ID A0A840P9D2_9ACTN Unreviewed; 295 AA.
AC A0A840P9D2;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 02-APR-2025, entry version 14.
DE SubName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000313|EMBL:MBB5135246.1};
DE EC=4.3.3.7 {ECO:0000313|EMBL:MBB5135246.1};
GN ORFNames=HNP84_004982 {ECO:0000313|EMBL:MBB5135246.1};
OS Thermocatellispora tengchongensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Thermocatellispora.
OX NCBI_TaxID=1073253 {ECO:0000313|EMBL:MBB5135246.1, ECO:0000313|Proteomes:UP000578449};
RN [1] {ECO:0000313|EMBL:MBB5135246.1, ECO:0000313|Proteomes:UP000578449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45615 {ECO:0000313|EMBL:MBB5135246.1,
RC ECO:0000313|Proteomes:UP000578449};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
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:MBB5135246.1}.
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DR EMBL; JACHGN010000010; MBB5135246.1; -; Genomic_DNA.
DR RefSeq; WP_185052185.1; NZ_BAABIX010000015.1.
DR AlphaFoldDB; A0A840P9D2; -.
DR Proteomes; UP000578449; Unassembled WGS sequence.
DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase activity; IEA:TreeGrafter.
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 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000578449}.
FT ACT_SITE 138
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 164
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 49
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 295 AA; 31936 MW; D161339145B41D6E CRC64;
MRSLDLHGMI STVVTPFDEH DRVDLDLLRG EVKYLLDAGV TAICACGSTG EGQTLSLEES
TDICRVVVEE VAGRVPVIAG VIQNSTAQVI RYSLALKETG VDALQITPVH YVFSPSADET
VAYFREIGEA VDLPIVLYNV VPWALVPVDV IERLAEVPQL VAVKQSGGDM HLLVDLLARV
RDRFTILAAL DDLHYPAFML GAHGALAAIP TVTPRLSVEL WNAVQAGDHD LARELHERIL
TVWRAIDGPN LPATLKAALR LQGRDGGLPR RPFSPASPAE RERIAAALRA ANLIA
//