ID A0A4W5L5M9_9TELE Unreviewed; 310 AA.
AC A0A4W5L5M9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=4-hydroxy-2-oxoglutarate aldolase, mitochondrial {ECO:0000256|ARBA:ARBA00018425};
DE EC=4.1.3.16 {ECO:0000256|ARBA:ARBA00012215};
DE EC=4.3.3.7 {ECO:0000256|ARBA:ARBA00012086};
DE AltName: Full=Dihydrodipicolinate synthase-like {ECO:0000256|ARBA:ARBA00032879};
DE AltName: Full=Probable 2-keto-4-hydroxyglutarate aldolase {ECO:0000256|ARBA:ARBA00030874};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000019440.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000019440.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- FUNCTION: Catalyzes the final step in the metabolic pathway of
CC hydroxyproline. {ECO:0000256|ARBA:ARBA00002577}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC Xref=Rhea:RHEA:30687, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:62213; EC=4.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00033610};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC Xref=Rhea:RHEA:35639, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:71685; EC=4.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00033613};
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000256|ARBA:ARBA00007592,
CC ECO:0000256|PIRNR:PIRNR001365}.
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DR AlphaFoldDB; A0A4W5L5M9; -.
DR STRING; 62062.ENSHHUP00000019440; -.
DR Ensembl; ENSHHUT00000020160.1; ENSHHUP00000019440.1; ENSHHUG00000012155.1.
DR GeneTree; ENSGT00530000063604; -.
DR UniPathway; UPA00034; UER00017.
DR Proteomes; UP000314982; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
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; cd00950; DHDPS; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Diaminopimelate biosynthesis {ECO:0000256|ARBA:ARBA00022915};
KW Lyase {ECO:0000256|PIRNR:PIRNR001365};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Reference proteome {ECO:0000313|Proteomes:UP000314982};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 150
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 179
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 62
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT BINDING 221
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 310 AA; 34024 MW; 2548CAE67A81230D CRC64;
FNCSILIFFF CNRDTFSFYF RTGVALITPF KEDFSIDIDA LKRIVNFSID GGIEYLVVLG
TTAENATLSQ DEKELVIQTV IEVNAGRLPL VLGVGGNNTV KVVEELKTRD LSSFVAILSV
SPYYNKPTQE GIYQHFKAVS EASPIPVILY NVPGRTASNM LPATVIRLAN DFENIVAIKE
AAGDMVQAMQ LLKNKPKDFL VISGDDMIAL PIVLAGGAGV ISVIGQGFPK EFSEMIRLGL
NRKVDEAYKS QYVLSDCIDM IFEQGNPAGI KEVFKILGIS ENVVRLPLVT VDESLANRLS
VFVKNIDKNA
//
