ID R7Y2R8_9ACTN Unreviewed; 342 AA.
AC R7Y2R8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=CF8_0278 {ECO:0000313|EMBL:EON25570.1};
OS Nocardioides sp. CF8.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=110319 {ECO:0000313|EMBL:EON25570.1, ECO:0000313|Proteomes:UP000015971};
RN [1] {ECO:0000313|EMBL:EON25570.1, ECO:0000313|Proteomes:UP000015971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF8 {ECO:0000313|EMBL:EON25570.1,
RC ECO:0000313|Proteomes:UP000015971};
RX PubMed=23833136;
RA Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT of Its Metabolic Capabilities.";
RL Genome Announc. 1:e00439-e00439(2013).
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: 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:EON25570.1}.
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DR EMBL; ASEP01000015; EON25570.1; -; Genomic_DNA.
DR RefSeq; WP_010831341.1; NZ_CM001852.1.
DR AlphaFoldDB; R7Y2R8; -.
DR STRING; 110319.CF8_0278; -.
DR PATRIC; fig|110319.3.peg.864; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_049173_0_0_11; -.
DR OrthoDB; 9803573at2; -.
DR Proteomes; UP000015971; Chromosome.
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:UP000015971}.
FT DOMAIN 3..255
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT ACT_SITE 15
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 11..12
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 12
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 194
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT SITE 11
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ SEQUENCE 342 AA; 36428 MW; 430AC7963F8981D6 CRC64;
MKLFIQDVTL RDGMHAIRHR IQPGRVGEIV AALDAAGVGG IEVTHGDGLS GGSLNYGPGS
HTDWAWIEAA AENITNARLT TLLLPGIGTI EDLKRAHAMG VRSVRVATHC TEADVSAQHI
ATARELGMDV SGFLMMSHMA DAATLAGQAK LMESYGAHCV YVTDSGGRLM MDGVRERMRA
YRDVLDPATE IGIHAHENLS LSVANSMVAV EEGVTRVDAS LTGLGAGAGN CPIEPFIAVA
DLNGWDHGCD LFALQDAAED LVRPLQDRPV RVDRETLTLG YAGVYGSFLR HTETAAERYG
VDSRELLLEV GRRGLVGGQE DMIVDIALNL VAARQEEPAP AS
//
