ID   HOGA1_XENTR             Reviewed;         328 AA.
AC   Q5M8W9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 84.
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   Name=hoga1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-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; CF375968; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC087798; AAH87798.1; -; mRNA.
DR   RefSeq; NP_001263607.1; NM_001276678.1.
DR   AlphaFoldDB; Q5M8W9; -.
DR   SMR; Q5M8W9; -.
DR   STRING; 8364.ENSXETP00000008975; -.
DR   PaxDb; 8364-ENSXETP00000007453; -.
DR   GeneID; 496669; -.
DR   KEGG; xtr:496669; -.
DR   AGR; Xenbase:XB-GENE-957775; -.
DR   CTD; 112817; -.
DR   Xenbase; XB-GENE-957775; hoga1.
DR   eggNOG; ENOG502QWNS; Eukaryota.
DR   InParanoid; Q5M8W9; -.
DR   OMA; GMDACVP; -.
DR   OrthoDB; 1780992at2759; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Bgee; ENSXETG00000003443; Expressed in mesonephros and 10 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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..26
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..328
FT                   /note="4-hydroxy-2-oxoglutarate aldolase, mitochondrial"
FT                   /id="PRO_0000273350"
FT   ACT_SITE        195
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         76..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            167
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   328 AA;  35644 MW;  02B53CFDBC0D3326 CRC64;
     MFGRTLFPAR VIALGSGLFR TPLRTLAAGP ALSIGGIYPP IATPFTDKEE VDYGKLHENL
     QNYSSFPFRG FVVQGSNGEY AYLTREERLE VVRRVRQAVP KEKLIMAGSG CESTQATIEM
     TVEMAQSGAD AVLVVTPSYY RGKMTSSALV HHYTKVADHS PVPVVLYSVP ANTGLDLPVD
     AVVTLSQHPN IIGLKDSGGD ITRIGLIIHK TKHLGFQVLS GSAGFLLAGY SVGAVGGVCA
     LANVLGAQVC ELERLCLNGR WQEAKELQYR LIEPNTAVTR KFGIPGLKQA MEWFGFNGGK
     CRSPLLPLTE QEIKELRHIF TVNGWLSL
//