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Database: UniProt
Entry: K5BL09_MYCHD
LinkDB: K5BL09_MYCHD
Original site: K5BL09_MYCHD 
ID   K5BL09_MYCHD            Unreviewed;       349 AA.
AC   K5BL09;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=4-hydroxy-2-oxovalerate aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
DE            Short=HOA {ECO:0000256|HAMAP-Rule:MF_01656};
DE            EC=4.1.3.39 {ECO:0000256|HAMAP-Rule:MF_01656};
DE   AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
DE   AltName: Full=4-hydroxy-2-oxopentanoate aldolase {ECO:0000256|HAMAP-Rule:MF_01656};
GN   Name=mhpE {ECO:0000313|EMBL:VCT92294.1};
GN   ORFNames=C731_0181 {ECO:0000313|EMBL:EKF25794.1}, MHAS_04021
GN   {ECO:0000313|EMBL:VCT92294.1};
OS   Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS   3849) (Mycobacterium hassiacum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF25794.1, ECO:0000313|Proteomes:UP000006265};
RN   [1] {ECO:0000313|EMBL:EKF25794.1, ECO:0000313|Proteomes:UP000006265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44199 {ECO:0000313|EMBL:EKF25794.1}, and DSM 44199 / CIP
RC   105218 / JCM 12690 / 3849 {ECO:0000313|Proteomes:UP000006265};
RX   PubMed=23209251; DOI=10.1128/JB.01880-12;
RA   Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA   Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT   "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT   heat-stable mycobacterial proteins.";
RL   J. Bacteriol. 194:7010-7011(2012).
RN   [2] {ECO:0000313|EMBL:VCT92294.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mhassiacum {ECO:0000313|EMBL:VCT92294.1};
RA   Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA   Castillo E.;
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000268660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC   {ECO:0000313|Proteomes:UP000268660};
RX   PubMed=30701245; DOI=10.1128/mra.01522-18;
RA   Sanchez M., Blesa A., Sacristan-Horcajada E., Berenguer J.;
RT   "Complete genome sequence of Mycolicibacterium hassiacum DSM 44199.";
RL   Microbiol. Resour. Announc. 8:e01522-e01522(2019).
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:0000256|ARBA:ARBA00023518};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36004;
CC         Evidence={ECO:0000256|ARBA:ARBA00023518};
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:0000256|HAMAP-
CC         Rule:MF_01656};
CC   -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC       {ECO:0000256|ARBA:ARBA00008944, ECO:0000256|HAMAP-Rule:MF_01656}.
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DR   EMBL; AMRA01000008; EKF25794.1; -; Genomic_DNA.
DR   EMBL; LR026975; VCT92294.1; -; Genomic_DNA.
DR   RefSeq; WP_005623450.1; NZ_LR026975.1.
DR   AlphaFoldDB; K5BL09; -.
DR   STRING; 1122247.GCA_000379865_01928; -.
DR   KEGG; mhas:MHAS_04021; -.
DR   PATRIC; fig|1122247.3.peg.168; -.
DR   eggNOG; COG0119; Bacteria.
DR   OMA; WARENGM; -.
DR   OrthoDB; 9803573at2; -.
DR   Proteomes; UP000006265; Unassembled WGS sequence.
DR   Proteomes; UP000268660; Chromosome 1.
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; 1.10.8.60; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR03217; 4OH_2_O_val_ald; 1.
DR   PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR   Pfam; PF07836; DmpG_comm; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW   ECO:0000256|HAMAP-Rule:MF_01656};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01656};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01656};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01656};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006265}.
FT   DOMAIN          5..257
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   ACT_SITE        17
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         13..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         198
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   SITE            13
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   349 AA;  37583 MW;  C910B4E14869677F CRC64;
     MTVQLYIQDV TLRDGMHAIR HRLPVDQLRR IAAALDAAGV AAIEVAHGDG LAGSSLTYGA
     GSHSDGVWIA AAAEVITNAR LTTLLLPGIG TVHDLVGAHD LGVTSVRVAT HATEADIAAQ
     HIAKARDLGM DVSGFLMMSH MAEPTELARQ AKIMEDAGAH CVYVTDSGGR LTMRDMRDRV
     RAYREVLRPE TQIGVHAHEN LSLSVANSVV AVEEGVYRVD ASLCGHGAGA GNCPIEAFVA
     VAELYGWRHG CDLFALQDAA ETLVRPLQDR PVRVDRETLT LGYAGVYSSF LRHAEWAAER
     YGLDVRDILV EVGRRRLVGG QEDMIDDVAL DLLAGQRTTP QRELNPSFG
//
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