ID U6DB79_NEOVI Unreviewed; 299 AA.
AC U6DB79;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 Name=HOGA1 {ECO:0000313|EMBL:CCP79143.1};
OS Neovison vison (American mink) (Mustela vison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Neogale.
OX NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP79143.1};
RN [1] {ECO:0000313|EMBL:CCP79143.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pool of brain {ECO:0000313|EMBL:CCP79143.1};
RA Anistoroaei R., Christensen K.;
RT "An American mink transcriptome.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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; HAAF01007319; CCP79143.1; -; mRNA.
DR AlphaFoldDB; U6DB79; -.
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 2: Evidence at transcript level;
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 299
FT /evidence="ECO:0000313|EMBL:CCP79143.1"
SQ SEQUENCE 299 AA; 32179 MW; 89BDBCA960F835D9 CRC64;
MLGRGIWSSV RQGLSRGLSR KVGAWASGEG RRVDIAGIYP PVTTPFTATA EVDYEKLEEN
LHKLGTLPFR GFVVQGSNGE FPFLTSSERL EVVSRVRQAM PKDKLLLAGS GCESTQATVE
MTVSMAQVGA DVAIVVTPCY YRGRMSSAAL IHHYTKVADL SPIPVVLYSV PANTGLDLPV
DAVVTLSQHP NIVGIKDSGG DVTKMGLLVH KTRRQDFQVL AGSAGFLLAS YAVGAVGGVC
ALANVLGAQV CQLERLCLTG QWEDAQKLQH RLIEPNTAVT RRFGIPGLKK TMDWFGYYG
//
