DAPA_BARHE
ID DAPA_BARHE Reviewed; 294 AA.
AC Q6G468;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=BH05000;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of dihydrodipicolinate synthase from Bartonella
RT henselae.";
RL Submitted (JUN-2011) to the PDB data bank.
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; BX897699; CAF27308.1; -; Genomic_DNA.
DR RefSeq; WP_011180431.1; NZ_LRIJ02000001.1.
DR PDB; 3SI9; X-ray; 2.10 A; A/B/C/D=1-294.
DR PDBsum; 3SI9; -.
DR AlphaFoldDB; Q6G468; -.
DR SMR; Q6G468; -.
DR STRING; 283166.BH05000; -.
DR PaxDb; Q6G468; -.
DR PRIDE; Q6G468; -.
DR EnsemblBacteria; CAF27308; CAF27308; BH05000.
DR GeneID; 64156781; -.
DR KEGG; bhe:BH05000; -.
DR eggNOG; COG0329; Bacteria.
DR OMA; GMDACVP; -.
DR BRENDA; 4.3.3.7; 7854.
DR UniPathway; UPA00034; UER00017.
DR EvolutionaryTrace; Q6G468; -.
DR Proteomes; UP000000421; 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 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..294
FT /note="4-hydroxy-tetrahydrodipicolinate synthase"
FT /id="PRO_1000050166"
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:3SI9"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:3SI9"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3SI9"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:3SI9"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:3SI9"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:3SI9"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:3SI9"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:3SI9"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:3SI9"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 227..243
FT /evidence="ECO:0007829|PDB:3SI9"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:3SI9"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:3SI9"
SQ SEQUENCE 294 AA; 31483 MW; CDD074F2CDE871AE CRC64;
MLKGAVTALI TPFDDNGAID EKAFCNFVEW QITQGINGVS PVGTTGESPT LTHEEHKRII
ELCVEQVAKR VPVVAGAGSN STSEAVELAK HAEKAGADAV LVVTPYYNRP NQRGLYTHFS
SIAKAISIPI IIYNIPSRSV IDMAVETMRD LCRDFKNIIG VKDATGKIER ASEQREKCGK
DFVQLSGDDC TALGFNAHGG VGCISVSSNV APKLCAQLHA ACLCSDYKTA LKLNDLLMPL
NRAVFIEPSP AGIKYAAAKL GLCGTIVRSP IVPLSDTTKK IIDEALYHAG LLKE
