DAPA_CAMJE
ID DAPA_CAMJE Reviewed; 298 AA.
AC Q9PPB4; Q0PA84;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=Cj0806;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL34934.1; -; Genomic_DNA.
DR PIR; F81352; F81352.
DR RefSeq; WP_002852574.1; NC_002163.1.
DR RefSeq; YP_002344213.1; NC_002163.1.
DR PDB; 3LER; X-ray; 1.84 A; A/B/C/D=1-298.
DR PDB; 3M5V; X-ray; 1.80 A; A/B/C/D=1-298.
DR PDB; 4LY8; X-ray; 1.70 A; A/B/C/D=1-298.
DR PDB; 4M19; X-ray; 2.00 A; A/B/C/D=1-298.
DR PDB; 4MLJ; X-ray; 2.30 A; A/B/C/D=1-298.
DR PDB; 4MLR; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-298.
DR PDB; 4R53; X-ray; 2.00 A; A/B/C/D=1-298.
DR PDB; 5F1U; X-ray; 2.35 A; A/B/C/D=2-298.
DR PDB; 5F1V; X-ray; 2.20 A; A/B/C/D=2-298.
DR PDB; 6TZU; X-ray; 1.80 A; A/B/C/D/E/F=1-298.
DR PDB; 6U01; X-ray; 1.87 A; A/B/C/D/E/F=1-298.
DR PDB; 7KG5; X-ray; 1.95 A; A/B/C/D/E/F=1-298.
DR PDB; 7KG9; X-ray; 2.06 A; A/B/C/D/E/F=1-298.
DR PDB; 7KH4; X-ray; 1.75 A; A/B/C/D/E/F=1-298.
DR PDB; 7KK1; X-ray; 1.77 A; A/B/C/D/E/F=1-298.
DR PDB; 7KKD; X-ray; 1.60 A; A/B/C/D/E/F=1-298.
DR PDB; 7KKG; X-ray; 1.64 A; A/B/C/D/E/F=1-298.
DR PDB; 7KKT; X-ray; 1.71 A; A/B/C/D/E/F=1-298.
DR PDB; 7KLQ; X-ray; 2.50 A; A/B/C/D/E/F=1-298.
DR PDB; 7KLS; X-ray; 2.59 A; A/B/C/D/E/F=1-298.
DR PDB; 7KLT; X-ray; 1.97 A; A/B/C/D/E/F=1-298.
DR PDB; 7KLY; X-ray; 1.67 A; A/B/C/D/E/F=1-298.
DR PDB; 7KM0; X-ray; 2.60 A; A/B/C/D/E/F=1-298.
DR PDB; 7KM1; X-ray; 1.84 A; A/B/C/D/E/F=1-298.
DR PDB; 7KN2; X-ray; 2.53 A; A/B/C/D/E/F=1-298.
DR PDB; 7KN9; X-ray; 2.07 A; A/B/C/D/E/F=1-298.
DR PDB; 7KNZ; X-ray; 2.28 A; A/B/C/D/E/F=1-298.
DR PDB; 7KO1; X-ray; 2.50 A; A/B/C/D/E/F=1-298.
DR PDB; 7KO3; X-ray; 2.22 A; A/B/C/D/E/F=1-298.
DR PDB; 7KOC; X-ray; 2.06 A; A/B/C/D/E/F=1-298.
DR PDB; 7KPC; X-ray; 1.76 A; A/B/C/D/E/F=1-298.
DR PDB; 7KPE; X-ray; 2.06 A; A/B/C/D/E/F=1-298.
DR PDB; 7KR7; X-ray; 2.22 A; A/B/C/D/E/F=1-298.
DR PDB; 7KR8; X-ray; 2.12 A; A/B/C/D/E/F=1-298.
DR PDB; 7KTO; X-ray; 2.13 A; A/B/C/D/E/F=1-298.
DR PDB; 7KU6; X-ray; 2.81 A; A/B/C/D/E/F=1-298.
DR PDB; 7KUZ; X-ray; 2.25 A; A/B/C/D/E/F=1-298.
DR PDB; 7KWF; X-ray; 2.82 A; A/B/C/D/E/F=1-298.
DR PDB; 7KWN; X-ray; 2.24 A; A/B/C/D/E/F=1-298.
DR PDB; 7KWP; X-ray; 2.26 A; A/B/C/D/E/F=1-298.
DR PDB; 7KX1; X-ray; 2.04 A; A/B/C/D/E/F=1-298.
DR PDB; 7KXG; X-ray; 2.28 A; A/B/C/D/E/F=1-298.
DR PDB; 7KXH; X-ray; 1.94 A; A/B/C/D/E/F=1-298.
DR PDB; 7KZ2; X-ray; 1.90 A; A/B/C/D/E/F=1-298.
DR PDB; 7L4B; X-ray; 2.42 A; A/B/C/D/E/F/G/H/I/J/K/L=1-298.
DR PDB; 7LBD; X-ray; 1.99 A; A/B/C/D/E/F=1-298.
DR PDB; 7LCF; X-ray; 2.69 A; A/B/C/D/E/F/G/H/I/J/K/L=1-298.
DR PDB; 7M06; X-ray; 2.70 A; A/B/C/D=1-298.
DR PDBsum; 3LER; -.
DR PDBsum; 3M5V; -.
DR PDBsum; 4LY8; -.
DR PDBsum; 4M19; -.
DR PDBsum; 4MLJ; -.
DR PDBsum; 4MLR; -.
DR PDBsum; 4R53; -.
DR PDBsum; 5F1U; -.
DR PDBsum; 5F1V; -.
DR PDBsum; 6TZU; -.
DR PDBsum; 6U01; -.
DR PDBsum; 7KG5; -.
DR PDBsum; 7KG9; -.
DR PDBsum; 7KH4; -.
DR PDBsum; 7KK1; -.
DR PDBsum; 7KKD; -.
DR PDBsum; 7KKG; -.
DR PDBsum; 7KKT; -.
DR PDBsum; 7KLQ; -.
DR PDBsum; 7KLS; -.
DR PDBsum; 7KLT; -.
DR PDBsum; 7KLY; -.
DR PDBsum; 7KM0; -.
DR PDBsum; 7KM1; -.
DR PDBsum; 7KN2; -.
DR PDBsum; 7KN9; -.
DR PDBsum; 7KNZ; -.
DR PDBsum; 7KO1; -.
DR PDBsum; 7KO3; -.
DR PDBsum; 7KOC; -.
DR PDBsum; 7KPC; -.
DR PDBsum; 7KPE; -.
DR PDBsum; 7KR7; -.
DR PDBsum; 7KR8; -.
DR PDBsum; 7KTO; -.
DR PDBsum; 7KU6; -.
DR PDBsum; 7KUZ; -.
DR PDBsum; 7KWF; -.
DR PDBsum; 7KWN; -.
DR PDBsum; 7KWP; -.
DR PDBsum; 7KX1; -.
DR PDBsum; 7KXG; -.
DR PDBsum; 7KXH; -.
DR PDBsum; 7KZ2; -.
DR PDBsum; 7L4B; -.
DR PDBsum; 7LBD; -.
DR PDBsum; 7LCF; -.
DR PDBsum; 7M06; -.
DR AlphaFoldDB; Q9PPB4; -.
DR SASBDB; Q9PPB4; -.
DR SMR; Q9PPB4; -.
DR IntAct; Q9PPB4; 18.
DR STRING; 192222.Cj0806; -.
DR PaxDb; Q9PPB4; -.
DR PRIDE; Q9PPB4; -.
DR EnsemblBacteria; CAL34934; CAL34934; Cj0806.
DR GeneID; 905109; -.
DR KEGG; cje:Cj0806; -.
DR PATRIC; fig|192222.6.peg.794; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_7_0_7; -.
DR OMA; GMDACVP; -.
DR UniPathway; UPA00034; UER00017.
DR EvolutionaryTrace; Q9PPB4; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-UniRule.
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..298
FT /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT /id="PRO_0000103093"
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT ACT_SITE 166
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT BINDING 48
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT BINDING 207
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 47
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 111
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:7KKD"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:7KKD"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:7KKD"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:7KKD"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:7KKD"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:7KKD"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:7KKD"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 230..246
FT /evidence="ECO:0007829|PDB:7KKD"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:7KKD"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:7KKD"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:7KKD"
SQ SEQUENCE 298 AA; 32671 MW; AD0C3CC9156301E4 CRC64;
MDKNIIIGAM TALITPFKNG KVDEQSYARL IKRQIENGID AVVPVGTTGE SATLTHEEHR
TCIEIAVETC KGTKVKVLAG AGSNATHEAV GLAKFAKEHG ADGILSVAPY YNKPTQQGLY
EHYKAIAQSV DIPVLLYNVP GRTGCEISTD TIIKLFRDCE NIYGVKEASG NIDKCVDLLA
HEPRMMLISG EDAINYPILS NGGKGVISVT SNLLPDMISA LTHFALDENY KEAKKINDEL
YNINKILFCE SNPIPIKTAM YLAGLIESLE FRLPLCSPSK ENFAKIEEVM KKYKIKGF
