ID A0A7W5VDQ4_9ACTN Unreviewed; 301 AA.
AC A0A7W5VDQ4;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 02-APR-2025, entry version 14.
DE SubName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000313|EMBL:MBB3725822.1};
DE EC=4.3.3.7 {ECO:0000313|EMBL:MBB3725822.1};
GN ORFNames=FHR33_001682 {ECO:0000313|EMBL:MBB3725822.1};
OS Nonomuraea dietziae.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=65515 {ECO:0000313|EMBL:MBB3725822.1, ECO:0000313|Proteomes:UP000579945};
RN [1] {ECO:0000313|EMBL:MBB3725822.1, ECO:0000313|Proteomes:UP000579945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44320 {ECO:0000313|EMBL:MBB3725822.1,
RC ECO:0000313|Proteomes:UP000579945};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000256|ARBA:ARBA00007592,
CC ECO:0000256|PIRNR:PIRNR001365}.
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:MBB3725822.1}.
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DR EMBL; JACIBV010000001; MBB3725822.1; -; Genomic_DNA.
DR RefSeq; WP_312895418.1; NZ_BAAAXX010000144.1.
DR AlphaFoldDB; A0A7W5VDQ4; -.
DR GeneID; 95388227; -.
DR Proteomes; UP000579945; Unassembled WGS sequence.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProtKB-ARBA.
DR CDD; cd00408; DHDPS-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR PANTHER; PTHR12128:SF66; 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 Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000579945};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 134
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 162
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 204
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 301 AA; 31392 MW; 1CA303AF9663D482 CRC64;
MKLTGVIPPV CTPLTPSFDV DGPSLTRLVD HLMDGGVDGL FVLGSSSEAA YLPDGHRRAV
LDTVVGHVAG QVPVLAGVID MTTLRVLDHV RAAVVAGVDG IVATAPFYAR THPAEIALHF
RTIAEVAELP VYAYDLPVSV HTKLGRDLLL ELASSGVLAG VKDSSGDDGG LRSLILSRPS
SFSVLTGSEV TVDCALWMGA DGVVPGLGNV DPHGYARLFA AARAGDWAAA KDEQERLINL
FELVTVGLPR MGGGSSALGA FKAALHLRGV IDHPTTAVPQ IPLNEEETRR VGKHLADAGL
L
//