ID F7NMF4_9FIRM Unreviewed; 305 AA.
AC F7NMF4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000256|ARBA:ARBA00012086};
DE EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086};
DE Flags: Fragment;
GN ORFNames=ALO_16422 {ECO:0000313|EMBL:EGO62783.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO62783.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO62783.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO62783.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
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}.
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};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGO62783.1}.
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DR EMBL; AFGF01000168; EGO62783.1; -; Genomic_DNA.
DR AlphaFoldDB; F7NMF4; -.
DR STRING; 1009370.ALO_16422; -.
DR eggNOG; COG0329; Bacteria.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000003240; Unassembled WGS sequence.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
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 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Reference proteome {ECO:0000313|Proteomes:UP000003240}.
FT ACT_SITE 140
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 169
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 214
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGO62783.1"
SQ SEQUENCE 305 AA; 33160 MW; 771BAE491084D0CB CRC64;
SVMMKNVELK GIIPPILTPM NPDESVNLKE LRNQTERMLE GGVHGLFPFG TNGEGYILSE
NEKIEVLEAV IDQVKHRVPV YAGTGCISTA DTIRISKKAQ ELGADVLSII TPSFAFASQK
ELYDHYAEIA KHVDIPIVLY NIPARTGNKL LPETVAKLAK DVDIIMGAKD SSGDWDNLLA
YINLTKDLDK GFRVLSGNDS LILPCLEAGG AGGIAGCANV YPHVLASIYY LFKAGKLEEA
KAAQDSIASF RAVFKYGNPN TVVKKAVSLL GYPVGDCRRP FNYLCDEGVD ALKQVLKENA
DQGMR
//
