ID G7PDP7_MACFA Unreviewed; 281 AA.
AC G7PDP7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=4-hydroxy-2-oxoglutarate aldolase, mitochondrial {ECO:0000256|ARBA:ARBA00018425};
DE EC=4.1.3.16 {ECO:0000256|ARBA:ARBA00012215};
DE AltName: Full=Dihydrodipicolinate synthase-like {ECO:0000256|ARBA:ARBA00032879};
DE AltName: Full=Probable 2-keto-4-hydroxyglutarate aldolase {ECO:0000256|ARBA:ARBA00030874};
DE Flags: Fragment;
GN ORFNames=EGM_18261 {ECO:0000313|EMBL:EHH64929.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH64929.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH64929.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|ARBA:ARBA00007592}.
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DR EMBL; CM001284; EHH64929.1; -; Genomic_DNA.
DR AlphaFoldDB; G7PDP7; -.
DR eggNOG; ENOG502QWNS; Eukaryota.
DR Proteomes; UP000009130; Chromosome 9.
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 3: Inferred from homology;
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 168
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 196
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 239
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT NON_TER 281
FT /evidence="ECO:0000313|EMBL:EHH64929.1"
SQ SEQUENCE 281 AA; 30015 MW; F24719FA21234649 CRC64;
MLGPQVWSSV RQGLSRSLSR NVRGWASGEG KKVDIAGIYP PVTTPFTATA EVDYGKLEEN
LHKLGTFPFR GFVVQGSNGE FPFLTSSERL EVVSRVRQAM PKNKLLLAGS GCESTQATVE
MTVSMAQVGA DAAMVVTPCY YRGRMSSAAL IHHYTKVADL SPIPVVLYSV PANTGLDLPV
DAVVTLSQHP NIVGMKDSGG DVTRIGLIVH KTRKQDFQVL AGSAGFLMAS YALGAVGGVC
ALANVLGAQV CQLERLCLTG QWEDAQKLQH RLIEPNAAVS Q
//