HOA_STRCO
ID HOA_STRCO Reviewed; 338 AA.
AC Q99PZ1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=SCP1.301;
GN and
GN OrderedLocusNames=SCP1.53c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OG Plasmid SCP1.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145; PLASMID=SCP1;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL589148; CAC36575.1; -; Genomic_DNA.
DR EMBL; AL589148; CAC36826.1; -; Genomic_DNA.
DR RefSeq; NP_639628.1; NC_003903.1.
DR RefSeq; NP_639910.1; NC_003903.1.
DR RefSeq; WP_011039354.1; NC_003903.1.
DR AlphaFoldDB; Q99PZ1; -.
DR SMR; Q99PZ1; -.
DR GeneID; 1095132; -.
DR GeneID; 1095383; -.
DR KEGG; sco:SCP1.301; -.
DR KEGG; sco:SCP1.53c; -.
DR PATRIC; fig|100226.15.peg.8001; -.
DR HOGENOM; CLU_049173_0_0_11; -.
DR InParanoid; Q99PZ1; -.
DR OMA; CALMVRF; -.
DR PhylomeDB; Q99PZ1; -.
DR Proteomes; UP000001973; Plasmid SCP1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IBA:GO_Central.
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 GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
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; Plasmid;
KW Reference proteome.
FT CHAIN 1..338
FT /note="4-hydroxy-2-oxovalerate aldolase"
FT /id="PRO_0000387924"
FT DOMAIN 6..256
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT ACT_SITE 18
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 14..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 15
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 168
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 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT SITE 14
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ SEQUENCE 338 AA; 35318 MW; ECC032842A1CF3BC CRC64;
MNPPTVTVHD STLRDGQHAV RHQLDADQIR AYAVAADTAG VPVLEVGHGN GIGASSRQVG
LSKTDDATML TTAREAMPHS RLATLMLPGW ATSTDLRSAI RHGVDIVRVA AHCTEADVTE
RHLGVIRDLG AEAQGVLLMS HLAAPDELAA QCQRMVGYGA QAVCIFDSAG TYLPEDVTAR
ITAITTAVDV PVAFHGHNNL GMAVANSLAA VRAGARVLDA CARGFGAGAG NTQLEVLVAV
LERYGHPTGI DLRLVAQAAD LAERTLMPAP PTIDSTSLVS GLAGVFSGFK KPVLAAAQRA
GVSPWDVFVE LGRRRVLAGQ EDLIPDAINT LTSMGERP
