ID A0A1K0FPZ5_9ACTN Unreviewed; 346 AA.
AC A0A1K0FPZ5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BG844_08120 {ECO:0000313|EMBL:OJF14784.1};
OS Couchioplanes caeruleus subsp. caeruleus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Couchioplanes.
OX NCBI_TaxID=56427 {ECO:0000313|EMBL:OJF14784.1, ECO:0000313|Proteomes:UP000182486};
RN [1] {ECO:0000313|EMBL:OJF14784.1, ECO:0000313|Proteomes:UP000182486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43634 {ECO:0000313|EMBL:OJF14784.1,
RC ECO:0000313|Proteomes:UP000182486};
RA Sheehan J., Caffrey P.;
RT "Couchioplanes caeruleus draft genome sequence.";
RL Submitted (SEP-2016) 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:OJF14784.1}.
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DR EMBL; MEIA01000086; OJF14784.1; -; Genomic_DNA.
DR RefSeq; WP_071804266.1; NZ_MEIA01000086.1.
DR AlphaFoldDB; A0A1K0FPZ5; -.
DR Proteomes; UP000182486; 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:UP000182486}.
FT DOMAIN 12..264
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 20..21
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 21
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 203
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 294
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT SITE 20
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ SEQUENCE 346 AA; 36117 MW; 85CE63DE8FB2C897 CRC64;
MPPRPFSADL DVRITDSALR DGSHAKRHQF TAAEVASVVA ALDAAGVPVI EVAHGDGLGG
SSFTYGLSRT PEQELIEVAV RTATRAKIAF LMLPGVGVVD DIRVAAGNGA SVCRIATHCT
EADIAVQHFG LARERGLETV GFLMMSHSQP PEALAKQARI MADAGCQCVY VVDSAGALVL
DQVADRVAAL VAELGDDAQV GFHGHENLGL GVANSVLAVR AGAAQIDGST RRFGAGAGNT
PVEAFVGVCD KLGIRTGVDF FAIVDAAEDV VRPAMAQECL LDRLSLTMGY AGVYSSFLTH
AFALSQRYGV PGAEILVRAG ERRLVGGQED QLIDIAVQLR QEAAQS
//
