ID F4GWN7_PUSST Unreviewed; 291 AA.
AC F4GWN7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|ARBA:ARBA00012086, ECO:0000256|HAMAP-Rule:MF_00418};
DE Short=HTPA synthase {ECO:0000256|HAMAP-Rule:MF_00418};
DE EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086, ECO:0000256|HAMAP-Rule:MF_00418};
GN Name=dapA {ECO:0000256|HAMAP-Rule:MF_00418};
GN OrderedLocusNames=PT7_0370 {ECO:0000313|EMBL:AEC18910.1};
OS Pusillimonas sp. (strain T7-7).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pusillimonas.
OX NCBI_TaxID=1007105 {ECO:0000313|EMBL:AEC18910.1, ECO:0000313|Proteomes:UP000008737};
RN [1] {ECO:0000313|EMBL:AEC18910.1, ECO:0000313|Proteomes:UP000008737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T7-7 {ECO:0000313|EMBL:AEC18910.1,
RC ECO:0000313|Proteomes:UP000008737};
RX PubMed=21622753; DOI=10.1128/JB.05242-11;
RA Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.;
RT "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant diesel
RT oil-degrading bacterium isolated from the Bohai Sea in China.";
RL J. Bacteriol. 193:4021-4022(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T7-7;
RA Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.;
RT "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7-7, a
RT novel species isolated from the Bohai Sea, China.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde
CC [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
CC {ECO:0000256|ARBA:ARBA00003294, ECO:0000256|HAMAP-Rule:MF_00418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-
CC hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O;
CC Xref=Rhea:RHEA:34171, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:67139, ChEBI:CHEBI:537519; EC=4.3.3.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000594, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00005120, ECO:0000256|HAMAP-Rule:MF_00418}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_00418}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00418}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000256|HAMAP-
CC Rule:MF_00418, ECO:0000256|PIRNR:PIRNR001365}.
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:0000256|HAMAP-Rule:MF_00418}.
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DR EMBL; CP002663; AEC18910.1; -; Genomic_DNA.
DR RefSeq; WP_013741459.1; NC_015458.1.
DR AlphaFoldDB; F4GWN7; -.
DR STRING; 1007105.PT7_0370; -.
DR KEGG; put:PT7_0370; -.
DR eggNOG; COG0329; Bacteria.
DR HOGENOM; CLU_049343_5_0_4; -.
DR OrthoDB; 199953at2; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000008737; 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; cd00408; DHDPS-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR00674; dapA; 1.
DR PANTHER; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00418};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00418};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915,
KW ECO:0000256|HAMAP-Rule:MF_00418};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00418};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW Rule:MF_00418};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00418}.
FT ACT_SITE 134
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 162
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 46
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 204
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418,
FT ECO:0000256|PIRSR:PIRSR001365-2"
FT SITE 45
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
FT SITE 108
FT /note="Part of a proton relay during catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00418"
SQ SEQUENCE 291 AA; 31423 MW; 5F957804ED7443F5 CRC64;
MNTQGVLVPI VTPFDADNKV DLQALKKLVE CFIEQGVGGI VACGTTGEYY ALNEDERQQV
LECVKEAGQG RVTLIAGVNG LSTQEAIGRV RQAEALGYDG LMLATPPYSL PGQAEIVAHF
RTVAEATKLP IVMYNFPARV GVEIGFDAVV ELSKIPNIVG IKESSGNFSR ALALIKADLP
NFEVICGCDD QAADFLFWGV RSWISGGANV FPGEQAAMIN ASLAGNWDEV KSLMTSMLPV
IQAMESGDYN QKAKLGCRRH GVDAGSVRQP LLPLPDSDAQ EFSRLLEQYR R
//
