ID A0A117RST3_9ACTN Unreviewed; 326 AA.
AC A0A117RST3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=4-hydroxy-2-oxovalerate aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
DE Short=HOA {ECO:0000256|HAMAP-Rule:MF_01656};
DE EC=4.1.3.39 {ECO:0000256|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-oxopentanoate aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
GN ORFNames=AQJ58_36725 {ECO:0000313|EMBL:KUO07311.1};
OS Streptomyces sp. DSM 15324.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1739111 {ECO:0000313|EMBL:KUO07311.1, ECO:0000313|Proteomes:UP000053431};
RN [1] {ECO:0000313|EMBL:KUO07311.1, ECO:0000313|Proteomes:UP000053431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15324 {ECO:0000313|EMBL:KUO07311.1,
RC ECO:0000313|Proteomes:UP000053431};
RA Ruckert C., Winkler A., Kalinowski J., Wink J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. DSM 15324, isolated from soil.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-hydroxy-2-oxohexanoate = propanal + pyruvate;
CC Xref=Rhea:RHEA:36003, ChEBI:CHEBI:15361, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:73142; EC=4.1.3.43;
CC Evidence={ECO:0000256|ARBA:ARBA00023518};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36004;
CC Evidence={ECO:0000256|ARBA:ARBA00023518};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate;
CC Xref=Rhea:RHEA:22624, ChEBI:CHEBI:15343, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:73143; EC=4.1.3.39; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01656};
CC -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC {ECO:0000256|ARBA:ARBA00008944, ECO:0000256|HAMAP-Rule:MF_01656}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01656}.
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:KUO07311.1}.
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DR EMBL; LMXA01000041; KUO07311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117RST3; -.
DR Proteomes; UP000053431; Unassembled WGS sequence.
DR GO; GO:0008701; F:4-hydroxy-2-oxovalerate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07943; DRE_TIM_HOA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01656; HOA; 1.
DR InterPro; IPR017629; 4OH_2_O-val_aldolase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012425; DmpG_comm.
DR InterPro; IPR035685; DRE_TIM_HOA.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR03217; 4OH_2_O_val_ald; 1.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF07836; DmpG_comm; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW ECO:0000256|HAMAP-Rule:MF_01656};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01656};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01656};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01656};
KW Reference proteome {ECO:0000313|Proteomes:UP000053431}.
FT DOMAIN 1..242
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT ACT_SITE 2
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 181
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 183
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ SEQUENCE 326 AA; 34824 MW; A7D947CB2CC1CF69 CRC64;
MHAIRHRMEP ETIREIAGAL DRAGVDSIEI AHGDGLAGST LTFGSSSHTD EEWIRAVTET
VQRARVATLL VPGLGRIGDL EAAFELGVTS VRVATHCTEP DVALQHIGRA RELGMDVAAF
LMMSHGLEPK ELAANARTME AAGANCVYVT DSAGHLTPHG VRDRILAYRD VLDENTEIGI
HAHENLSLSV ANSLAAVEAG AVRVDASLAG HGAGAGNCPI EAFVAAANLY GWEHGCDVWA
LQDAADDLVR PVQDRPVRVD RETLTLGYVG VYSSYLRHAE HVAERSGLST RQILVEAGRR
KLIAGQEDML ADIALELLEQ KTGAPT
//
