HOA_ROSCS
ID HOA_ROSCS Reviewed; 336 AA.
AC A7NLU2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=4-hydroxy-2-oxovalerate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
DE Short=HOA {ECO:0000255|HAMAP-Rule:MF_01656};
DE EC=4.1.3.39 {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-oxopentanoate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
GN OrderedLocusNames=Rcas_2410;
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-
CC Rule:MF_01656};
CC -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01656}.
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DR EMBL; CP000804; ABU58490.1; -; Genomic_DNA.
DR RefSeq; WP_012120914.1; NC_009767.1.
DR AlphaFoldDB; A7NLU2; -.
DR SMR; A7NLU2; -.
DR STRING; 383372.Rcas_2410; -.
DR EnsemblBacteria; ABU58490; ABU58490; Rcas_2410.
DR KEGG; rca:Rcas_2410; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_049173_0_0_0; -.
DR OMA; DLYKMMD; -.
DR OrthoDB; 840579at2; -.
DR Proteomes; UP000000263; 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; 3.20.20.70; -; 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 Pfam; PF07836; DmpG_comm; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR TIGRFAMs; TIGR03217; 4OH_2_O_val_ald; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Lyase; Manganese; Metal-binding.
FT CHAIN 1..336
FT /note="4-hydroxy-2-oxovalerate aldolase"
FT /id="PRO_0000387909"
FT DOMAIN 4..254
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT ACT_SITE 16
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 12..13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT SITE 12
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ SEQUENCE 336 AA; 36222 MW; EB2D8E801A9D713F CRC64;
MNAPRLTDTT LRDGSHAMRH MFTRQHVRDI VTALDRAGVP VIEVTHGDGL AGSSLQYGFS
FVSDLDLIAE ARESAERARI AALLLPGIGT RRELKAAVER GVQVLRIATQ CTEADISEEH
FKMAKDMGLE TVGFLMMSHM RSPEFLAEQA LLMESYGADC VYVVDSAGAM LPRDAAARVR
ALKDTLRVQV GFHAHNNLGL GIGNTLAALE AGADQIDGCL RGLGAGAGNA ATELLAAVLD
RLGVNPGLDV LALMDAAEYV VAPIMPFQPF PDRDAITIGY AGVYSTFLLH AKRVGEQLGV
DPRAILIELG RRQTVAGQED WILDVALELV RKRERA
