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HOA2_MYCSK
ID   HOA2_MYCSK              Reviewed;         349 AA.
AC   A1UQA1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Mkms_5835;
OS   Mycobacterium sp. (strain KMS).
OG   Plasmid pMKMS02.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of plasmid pMKMS02 of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) 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; CP000520; ABL95009.1; -; Genomic_DNA.
DR   RefSeq; WP_011562978.1; NC_008704.1.
DR   AlphaFoldDB; A1UQA1; -.
DR   SMR; A1UQA1; -.
DR   EnsemblBacteria; ABL95009; ABL95009; Mkms_5835.
DR   KEGG; mkm:Mkms_5835; -.
DR   HOGENOM; CLU_049173_0_0_11; -.
DR   OMA; WARENGM; -.
DR   OrthoDB; 840579at2; -.
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; Plasmid.
FT   CHAIN           1..349
FT                   /note="4-hydroxy-2-oxovalerate aldolase 2"
FT                   /id="PRO_0000387859"
FT   DOMAIN          16..268
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   ACT_SITE        28
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         24..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         25
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         207
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         209
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   SITE            24
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   349 AA;  37196 MW;  45E766A870730D8C CRC64;
     MTETVSRPHA TEGAALYIQD VTLRDGMHAM RHRISPEKVA AIAGALDTAG VDAIEVTHGD
     GLAGHSLTYG PGSNTDWEWI EAAADVVHRA KLTTLLLPGV GTVRELEHAY KLGVTSVRVA
     THCTEADVSA QHIGTARELG MDVSGFLMMS HLAEPSHLAA QAKLMESYGA HCVYVTDSGG
     RLTMGSVRDR VRAYRDVLDA GTQIGIHAHQ NLSLSVANTV VAVEEGVTRV DASLAGHGAG
     AGNCPIEPFI AVADLHGWKH NCDLFGLQDA ADDIVRPLQD RPVQVDRETL TLGYAGVYSS
     FLRHAEAAAK QYGLDTRAIL LAVGERGLVG GQEDLIPDIA LDLQQNLRR
 
 
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