HOGA1_BOVIN
ID HOGA1_BOVIN Reviewed; 327 AA.
AC Q0P5I5; Q0V7M3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=4-hydroxy-2-oxoglutarate aldolase, mitochondrial;
DE EC=4.1.3.16 {ECO:0000269|PubMed:1587831};
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; Synonyms=DHDPSL;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 26-30, TRANSIT PEPTIDE CLEAVAGE SITE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21998747; DOI=10.1371/journal.pone.0026021;
RA Riedel T.J., Johnson L.C., Knight J., Hantgan R.R., Holmes R.P.,
RA Lowther W.T.;
RT "Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate
RT aldolase: implications for hydroxyproline metabolism in primary
RT hyperoxaluria.";
RL PLoS ONE 6:E26021-E26021(2011).
RN [4]
RP SUBUNIT, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1587831; DOI=10.1016/s0021-9258(19)50046-1;
RA Dekker E.E., Kitson R.P.;
RT "2-Keto-4-hydroxyglutarate aldolase: purification and characterization of
RT the homogeneous enzyme from bovine kidney.";
RL J. Biol. Chem. 267:10507-10514(1992).
RN [5]
RP IDENTIFICATION.
RX PubMed=20797690; DOI=10.1016/j.ajhg.2010.07.023;
RA Belostotsky R., Seboun E., Idelson G.H., Milliner D.S., Becker-Cohen R.,
RA Rinat C., Monico C.G., Feinstein S., Ben-Shalom E., Magen D., Weissman I.,
RA Charon C., Frishberg Y.;
RT "Mutations in DHDPSL are responsible for primary hyperoxaluria type III.";
RL Am. J. Hum. Genet. 87:392-399(2010).
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 Evidence={ECO:0000269|PubMed:1587831};
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:0000269|PubMed:1587831};
CC -!- ACTIVITY REGULATION: Inhibited by divalent cations.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=26 uM for DL-4-hydroxy-2-oxoglutarate
CC {ECO:0000269|PubMed:1587831};
CC Vmax=10.7 umol/min/mg enzyme {ECO:0000269|PubMed:1587831};
CC pH dependence:
CC Optimum pH is 8.8. {ECO:0000269|PubMed:1587831};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1587831}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21998747}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
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DR EMBL; BT026547; ABH06334.1; -; mRNA.
DR EMBL; BC119998; AAI19999.1; -; mRNA.
DR RefSeq; NP_001068705.1; NM_001075237.1.
DR AlphaFoldDB; Q0P5I5; -.
DR SMR; Q0P5I5; -.
DR STRING; 9913.ENSBTAP00000016909; -.
DR PaxDb; Q0P5I5; -.
DR Ensembl; ENSBTAT00000016909; ENSBTAP00000016909; ENSBTAG00000012721.
DR GeneID; 506001; -.
DR KEGG; bta:506001; -.
DR CTD; 112817; -.
DR VEuPathDB; HostDB:ENSBTAG00000012721; -.
DR VGNC; VGNC:29900; HOGA1.
DR eggNOG; ENOG502QWNS; Eukaryota.
DR GeneTree; ENSGT00530000063604; -.
DR HOGENOM; CLU_049343_0_1_1; -.
DR InParanoid; Q0P5I5; -.
DR OMA; GMDACVP; -.
DR OrthoDB; 1238597at2759; -.
DR TreeFam; TF324600; -.
DR BRENDA; 4.1.3.16; 908.
DR SABIO-RK; Q0P5I5; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000012721; Expressed in cortex of kidney and 86 other tissues.
DR ExpressionAtlas; Q0P5I5; baseline.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
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; IDA:UniProtKB.
DR GO; GO:0009436; P:glyoxylate catabolic process; IDA:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Mitochondrion; Reference proteome;
KW Schiff base; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:21998747"
FT CHAIN 26..327
FT /note="4-hydroxy-2-oxoglutarate aldolase, mitochondrial"
FT /id="PRO_0000273345"
FT ACT_SITE 196
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 77..78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 168
FT /note="Involved in proton transfer during cleavage"
FT /evidence="ECO:0000250"
FT CONFLICT 327
FT /note="L -> F (in Ref. 1; ABH06334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 35217 MW; 153314DCD1F0D587 CRC64;
MLVPRVWSSV RLGLSRVLSR TLRGWPSGEG RGMDLSGIYP PVTTPFTATA EVDYGKLEEN
LHKLGTLPFR GFVVQGSNGE FPFLTSSERL EVVSRARQAL PKDKLLLAGS GCESTQATVE
MTVSMAQVGA DAAMVVTPCY YRGRMSSAAL IHHYTKVADL SPVPVVLYSV PANTGLDLPV
DAVVTLSQHP NIVGIKDSGG DVTRIGLIVH KTRSQDFQVL AGSAGFLLAS YAIGAVGGVC
ALANVLGSQV CQLERLCLTG QWEDAQKLQH RLIEPNTAVT RRFGIPGLKK TMDWFGYYGG
PCRSPLQELS PAQEEALRLD FASNGWL
