ID F7B5W8_CALJA Unreviewed; 327 AA.
AC F7B5W8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 57.
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};
GN Name=HOGA1 {ECO:0000313|EMBL:JAB17577.1,
GN ECO:0000313|Ensembl:ENSCJAP00000030846.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000030846.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000030846.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB17577.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:JAB42182.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB17577.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB36587.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000030846.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00007592,
CC ECO:0000256|PIRNR:PIRNR001365}.
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DR EMBL; GAMS01005559; JAB17577.1; -; mRNA.
DR EMBL; GAMQ01005264; JAB36587.1; -; mRNA.
DR EMBL; GAMP01010573; JAB42182.1; -; mRNA.
DR RefSeq; XP_009008345.1; XM_009010097.2.
DR STRING; 9483.ENSCJAP00000030846; -.
DR Ensembl; ENSCJAT00000032597.5; ENSCJAP00000030846.3; ENSCJAG00000047404.3.
DR GeneID; 103796777; -.
DR KEGG; cjc:103796777; -.
DR CTD; 112817; -.
DR GeneTree; ENSGT00530000063604; -.
DR HOGENOM; CLU_032516_0_0_1; -.
DR OMA; GMDACVP; -.
DR OrthoDB; 1780992at2759; -.
DR Proteomes; UP000008225; Chromosome 12.
DR Bgee; ENSCJAG00000047404; Expressed in kidney and 5 other cell types or tissues.
DR GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0019470; P:4-hydroxyproline catabolic process; IEA:Ensembl.
DR GO; GO:0009436; P:glyoxylate catabolic process; IEA:Ensembl.
DR GO; GO:0033609; P:oxalate metabolic process; IEA:Ensembl.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IEA:Ensembl.
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 {ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
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"
SQ SEQUENCE 327 AA; 35294 MW; 9785C1A7324C5BDF CRC64;
MLGPQVWSSV RQGLSRGLSR NVRGWASGEG KKVDISGIYP PVTTPFTATA EVDYGKLEEN
LHKLGTLPFR GFVVQGSNGE FPFLTSSERL EVVSCVRQAM PKDRLLLAGS GCESTQATVE
MTVSMAQVGA DAAMVVTPCY YRGRMSSAAL IHHYTKVADL SPIPVVLYSV PANTGLDLPV
DAVVMLSQHP NIVGMKDSGG DVTRIGLIVH KTRKQDFQVL AGSAGFLMAS YALGAVGGVC
ALANVLGAQV CQLERLCLTG QWEDAQKLQH RLIEPNMAVT RRFGIPGLKK TMDWFGYYGG
PCRAPLQELS PAEEEALRMD FTSNGWL
//
