HOA_PSEUF
ID HOA_PSEUF Reviewed; 345 AA.
AC P51016;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=4-hydroxy-2-oxovalerate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
DE Short=HOA {ECO:0000255|HAMAP-Rule:MF_01656};
DE EC=4.1.3.39 {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-keto-pentanoic acid aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
DE AltName: Full=4-hydroxy-2-oxopentanoate aldolase {ECO:0000255|HAMAP-Rule:MF_01656};
GN Name=dmpG;
OS Pseudomonas sp. (strain CF600).
OG Plasmid pVI150.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=79676;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=CF600;
RX PubMed=1732207; DOI=10.1128/jb.174.3.711-724.1992;
RA Shingler V., Marklund U., Powlowski J.;
RT "Nucleotide sequence and functional analysis of the complete phenol/3,4-
RT dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600.";
RL J. Bacteriol. 174:711-724(1992).
RN [2]
RP PROTEIN SEQUENCE OF 2-7, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH DMPF, AND PH DEPENDENCE.
RC STRAIN=CF600;
RX PubMed=8419288; DOI=10.1128/jb.175.2.377-385.1993;
RA Powlowski J., Sahlman L., Shingler V.;
RT "Purification and properties of the physically associated meta-cleavage
RT pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde
RT dehydrogenase (acylating) from Pseudomonas sp. strain CF600.";
RL J. Bacteriol. 175:377-385(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DMPF; NAD; MANGANESE
RP AND OXALATE, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=CF600;
RX PubMed=12764229; DOI=10.1073/pnas.1236794100;
RA Manjasetty B.A., Powlowski J., Vrielink A.;
RT "Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a
RT reactive and volatile intermediate.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6992-6997(2003).
CC -!- FUNCTION: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-
CC oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-
CC cleavage pathway for the degradation of aromatic compounds such as
CC phenols, cresols and catechols. {ECO:0000269|PubMed:1732207}.
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:0000255|HAMAP-
CC Rule:MF_01656, ECO:0000269|PubMed:8419288};
CC -!- ACTIVITY REGULATION: Six- to eight-fold activated by Mn(2+). Retains
CC residual activity after EDTA treatment in vitro. Also activated by NADH
CC and, to a lesser extent, by NAD(+). Strongly inhibited by Zn(2+).
CC Mg(2+) and Ca(2+) have no effect on enzymatic activity.
CC {ECO:0000269|PubMed:8419288}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:8419288};
CC -!- PATHWAY: Aromatic compound metabolism; benzoate degradation via
CC hydroxylation.
CC -!- PATHWAY: Aromatic compound metabolism; phenol degradation.
CC -!- SUBUNIT: Heterotetramer composed of two DmpG (aldolase) and two DmpF
CC (dehydrogenase) subunits, which allows a direct channeling of
CC acetaldehyde between the two active sites.
CC {ECO:0000269|PubMed:12764229, ECO:0000269|PubMed:8419288}.
CC -!- SIMILARITY: Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01656}.
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DR EMBL; X60835; CAA43227.1; -; Genomic_DNA.
DR PDB; 1NVM; X-ray; 1.70 A; A/C/E/G=1-345.
DR PDBsum; 1NVM; -.
DR AlphaFoldDB; P51016; -.
DR SMR; P51016; -.
DR IntAct; P51016; 1.
DR KEGG; ag:CAA43227; -.
DR BioCyc; MetaCyc:MON-12778; -.
DR BRENDA; 4.1.3.39; 5085.
DR UniPathway; UPA00156; -.
DR UniPathway; UPA00728; -.
DR EvolutionaryTrace; P51016; -.
DR GO; GO:0008701; F:4-hydroxy-2-oxovalerate aldolase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
DR GO; GO:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0019336; P:phenol-containing compound catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07943; DRE_TIM_HOA; 1.
DR Gene3D; 3.20.20.70; -; 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 Pfam; PF07836; DmpG_comm; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR TIGRFAMs; TIGR03217; 4OH_2_O_val_ald; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Lyase; Manganese; Metal-binding; Plasmid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8419288"
FT CHAIN 2..345
FT /note="4-hydroxy-2-oxovalerate aldolase"
FT /id="PRO_0000079938"
FT DOMAIN 9..261
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT ACT_SITE 21
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 17..18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 18
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656,
FT ECO:0000269|PubMed:12764229"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656,
FT ECO:0000269|PubMed:12764229"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656,
FT ECO:0000269|PubMed:12764229"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT SITE 17
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01656"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1NVM"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:1NVM"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1NVM"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:1NVM"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 280..288
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 309..319
FT /evidence="ECO:0007829|PDB:1NVM"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:1NVM"
SQ SEQUENCE 345 AA; 37471 MW; 8B38B37A8A0EFEE0 CRC64;
MTFNPSKKLY ISDVTLRDGS HAIRHQYTLD DVRAIARALD KAKVDSIEVA HGDGLQGSSF
NYGFGRHTDL EYIEAVAGEI SHAQIATLLL PGIGSVHDLK NAYQAGARVV RVATHCTEAD
VSKQHIEYAR NLGMDTVGFL MMSHMIPAEK LAEQGKLMES YGATCIYMAD SGGAMSMNDI
RDRMRAFKAV LKPETQVGMH AHHNLSLGVA NSIVAVEEGC DRVDASLAGM GAGAGNAPLE
VFIAVAERLG WNHGTDLYTL MDAADDIVRP LQDRPVRVDR ETLGLGYAGV YSSFLRHAEI
AAAKYNLKTL DILVELGHRR MVGGQEDMIV DVALDLLAAH KENRA
