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HOA_THERP
ID   HOA_THERP               Reviewed;         356 AA.
AC   B9L2J0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=trd_1392;
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC   Thermomicrobium.
OX   NCBI_TaxID=309801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA   Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA   Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
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; CP001275; ACM06249.1; -; Genomic_DNA.
DR   RefSeq; WP_015922341.1; NC_011959.1.
DR   AlphaFoldDB; B9L2J0; -.
DR   SMR; B9L2J0; -.
DR   STRING; 309801.trd_1392; -.
DR   PRIDE; B9L2J0; -.
DR   EnsemblBacteria; ACM06249; ACM06249; trd_1392.
DR   KEGG; tro:trd_1392; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_049173_0_0_0; -.
DR   OMA; DLYKMMD; -.
DR   OrthoDB; 840579at2; -.
DR   Proteomes; UP000000447; 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.
FT   CHAIN           1..356
FT                   /note="4-hydroxy-2-oxovalerate aldolase"
FT                   /id="PRO_0000387927"
FT   DOMAIN          7..257
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   ACT_SITE        19
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         15..16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         16
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         198
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT   SITE            15
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   356 AA;  38125 MW;  AF99494DBA9E947B CRC64;
     MKTLTPPRVT DTTLRDGSHA MRHQFTREQV RAIVAALDEA GVPVIEVTHG DGLAGSSIQY
     GFSATSELEL IEEAAKTAKR AKIAALLLPG IGTRRELSAA IERGIKVVRI ATQCTEADIS
     EQHFGMAKEM GLETVGFLMM AHMRPPEFLA EQAALMESYG ADCVYIVDSA GAMLPDDVRR
     RVAALKERLS IQVGFHAHNN LGLAIGNTLA AIEEGADQVD GCLRGLGAGA GNAPTELIAA
     VLDKLGINPG LDVFKLMDAA EYIVAPIMPY QPIPDRDAIT IGYAGVYSTF LLHARHIAAE
     FGLDPREILV ELGRRQAVAG QEDWILDVAL DILRRKRAAE GAGDAREPAA AERSAD
 
 
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