ID   HOGA1_XENLA             Reviewed;         326 AA.
AC   Q5XGL6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 78.
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 laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-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; BC084421; AAH84421.1; -; mRNA.
DR   RefSeq; NP_001088351.1; NM_001094882.1.
DR   AlphaFoldDB; Q5XGL6; -.
DR   SMR; Q5XGL6; -.
DR   DNASU; 495193; -.
DR   GeneID; 495193; -.
DR   KEGG; xla:495193; -.
DR   AGR; Xenbase:XB-GENE-957779; -.
DR   CTD; 495193; -.
DR   Xenbase; XB-GENE-957779; hoga1.L.
DR   OrthoDB; 1780992at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 495193; Expressed in kidney and 15 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..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..326
FT                   /note="4-hydroxy-2-oxoglutarate aldolase, mitochondrial"
FT                   /id="PRO_0000273349"
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   326 AA;  35488 MW;  3F4279E411C5E542 CRC64;
     MFGRTLFPAR ALCSGLFKTP LRTLATRPAL SIGGIYPPIA TPFTDKEEVD YGKLHENLQK
     YCSFPFSGFV VQGSNGEYAY LTREERLEVV RRVRQAVPKE KLIMAGSGCE STQATIEMTV
     EMARSGADVV LVVTPSYYRG KMTSSALVHH YTKVADHSPV PVVLYSVPAN TGLDLPVDAV
     VTLSQHPNII GLKDSGGDIT RIGLIIHKTK HLGFQVLSGS AGFLLAGYSV GAVGGVCALA
     NVLGAQVCEL EKLCLNGRWQ EAKELQHRLI EPNSAVTRKF GIPGLKQAMD WFGFNGGKCR
     SPLLPLTEQE IKELRHIFTV NGWLSS
//