ID A0A1V6VA45_9EURO Unreviewed; 309 AA.
AC A0A1V6VA45;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=4-hydroxy-2-oxoglutarate aldolase, mitochondrial {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENCOP_c001G02673 {ECO:0000313|EMBL:OQE47369.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE47369.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE47369.1}.
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DR EMBL; MDDG01000001; OQE47369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6VA45; -.
DR STRING; 36646.A0A1V6VA45; -.
DR OrthoDB; 1780992at2759; -.
DR Proteomes; UP000191500; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500}.
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 173
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 216
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 309 AA; 32879 MW; 4A8A452D7392915A CRC64;
MIVKPTFGVY TPLVTFFQND ESLDLHSTLE HAKRMAEGGV AGLVLQGSNG EAPHLDHGER
KSLVRAVRDH LDQQAYTGLQ LIVGCGAPSV RETLSYIAEA KASGADFALV LPPAYWVTAM
NASVIENFFL DVASQSELPI LIYNFPGVTG GIDISSDSII RLAKSNPNIV GCKLTCGNVG
KLQRVSSALS GTSFATFGGK SDFFLPALVA GSNGIIAALT NIAPKLHVKV LRYYEKGELP
AAQELQSKLS HADWALTKVG IAGVKAIVSH HFGYGTGRGR RPLGNVTIAT LSQETVAHIN
ELVELEKSL
//
