HBZF_PSEAC
ID HBZF_PSEAC Reviewed; 287 AA.
AC Q0QFQ3;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Maleylpyruvate hydrolase {ECO:0000303|PubMed:7400101};
DE Short=MPH11 {ECO:0000303|PubMed:7400101};
DE EC=3.7.1.23 {ECO:0000269|PubMed:23204427, ECO:0000269|PubMed:7400101};
GN Name=hbzF {ECO:0000303|PubMed:17720458};
OS Pseudomonas alcaligenes.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=43263;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCIMB 9867 / P25X;
RX PubMed=17720458; DOI=10.1016/j.resmic.2007.06.003;
RA Yeo C.C., Tan C.L., Gao X., Zhao B., Poh C.L.;
RT "Characterization of hbzE-encoded gentisate 1,2-dioxygenase from
RT Pseudomonas alcaligenes NCIMB 9867.";
RL Res. Microbiol. 158:608-616(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=NCIMB 9867 / P25X;
RX PubMed=7400101; DOI=10.1128/jb.143.1.70-77.1980;
RA Bayly R.C., Chapman P.J., Dagley S., Di Berardino D.;
RT "Purification and some properties of maleylpyruvate hydrolase and
RT fumarylpyruvate hydrolase from Pseudomonas alcaligenes.";
RL J. Bacteriol. 143:70-77(1980).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=NCIMB 9867 / P25X;
RX PubMed=23204427; DOI=10.1128/aem.02931-12;
RA Liu K., Liu T.T., Zhou N.Y.;
RT "HbzF catalyzes direct hydrolysis of maleylpyruvate in the gentisate
RT pathway of Pseudomonas alcaligenes NCIMB 9867.";
RL Appl. Environ. Microbiol. 79:1044-1047(2013).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=NCIMB 9867 / P25X;
RX PubMed=26070679; DOI=10.1128/aem.00975-15;
RA Liu K., Xu Y., Zhou N.Y.;
RT "Identification of a specific maleate hydratase in the direct hydrolysis
RT route of the gentisate pathway.";
RL Appl. Environ. Microbiol. 81:5753-5760(2015).
CC -!- FUNCTION: Involved in the degradation of gentisate (PubMed:7400101,
CC PubMed:23204427). Catalyzes the hydrolysis of 3-maleylpyruvate, the
CC ring-cleavage product of gentisate (PubMed:7400101, PubMed:23204427).
CC {ECO:0000269|PubMed:23204427, ECO:0000269|PubMed:7400101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-maleylpyruvate + H2O = H(+) + maleate + pyruvate;
CC Xref=Rhea:RHEA:47956, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16727, ChEBI:CHEBI:30780; EC=3.7.1.23;
CC Evidence={ECO:0000269|PubMed:23204427, ECO:0000269|PubMed:7400101};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47957;
CC Evidence={ECO:0000269|PubMed:23204427, ECO:0000269|PubMed:7400101};
CC -!- ACTIVITY REGULATION: Activated by Mn(2+) (PubMed:7400101,
CC PubMed:23204427). Inhibited by Ni(2+), Cd(2+), Co(2+) or Cu(2+)
CC (PubMed:23204427). {ECO:0000269|PubMed:23204427,
CC ECO:0000269|PubMed:7400101}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.9 uM for maleylpyruvate {ECO:0000269|PubMed:23204427};
CC pH dependence:
CC Optimum pH is 7.2-7.7 (PubMed:7400101). Optimum pH is 7.6
CC (PubMed:23204427). {ECO:0000269|PubMed:23204427,
CC ECO:0000269|PubMed:7400101};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:23204427};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23204427}.
CC -!- INDUCTION: Induced by 3-hydroxybenzoate. {ECO:0000269|PubMed:23204427}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant can still grow on gentisate.
CC {ECO:0000269|PubMed:26070679}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; DQ394580; ABD64512.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0QFQ3; -.
DR SMR; Q0QFQ3; -.
DR KEGG; ag:ABD64512; -.
DR BioCyc; MetaCyc:MON-14773; -.
DR BRENDA; 3.7.1.23; 5088.
DR GO; GO:0102054; F:maleylpyruvate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.850.10; -; 1.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; SSF56529; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Hydrolase; Metal-binding; Pyruvate.
FT CHAIN 1..287
FT /note="Maleylpyruvate hydrolase"
FT /id="PRO_0000452282"
FT BINDING 143
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6P587"
FT BINDING 145
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6P587"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:Q6P587"
SQ SEQUENCE 287 AA; 31208 MW; 58FEBF6E77AB253E CRC64;
MKICRFNENR LGVVDGDEVL DVTEALSVLP SYEYPLPGYD PLIKHLDALL ARIETLIKDA
PRILLADVRL LSPVANPGKI IAAPINYTRH LQEVLADSAI NNGVASFTQH IKKSGLFLKA
NSSLAGAGEG VALSHQDRRN DHEVELAIVI GKTARNVPRE KSLEYVAGYC IGIDMTVRGP
EERSFRKSPD SYTILGPWLV TRDEIDSPGE LQMSLKVNGE VRQNANTSDL ILGVEELVEF
ASSFYTLHPG DVIISGTPEG VGPVNPGDAM LAEIERIGTM TIAIRSV
