DAPA_AQUAE
ID DAPA_AQUAE Reviewed; 294 AA.
AC O67216;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=aq_1143;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07169.1; -; Genomic_DNA.
DR PIR; E70398; E70398.
DR RefSeq; NP_213780.1; NC_000918.1.
DR RefSeq; WP_010880718.1; NC_000918.1.
DR PDB; 2EHH; X-ray; 1.90 A; A/C/D/E=1-294.
DR PDBsum; 2EHH; -.
DR AlphaFoldDB; O67216; -.
DR SMR; O67216; -.
DR STRING; 224324.aq_1143; -.
DR EnsemblBacteria; AAC07169; AAC07169; aq_1143.
DR KEGG; aae:aq_1143; -.
DR PATRIC; fig|224324.8.peg.891; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_7_1_0; -.
DR InParanoid; O67216; -.
DR OMA; GMDACVP; -.
DR OrthoDB; 1438588at2; -.
DR BRENDA; 4.3.3.7; 396.
DR UniPathway; UPA00034; UER00017.
DR EvolutionaryTrace; O67216; -.
DR Proteomes; UP000000798; 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..294
FT /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT /id="PRO_0000103081"
FT ACT_SITE 132
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 44
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 43
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT SITE 106
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:2EHH"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:2EHH"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2EHH"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:2EHH"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:2EHH"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:2EHH"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:2EHH"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:2EHH"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:2EHH"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 226..242
FT /evidence="ECO:0007829|PDB:2EHH"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 250..258
FT /evidence="ECO:0007829|PDB:2EHH"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:2EHH"
SQ SEQUENCE 294 AA; 32670 MW; 0778B824E6619E31 CRC64;
MFQGSIVALI TPFKEGEVDY EALGNLIEFH VDNGTDAILV CGTTGESPTL TFEEHEKVIE
FAVKRAAGRI KVIAGTGGNA THEAVHLTAH AKEVGADGAL VVVPYYNKPT QRGLYEHFKT
VAQEVDIPII IYNIPSRTCV EISVDTMFKL ASECENIVAS KESTPNMDRI SEIVKRLGES
FSVLSGDDSL TLPMMALGAK GVISVANNVM PREVKELIRA ALEGDFRRAR EIHYYLHDLF
KVLFIETNPI PVKTACWMLG MCEKEFRLPL TEMSPENENK LREVLKKYNL PLKN
