DAPA_BRUSU
ID DAPA_BRUSU Reviewed; 293 AA.
AC Q8G1R0; G0K7Y7;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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};
GN OrderedLocusNames=BR0646, BS1330_I0642;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014291; AAN29575.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM17992.1; -; Genomic_DNA.
DR RefSeq; WP_004690695.1; NZ_KN046804.1.
DR PDB; 6XGS; X-ray; 2.20 A; A/B/C/D=1-293.
DR PDBsum; 6XGS; -.
DR AlphaFoldDB; Q8G1R0; -.
DR SMR; Q8G1R0; -.
DR EnsemblBacteria; AEM17992; AEM17992; BS1330_I0642.
DR GeneID; 45051730; -.
DR GeneID; 55590373; -.
DR KEGG; bms:BR0646; -.
DR KEGG; bsi:BS1330_I0642; -.
DR PATRIC; fig|204722.21.peg.1533; -.
DR HOGENOM; CLU_049343_7_1_5; -.
DR OMA; GMDACVP; -.
DR PhylomeDB; Q8G1R0; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000007104; Chromosome I.
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 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; PS00666; DHDPS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm;
KW Diaminopimelate biosynthesis; Lyase; Lysine biosynthesis; Schiff base.
FT CHAIN 1..293
FT /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT /id="PRO_0000103089"
FT ACT_SITE 133
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00418"
FT ACT_SITE 162
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 204
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 4..8
FT /evidence="ECO:0007829|PDB:6XGS"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:6XGS"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:6XGS"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:6XGS"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:6XGS"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:6XGS"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:6XGS"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:6XGS"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 227..243
FT /evidence="ECO:0007829|PDB:6XGS"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:6XGS"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:6XGS"
SQ SEQUENCE 293 AA; 31598 MW; 4687B828C4AA5C7B CRC64;
MLKGSITALV TPFDREGAFD EKAFRAFVNW QIEEGTKGLV PVGTTGETPT LSHDEHKRVI
EVCIEVAAGR VPVIAGAGSN NTVEAIELAQ HAEKAGADAV LVVTPYYNKP NQRGLYEHFS
RVVRSISIPL VIYNIPGRSI IDMTPETMGA LVRDCKNIVG VKDATGKIER VSEQRAICGK
EFIQLSGEDA TALGFNAHGG VGCISVTSNI APRLCAEFQE ACQAGNFAKA LELQDRLMPL
HKALFLEPNP SGPKYALSRL GRIENVLRSP MVTIEAATAE KIDHAMKHAG LIN
