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Database: UniProt
Entry: A0A1V4LX53_9PSED
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Original site: A0A1V4LX53_9PSED 
ID   A0A1V4LX53_9PSED        Unreviewed;       345 AA.
AC   A0A1V4LX53;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=BZ163_05480 {ECO:0000313|EMBL:OPK11242.1};
OS   Pseudomonas sp. VI4.1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1941346 {ECO:0000313|EMBL:OPK11242.1, ECO:0000313|Proteomes:UP000189889};
RN   [1] {ECO:0000313|EMBL:OPK11242.1, ECO:0000313|Proteomes:UP000189889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VI4.1 {ECO:0000313|EMBL:OPK11242.1,
RC   ECO:0000313|Proteomes:UP000189889};
RA   Imperato V., Thijs S., Mcammond B., Douwen Y., Broeders P., Kowalkowski L.,
RA   Gawronski S., Vangronsveld J.;
RT   "Draft genome sequence of Pseudomonas yorbenii VI4.1, a hydrocarbonoclastic
RT   isolate from crude oil contaminated soil in Bobrka, Poland.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:OPK11242.1}.
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DR   EMBL; MULM01000104; OPK11242.1; -; Genomic_DNA.
DR   RefSeq; WP_004574815.1; NZ_MULM01000104.1.
DR   AlphaFoldDB; A0A1V4LX53; -.
DR   Proteomes; UP000189889; 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}.
FT   DOMAIN          9..261
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   ACT_SITE        21
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         17..18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         18
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         202
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   BINDING         291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
FT   SITE            17
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01656"
SQ   SEQUENCE   345 AA;  37458 MW;  EFB2F08AC6CA4311 CRC64;
     MTFNPGKKLY ISDVTLRDGS HAIRHQYSIQ NVQDIARALD KARVDSIEVT HGDGLQGSSF
     NYGFGAHSDL EWIEAAADVI QHARITVLLL PGIGTVHDLK AAYDAGARSV RVATHCTEAD
     VSRQHIEYAR ELGMDTVGFL MMSHMIPAEQ LAAQGKLMES YGAQCIYMAD SGGAMNMNDI
     RDRMRAFKAA LNPETQTGMH AHHNLSLGVA NSIIAVEEGC DRIDASLAGM GAGAGNAPLE
     VFIAAAERMG WNHGTDLYAL MDAADDIVRP LQDRPVRVDR ETLGLGYAGV YSSFLRHAEV
     AAAKYGLKTL DILVELGRRR MVGGQEDMIV DVALDLLATR KEQHA
//
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