ID E6SI03_THEM7 Unreviewed; 340 AA.
AC E6SI03;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 OrderedLocusNames=Tmar_1781 {ECO:0000313|EMBL:ADU51883.1};
OS Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 /
OS 7p75a).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX NCBI_TaxID=644966 {ECO:0000313|EMBL:ADU51883.1, ECO:0000313|Proteomes:UP000008915};
RN [1] {ECO:0000313|EMBL:ADU51883.1, ECO:0000313|Proteomes:UP000008915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC {ECO:0000313|Proteomes:UP000008915};
RX PubMed=21304738;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Del Rio T.G., Tice H., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Schneider S., Rohde M., Goker M., Pukall R., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75a).";
RL Stand. Genomic Sci. 3:337-345(2010).
RN [2] {ECO:0000313|Proteomes:UP000008915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a
RC {ECO:0000313|Proteomes:UP000008915};
RX DOI=10.4056/sigs.1373474;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Schneider S.,
RA Rohde M., Goker M., Pukall R., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Detter J.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75aT).";
RL Stand. Genomic Sci. 3:337-345(2010).
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; CP002344; ADU51883.1; -; Genomic_DNA.
DR RefSeq; WP_013496184.1; NC_014831.1.
DR AlphaFoldDB; E6SI03; -.
DR STRING; 644966.Tmar_1781; -.
DR KEGG; tmr:Tmar_1781; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_049173_0_0_9; -.
DR OrthoDB; 9804858at2; -.
DR Proteomes; UP000008915; 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; 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:UP000008915}.
FT DOMAIN 4..254
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT ACT_SITE 16
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 12..13
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT SITE 12
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ SEQUENCE 340 AA; 36024 MW; A0888696C9B0C559 CRC64;
MNPPRLTDTT LRDGSHAMKH RFTSEQVRAI VTALDEAGVP VIEVSHGDGL GGSSIQYGFS
LEPELDLIAE ATRTARRARI AVLLLPGIGT KDLLERAAEL GVRVARIATQ CTEADISEQH
FGIAKKLGLE AVGFLMMAHI RPPEVLVEQA KLMESYGADC VYIVDSAGAM LPPDVKARVS
ALKEALSIQV GFHAHNNLGA AIGNTLAALE AGADQVDGSL RGLGAGAGNA ATEVLAAGLD
KLGLNPGLDV FRLMDAAEYV VAPLMPYQPV PDRDSLTIGY AGVYSTFLLH AKHVASRFGL
DARDILVELG RRQAVAGQED WIVDVAVDLV EQEAGQRHAS
//
