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Database: UniProt
Entry: M0QJM3_9ACTN
LinkDB: M0QJM3_9ACTN
Original site: M0QJM3_9ACTN 
ID   M0QJM3_9ACTN            Unreviewed;       371 AA.
AC   M0QJM3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=GS4_15_01210 {ECO:0000313|EMBL:GAC68471.1};
OS   Gordonia soli NBRC 108243.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC68471.1, ECO:0000313|Proteomes:UP000011666};
RN   [1] {ECO:0000313|EMBL:GAC68471.1, ECO:0000313|Proteomes:UP000011666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC68471.1,
RC   ECO:0000313|Proteomes:UP000011666};
RA   Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia soli NBRC 108243.";
RL   Submitted (JAN-2013) 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:GAC68471.1}.
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DR   EMBL; BANX01000015; GAC68471.1; -; Genomic_DNA.
DR   RefSeq; WP_007620635.1; NZ_BANX01000015.1.
DR   AlphaFoldDB; M0QJM3; -.
DR   STRING; 1223545.GS4_15_01210; -.
DR   eggNOG; COG0119; Bacteria.
DR   OrthoDB; 9803573at2; -.
DR   Proteomes; UP000011666; 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:UP000011666}.
FT   DOMAIN          34..286
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   ACT_SITE        46
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         42..43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         43
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         225
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         227
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   SITE            42
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   371 AA;  38944 MW;  529B4D6D5C5E34CA CRC64;
     MNTATTSTTT TTAAGGAATG LMANARAYSD LLDIRITDSS LRDGSHHKRH QFTEAEVRAI
     VGALDGAGVP VIEVTHGDGL GGSSFNYGFS KTPEQQLIKA AAETAKRAKI AFLMLPGLGV
     KDDIRAAQDN GGQICRIATH CTEADVSIQH FGLARELGLE TVGFLMMSHS QPPEKLAEQA
     RIMADAGCQC VYVVDSAGAL VLEDVTVRVQ ALVAELGDDA QVGFHGHENL DIAVANSVNA
     IRAGAQQIDG SIRRFGAGAG NTPTEAFVGV CDKLGIRTGV DFMTIADAAQ DVVRPAMPSE
     CLVDRSSMMM GYAGCYSSFL KHAEGHAERY NVSAAAILLE AGNRKLVGGQ EDQLIDIALE
     LKKKQDADAG V
//
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