ID   HOGA1_DANRE             Reviewed;         324 AA.
AC   Q6NY77;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=4-hydroxy-2-oxoglutarate aldolase, mitochondrial;
DE            EC=4.1.3.16;
DE   AltName: Full=Dihydrodipicolinate synthase-like;
DE            Short=DHDPS-like protein;
DE   AltName: Full=Probable 2-keto-4-hydroxyglutarate aldolase;
DE            Short=Probable KHG-aldolase;
DE   Flags: Precursor;
GN   ORFNames=zgc:77082;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the final step in the metabolic pathway of
CC       hydroxyproline. {ECO:0000250}.
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   -!- 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   -!- ACTIVITY REGULATION: Inhibited by divalent cations. {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q0P5I5}.
CC   -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
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DR   EMBL; BC066708; AAH66708.1; -; mRNA.
DR   RefSeq; NP_998035.1; NM_212870.1.
DR   AlphaFoldDB; Q6NY77; -.
DR   SMR; Q6NY77; -.
DR   STRING; 7955.ENSDARP00000021126; -.
DR   PaxDb; 7955-ENSDARP00000021126; -.
DR   GeneID; 405806; -.
DR   KEGG; dre:405806; -.
DR   AGR; ZFIN:ZDB-GENE-040426-2242; -.
DR   CTD; 112817; -.
DR   ZFIN; ZDB-GENE-040426-2242; hoga1.
DR   eggNOG; ENOG502QWNS; Eukaryota.
DR   InParanoid; Q6NY77; -.
DR   OMA; GMDACVP; -.
DR   OrthoDB; 1780992at2759; -.
DR   PhylomeDB; Q6NY77; -.
DR   TreeFam; TF324600; -.
DR   Reactome; R-DRE-389661; Glyoxylate metabolism and glycine degradation.
DR   PRO; PR:Q6NY77; -.
DR   Proteomes; UP000000437; Chromosome 22.
DR   Bgee; ENSDARG00000018944; Expressed in liver and 21 other cell types or tissues.
DR   ExpressionAtlas; Q6NY77; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0106009; F:(4S)-4-hydroxy-2-oxoglutarate aldolase activity; IEA:RHEA.
DR   GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; ISS:UniProtKB.
DR   GO; GO:0008747; F:N-acetylneuraminate lyase activity; IBA:GO_Central.
DR   GO; GO:0009436; P:glyoxylate catabolic process; ISS:UniProtKB.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
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: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   2: Evidence at transcript level;
KW   Lyase; Mitochondrion; Reference proteome; Schiff base; Transit peptide.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..324
FT                   /note="4-hydroxy-2-oxoglutarate aldolase, mitochondrial"
FT                   /id="PRO_0000273348"
FT   ACT_SITE        193
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         74..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            165
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  35307 MW;  C2D821D59F046031 CRC64;
     MFAHRSFSLL CRRSAVTSWR SQSHTAGKRL DISGIYPPIA TPFTEPEDVD YQKLDDNIRK
     YGRLPFRGLV VQGSNGEYPY LTAEERVEVV KRVKQALPKD KLVMAGSGCE STRATIQMSQ
     RMADAGADCV LVVTPCFYRG RMDSRALINH YSKVADSCSV PVVLYSVPAN TGLDLPVDAV
     IQLSKHPNIV GLKDSGGDIT RIALMVQKTR SQDFQVLAGS AGFLMAAYAV GAVGGVCALA
     NVLGQQVCEL AQLCVSGRWD EAKELQYRLI EPNTAVTRGF GVPALKLAMD WFGYHGGICR
     SPLQPLSKAD LEALRGKFSS NGWL
//