HOA2_RHIWR
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 03-AUG-2022, entry version 83.
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; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; 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 / RW1;
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., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Halden R.U., Miller T.R., Salzberg S.L., Eisen J.A.,
RA Richardson P.;
RT "Complete sequence of chromosome of Sphingomonas wittichii RW1.";
RL Submitted (MAY-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; CP000699; ABQ68472.1; -; Genomic_DNA.
DR RefSeq; WP_011952949.1; NC_009511.1.
DR AlphaFoldDB; A5V856; -.
DR SMR; A5V856; -.
DR STRING; 392499.Swit_2113; -.
DR EnsemblBacteria; ABQ68472; ABQ68472; Swit_2113.
DR KEGG; swi:Swit_2113; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_049173_0_0_5; -.
DR OMA; WARENGM; -.
DR OrthoDB; 840579at2; -.
DR Proteomes; UP000001989; 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..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
