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HOA_MYCTO
ID   HOA_MYCTO               Reviewed;         346 AA.
AC   P9WMK4; L0TFQ6; P71867; Q7D5C4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
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=MT3638;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK47997.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK47997.1; ALT_INIT; Genomic_DNA.
DR   PIR; G70675; G70675.
DR   RefSeq; WP_003419250.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMK4; -.
DR   SMR; P9WMK4; -.
DR   EnsemblBacteria; AAK47997; AAK47997; MT3638.
DR   KEGG; mtc:MT3638; -.
DR   PATRIC; fig|83331.31.peg.3919; -.
DR   HOGENOM; CLU_049173_0_0_11; -.
DR   Proteomes; UP000001020; 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_0000427288"
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
 
 
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