HOA_MYCBP
ID HOA_MYCBP Reviewed; 346 AA.
AC A1KPL9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=4-hydroxy-2-oxohexanoate aldolase {ECO:0000250|UniProtKB:P9WMK5};
DE EC=4.1.3.43 {ECO:0000250|UniProtKB:P9WMK5};
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};
DE AltName: 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};
GN Name=hsaF {ECO:0000250|UniProtKB:P9WMK5}; OrderedLocusNames=BCG_3598c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
CC -!- FUNCTION: Involved in cholesterol degradation. Catalyzes the retro-
CC aldol cleavage of 4-hydroxy-2-oxohexanoate (HOHA) to pyruvate and
CC propanal. Can also catalyze the cleavage of 4-hydroxy-2-oxopentanoate
CC (HOPA) to pyruvate and acetaldehyde. The aldehydes produced by this
CC reaction are directly channeled to the dehydrogenase HsaG.
CC {ECO:0000250|UniProtKB:P9WMK5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-hydroxy-2-oxohexanoate = propanal + pyruvate;
CC Xref=Rhea:RHEA:36003, ChEBI:CHEBI:15361, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:73142; EC=4.1.3.43;
CC Evidence={ECO:0000250|UniProtKB:P9WMK5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36004;
CC Evidence={ECO:0000250|UniProtKB:P9WMK5};
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22625;
CC Evidence={ECO:0000250|UniProtKB:P9WMK5};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P9WMK5};
CC -!- SUBUNIT: Homodimer. Forms an heterotetramer composed of two aldolase
CC (HsaF) and two dehydrogenase (HsaG) subunits.
CC {ECO:0000250|UniProtKB:P9WMK5}.
CC -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01656}.
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DR EMBL; AM408590; CAL73587.1; -; Genomic_DNA.
DR RefSeq; WP_003419250.1; NC_008769.1.
DR AlphaFoldDB; A1KPL9; -.
DR SMR; A1KPL9; -.
DR KEGG; mbb:BCG_3598c; -.
DR HOGENOM; CLU_049173_0_0_11; -.
DR OMA; DLYKMMD; -.
DR Proteomes; UP000001472; 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..346
FT /note="4-hydroxy-2-oxohexanoate aldolase"
FT /id="PRO_0000387848"
FT DOMAIN 7..259
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 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 198
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 289
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 346 AA; 36442 MW; FB8634AC62E222CE CRC64;
MTDMWDVRIT DTSLRDGSHH KRHQFTKDEV GAIVAALDAA GVPVIEVTHG DGLGGSSFNY
GFSKTPEQEL IKLAAATAKE ARIAFLMLPG VGTKDDIKEA RDNGGSICRI ATHCTEADVS
IQHFGLAREL GLETVGFLMM AHTIAPEKLA AQARIMADAG CQCVYVVDSA GALVLDGVAD
RVSALVAELG EDAQVGFHGH ENLGLGVANS VAAVRAGAKQ IDGSCRRFGA GAGNAPVEAL
IGVFDKIGVK TGIDFFDIAD AAEDVVRPAM PAECLLDRNA LIMGYSGVYS SFLKHAVRQA
ERYGVPASAL LHRAGQRKLI GGQEDQLIDI ALEIKRELDS GAAVTH
