GenomeNet

Database: UniProt
Entry: A0A384D2A7_URSMA
LinkDB: A0A384D2A7_URSMA
Original site: A0A384D2A7_URSMA 
ID   A0A384D2A7_URSMA        Unreviewed;       327 AA.
AC   A0A384D2A7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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|Ensembl:ENSUMAP00000031072,
GN   ECO:0000313|RefSeq:XP_008701207.1};
OS   Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008701207.1};
RN   [1] {ECO:0000313|Ensembl:ENSUMAP00000031072}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_008701207.1}
RP   IDENTIFICATION.
RC   TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008701207.1};
RG   RefSeq;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_008701207.1; XM_008702985.2.
DR   STRING; 29073.ENSUMAP00000031072; -.
DR   Ensembl; ENSUMAT00000036707.1; ENSUMAP00000031072.1; ENSUMAG00000022428.1.
DR   GeneID; 103674087; -.
DR   KEGG; umr:103674087; -.
DR   CTD; 112817; -.
DR   OMA; GMDACVP; -.
DR   OrthoDB; 1780992at2759; -.
DR   Proteomes; UP000261680; Unplaced.
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   3: Inferred from homology;
KW   Lyase {ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261680};
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;  35254 MW;  7B0B78262E9FD087 CRC64;
     MLGRGVWSSV RQGLSRGLSR NVGGWASGEG RKVDIAGIYP PVTTPFTATA EVDYGKLEEN
     LHKLGTFPFR GFVVQGSNGE FPFLTSSERL EVVSRVRQAM SKDKLLLAGS GCESTQATVE
     MTVSMAQVGA DAAIVVTPCY YRGRMSSAAL IHHYTKVADL SPIPVVLYSV PANTGLDLPM
     DAVVTLSQHP NIVGIKDSGG DVTRMGLMVH KTRRQDFQVL AGSAGFLLAS YAVGAVGGVC
     ALANVLGAQV CQLERLCLTG QWEDAQKLQH RLIEPNTAVT RRFGIPGLKK TMDWFGYYGG
     PCRAPLQELS PKDEEALRMD FTSNGWL
//
DBGET integrated database retrieval system