ID   HOA2_RHIWR              Reviewed;         345 AA.
AC   A5V856;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   10-JUN-2026, entry version 99.
DE   RecName: Full=4-hydroxy-2-oxovalerate aldolase 2 {ECO:0000255|HAMAP-Rule:MF_01656};
DE            Short=HOA 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01656};
DE   AltName: Full=4-hydroxy-2-oxopentanoate aldolase 2 {ECO:0000255|HAMAP-Rule:MF_01656};
GN   OrderedLocusNames=Swit_2113;
OS   Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC
OS   105917 / EY 4224 / RW1) (Sphingomonas wittichii).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Sphingomonadales; Rhizorhabdaceae; Rhizorhabdus.
OX   NCBI_TaxID=392499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 /
RC   RW1;
RX   PubMed=20833805; DOI=10.1128/jb.01030-10;
RA   Miller T.R., Delcher A.L., Salzberg S.L., Saunders E., Detter J.C.,
RA   Halden R.U.;
RT   "Genome sequence of the dioxin-mineralizing bacterium Sphingomonas
RT   wittichii RW1.";
RL   J. Bacteriol. 192:6101-6102(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; CP000699; ABQ68472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5V856; -.
DR   SMR; A5V856; -.
DR   STRING; 392499.Swit_2113; -.
DR   PaxDb; 392499-Swit_2113; -.
DR   KEGG; swi:Swit_2113; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_049173_0_0_5; -.
DR   OrthoDB; 9803573at2; -.
DR   Proteomes; UP000001989; Chromosome.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:TreeGrafter.
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:0009098; P:L-leucine biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd07943; DRE_TIM_HOA; 1.
DR   FunFam; 1.10.8.60:FF:000042; 4-hydroxy-2-oxovalerate aldolase; 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; IPR050073; 2-IPM_HCS-like.
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   NCBIfam; NF006049; PRK08195.1; 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; Lyase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..345
FT                   /note="4-hydroxy-2-oxovalerate aldolase 2"
FT                   /id="PRO_0000387920"
FT   DOMAIN          10..262
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   ACT_SITE        22
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         18..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         19
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         201
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   345 AA;  37239 MW;  F10D8B927923165A CRC64;
     MSFDVGKDKL YIQDVTLRDG MHAIRHMYGI DHVRAIAQAL DEAGVDAIEV AHGDGLNGAS
     FNYGFGAHTD WEWLEAVADV LTRSVLTTLI LPGVGTVDEL RRAYDIGVRS VRVATHCTEA
     DVSKQHIGIA RDLGMDVSGF LMMSHMIEPE ALAQQALLME SYGAQCVYVT DSGGALDMDG
     VRARFQAYDR VLRPETQRGM HAHHNLSLGV ANSIVAAQQG AVRIDASLAG MGAGAGNAPL
     EVFIAAVDRK GWNHGCDVNA LMDAAEDLVR PLQDRPVRVD RETLALGYAG VYSSFLRHAE
     KAAADYGLDT RTILVELGRR KMVGGQEDMI VDVALDLVRE RGAAA
//