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HOA_METSB
ID   HOA_METSB               Reviewed;         346 AA.
AC   B8ESV2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=Msil_1479;
OS   Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS   13906 / BL2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=395965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2;
RX   PubMed=20472789; DOI=10.1128/jb.00506-10;
RA   Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA   Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT   "Complete genome sequence of the aerobic facultative methanotroph
RT   Methylocella silvestris BL2.";
RL   J. Bacteriol. 192:3840-3841(2010).
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; CP001280; ACK50437.1; -; Genomic_DNA.
DR   RefSeq; WP_012590507.1; NC_011666.1.
DR   AlphaFoldDB; B8ESV2; -.
DR   SMR; B8ESV2; -.
DR   STRING; 395965.Msil_1479; -.
DR   EnsemblBacteria; ACK50437; ACK50437; Msil_1479.
DR   KEGG; msl:Msil_1479; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_049173_0_0_5; -.
DR   OMA; DLYKMMD; -.
DR   OrthoDB; 840579at2; -.
DR   Proteomes; UP000002257; 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;
KW   Reference proteome.
FT   CHAIN           1..346
FT                   /note="4-hydroxy-2-oxovalerate aldolase"
FT                   /id="PRO_0000387842"
FT   DOMAIN          9..261
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   ACT_SITE        21
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         17..18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         18
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         202
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   SITE            17
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   346 AA;  37079 MW;  F1002FB934EF9D37 CRC64;
     MARINPNKLY VQDVTLRDGM HSVRHQYSLD AVRAIARALD RAHVDAIEIS HGDGITGSTF
     NYGFGAHDDT EWIAAVAGEC KFSRITVLLL PGIGTVHDLK YACEAGARSV RVATHCTEAD
     VSRQHIEAGR KLGMDTVGFL MMAHMAPVEK LVEQALLMES YGAECVYVTD SAGALLPKQY
     AERVKAVRGA LKPETEIGVH THHNLTLGVA NAVAGIEAGA VRVDASLAGM GAGAGNAPLE
     ALIAVLDRMG IETGCDLHML MDAADDLVRP LQDRPVRVDR ESLSLGYAGV YSSFLRHAES
     ASKLYGVDTR DILTELGKRR MVGGQEDMIV DVALDILKSH GAEAAQ
 
 
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