PRO_0000103150"
FT ACT_SITE 133
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT ACT_SITE 161
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT BINDING 45
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT BINDING 203
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 44
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 107
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:3G0S"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3G0S"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:3G0S"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:3G0S"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:3G0S"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:3G0S"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:3G0S"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:3G0S"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:3G0S"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 211..222
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 226..242
FT /evidence="ECO:0007829|PDB:3G0S"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 250..258
FT /evidence="ECO:0007829|PDB:3G0S"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3G0S"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:3G0S"
SQ SEQUENCE 292 AA; 31294 MW; 384A48F3D3FB7BCE CRC64;
MFTGSIVALV TPMDEKGNVS RSCLKKLIDY HVANGTSAIV SVGTTGESAT LSHDEHGDVV
MMTLELADGR IPVIAGTGAN ATAEAISLTQ RFNDSGIVGC LTVTPYYNRP TQEGLFQHFK
AIAEHTDLPQ ILYNVPSRTG CDMLPETVGR LAEIKNIIAI KEATGNLTRV HQIKELVSDD
FILLSGDDAS ALDFMQLGGH GVISVTANVA AREMADMCKL AAEGQFAEAR AINQRLMPLH
NKLFVEPNPI PVKWACKALG LVATDTLRLP MTPITDHGRD IVKAALQHAG LL
