ID   HOGA1_MOUSE             Reviewed;         321 AA.
AC   Q9DCU9; Q91W74; Q9CY60;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 136.
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; Synonyms=Dhdpsl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16430.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB27226.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK002457; BAB22114.1; -; mRNA.
DR   EMBL; AK010857; BAB27226.1; ALT_FRAME; mRNA.
DR   EMBL; BC016430; AAH16430.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS29820.1; -.
DR   RefSeq; NP_080428.1; NM_026152.1.
DR   AlphaFoldDB; Q9DCU9; -.
DR   SMR; Q9DCU9; -.
DR   STRING; 10090.ENSMUSP00000080414; -.
DR   iPTMnet; Q9DCU9; -.
DR   PhosphoSitePlus; Q9DCU9; -.
DR   SwissPalm; Q9DCU9; -.
DR   jPOST; Q9DCU9; -.
DR   MaxQB; Q9DCU9; -.
DR   PaxDb; 10090-ENSMUSP00000080414; -.
DR   PeptideAtlas; Q9DCU9; -.
DR   ProteomicsDB; 267059; -.
DR   Pumba; Q9DCU9; -.
DR   Antibodypedia; 55095; 35 antibodies from 9 providers.
DR   DNASU; 67432; -.
DR   Ensembl; ENSMUST00000081714.5; ENSMUSP00000080414.5; ENSMUSG00000025176.15.
DR   GeneID; 67432; -.
DR   KEGG; mmu:67432; -.
DR   UCSC; uc008hnb.1; mouse.
DR   AGR; MGI:1914682; -.
DR   CTD; 112817; -.
DR   MGI; MGI:1914682; Hoga1.
DR   VEuPathDB; HostDB:ENSMUSG00000025176; -.
DR   eggNOG; ENOG502QWNS; Eukaryota.
DR   GeneTree; ENSGT00530000063604; -.
DR   HOGENOM; CLU_049343_0_1_1; -.
DR   InParanoid; Q9DCU9; -.
DR   OMA; GMDACVP; -.
DR   OrthoDB; 1780992at2759; -.
DR   PhylomeDB; Q9DCU9; -.
DR   TreeFam; TF324600; -.
DR   Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR   BioGRID-ORCS; 67432; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Hoga1; mouse.
DR   PRO; PR:Q9DCU9; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q9DCU9; Protein.
DR   Bgee; ENSMUSG00000025176; Expressed in right kidney and 149 other cell types or tissues.
DR   ExpressionAtlas; Q9DCU9; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
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; ISS:UniProtKB.
DR   GO; GO:0008747; F:N-acetylneuraminate lyase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0019470; P:4-hydroxyproline catabolic process; ISO:MGI.
DR   GO; GO:0009436; P:glyoxylate catabolic process; ISS:UniProtKB.
DR   GO; GO:0046487; P:glyoxylate metabolic process; ISO:MGI.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
DR   GO; GO:0033609; P:oxalate metabolic process; ISO:MGI.
DR   GO; GO:0042866; P:pyruvate biosynthetic process; ISO:MGI.
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.
DR   Genevisible; Q9DCU9; MM.
PE   1: Evidence at protein level;
KW   Lyase; Mitochondrion; Reference proteome; Schiff base; Transit peptide.
FT   TRANSIT         1..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P5I5"
FT   CHAIN           24..321
FT                   /note="4-hydroxy-2-oxoglutarate aldolase, mitochondrial"
FT                   /id="PRO_0000273347"
FT   ACT_SITE        190
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         71..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            162
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        25
FT                   /note="K -> M (in Ref. 1; BAB27226)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   321 AA;  34644 MW;  75B3DC959756D5A7 CRC64;
     MLGPQIWASM RQGLSRGLSR NVKGKKVDIA GIYPPVTTPF TATAEVDYGK LEENLNRLAT
     FPFRGFVVQG STGEFPFLTS LERLEVVSRV RQAIPKDKFL IAGSGCESTQ ATVEMTVSMA
     QVGADVAMVV TPCYYRGRMS SAALIHHYTK VADVSPIPVV LYSVPANTGL ELPVDAVVTL
     SQHPNIIGLK DSGGDVTRIG LIVHKTSKQD FQVLAGSAGF LLASYAVGAV GGICGLANVL
     GAQVCQLERL CLTGQWEAAQ ELQHRLIEPN TAVTRRFGIP GLKKTMDWFG YYGGPCRAPL
     QELSPTEEEA LRLDFSNNGW L
//