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Database: UniProt
Entry: A0A7W5VDQ4_9ACTN
LinkDB: A0A7W5VDQ4_9ACTN
Original site: A0A7W5VDQ4_9ACTN 
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
//
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