ID A0A091EAZ6_CORBR Unreviewed; 295 AA.
AC A0A091EAZ6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-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 ORFNames=N302_13557 {ECO:0000313|EMBL:KFO54341.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO54341.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO54341.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO54341.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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; KK718105; KFO54341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091EAZ6; -.
DR STRING; 85066.A0A091EAZ6; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 136
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 164
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 207
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO54341.1"
FT NON_TER 295
FT /evidence="ECO:0000313|EMBL:KFO54341.1"
SQ SEQUENCE 295 AA; 31687 MW; 0134D0C067666FF8 CRC64;
LDLRGIFPPL ATPFSPSQEV DYAQLEGNLR RYASIPFRGL VVLGSNGEYP YLAPHERVEV
VSCVRQALPR DRLLLAGSGC ESTQATIELT VSMAEAGADV ALVVTPCYYR GAMTTAALVH
HYTEVGNASP IPVVLYNVPA NTGLDLPMDA VITLAQHPNI IGIKDSGGDI TRMGLMVHKT
RQEDFQVLAG SAGFLLASYA VGAAGGVCAL ANVLGDPLCQ LDHLCREGRW QEARDLQHRL
IEPNTAVTRQ FGIPGLKKAM EWFGYYGGPC RAPLAPLSPA QAEELKSTFS ANGWL
//
