ID A0A132TC20_9MYCO Unreviewed; 351 AA.
AC A0A132TC20;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=ASJ79_16160 {ECO:0000313|EMBL:KWX68821.1};
OS Mycobacterium sp. NAZ190054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX68821.1, ECO:0000313|Proteomes:UP000070146};
RN [1] {ECO:0000313|EMBL:KWX68821.1, ECO:0000313|Proteomes:UP000070146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX68821.1,
RC ECO:0000313|Proteomes:UP000070146};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KWX68821.1}.
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DR EMBL; LMVQ01000022; KWX68821.1; -; Genomic_DNA.
DR RefSeq; WP_067952882.1; NZ_LMVQ01000022.1.
DR AlphaFoldDB; A0A132TC20; -.
DR OrthoDB; 9803573at2; -.
DR Proteomes; UP000070146; Unassembled WGS sequence.
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:UP000070146}.
FT DOMAIN 14..266
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT ACT_SITE 26
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 22..23
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 23
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 205
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 207
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT SITE 22
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ SEQUENCE 351 AA; 37419 MW; 5F29C4A5E7E30634 CRC64;
MSTEGVYFNP VWDVRMTDTS LRDGSHHKRH QFTKDEVHAI VAALDAAGVP VIEVTHGDGL
GGSSFNYGFS KTPEQELIKL AAETAKESKI AFLMLPGVGT KEDIKEAQNN GGSICRIATH
CTEADVSIQH FGLARELGLE TVGFLMMSHT IPPEKLAKQA RIMADAGCQC VYVVDSAGAL
VLEGVRDRVA ALVAELGSDA QVGFHGHENL GLGVANSIEA VRAGAKQIDG SCRRFGAGAG
NAPVEALIGV FDKIGVKTGI DFFDIADAAE EVVAPAMPAE CLLDRNALIM GYSGVYSSFL
KHAIRQSERY GVPAHKLLHR AGQRKLIGGQ EDQLIDIALE IKREMEASPA S
//
