GDO2_PSEAC
ID GDO2_PSEAC Reviewed; 348 AA.
AC Q0QFQ2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Gentisate 1,2 dioxygenase 2 {ECO:0000303|PubMed:17720458};
DE Short=GDOII {ECO:0000303|PubMed:12909360};
DE EC=1.13.11.4 {ECO:0000269|PubMed:17720458};
GN Name=hbzE {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], PROTEIN SEQUENCE OF 2-16, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND INDUCTION.
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 INDUCTION.
RC STRAIN=NCIMB 9867 / P25X;
RX PubMed=12909360; DOI=10.1016/s0378-1119(03)00619-x;
RA Yeo C.C., Wong M.V.-M., Feng Y., Song K.P., Poh C.L.;
RT "Molecular characterization of an inducible gentisate 1,2-dioxygenase gene,
RT xlnE, from Pseudomonas alcaligenes NCIMB 9867.";
RL Gene 312:239-248(2003).
CC -!- FUNCTION: Involved in the degradation of gentisate. Catalyzes the
CC conversion of gentisate (2,5-dihydroxybenzoate) to maleylpyruvate. Can
CC also use other substrates such as 3-bromogentisate, 3-fluorogentisate,
CC 3-isopropylgentisate, 3-methylgentisate and 3-ethylgentisate, but is
CC unable to utilize gentisate that is substituted at the carbon-4
CC position. {ECO:0000269|PubMed:17720458}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,5-dihydroxybenzoate + O2 = 3-maleylpyruvate + H(+);
CC Xref=Rhea:RHEA:18237, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16727, ChEBI:CHEBI:58044; EC=1.13.11.4;
CC Evidence={ECO:0000269|PubMed:17720458};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18238;
CC Evidence={ECO:0000269|PubMed:17720458};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:17720458};
CC -!- ACTIVITY REGULATION: Partially inhibited by Na(+), Ca(2+) or Mn(2+) at
CC concentrations of 5 mM. Presence of 5 mM of Zn(2+), Hg(2+) or EDTA
CC results in more than 95% inhibition. {ECO:0000269|PubMed:17720458}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=113.38 uM for gentisate {ECO:0000269|PubMed:17720458};
CC KM=29.27 uM for 3-bromogentisate {ECO:0000269|PubMed:17720458};
CC KM=50.51 uM for 3-fluorogentisate {ECO:0000269|PubMed:17720458};
CC KM=31.28 uM for 3-isopropylgentisate {ECO:0000269|PubMed:17720458};
CC KM=54.80 uM for 3-methylgentisate {ECO:0000269|PubMed:17720458};
CC KM=11.55 uM for 3-ethylgentisate {ECO:0000269|PubMed:17720458};
CC Vmax=17.35 umol/min/mg enzyme with gentisate as substrate
CC {ECO:0000269|PubMed:17720458};
CC Vmax=8.41 umol/min/mg enzyme with 3-bromogentisate as substrate
CC {ECO:0000269|PubMed:17720458};
CC Vmax=20.90 umol/min/mg enzyme with 3-fluorogentisate as substrate
CC {ECO:0000269|PubMed:17720458};
CC Vmax=9.90 umol/min/mg enzyme with 3-isopropylgentisate as substrate
CC {ECO:0000269|PubMed:17720458};
CC Vmax=1.76 umol/min/mg enzyme with 3-methylgentisate as substrate
CC {ECO:0000269|PubMed:17720458};
CC Vmax=6.88 umol/min/mg enzyme with 3-ethylgentisate as substrate
CC {ECO:0000269|PubMed:17720458};
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:17720458};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:17720458};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17720458}.
CC -!- INDUCTION: Strictly inducible. Induced by 3-hydroxybenzoate and
CC gentisate. {ECO:0000269|PubMed:12909360, ECO:0000269|PubMed:17720458}.
CC -!- SIMILARITY: Belongs to the gentisate 1,2-dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; DQ394580; ABD64513.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0QFQ2; -.
DR SMR; Q0QFQ2; -.
DR BioCyc; MetaCyc:MON-18565; -.
DR GO; GO:0047922; F:gentisate 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR013096; Cupin_2.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF07883; Cupin_2; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing;
KW Iron; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17720458"
FT CHAIN 2..348
FT /note="Gentisate 1,2 dioxygenase 2"
FT /id="PRO_0000452281"
SQ SEQUENCE 348 AA; 38162 MW; 0171C2442AFBAC95 CRC64;
MSELNLGTVE DLPKDYYEQL VANNTLPLWP SLRSVLPHGK PARRTRPVIW RYADVRPDLL
RAGDLTPIEK AEGRVLVLCN PGLGLENMQV TGSIYIGLQL IQPGETAPNH KHSPSAVRFV
IEGKGGYTLV NGEKLPMEKG DLILTPPGMW HQHGHEGDGP VVWLDALDLP LIYGIDASYH
IDGEEQTLDK AAGTCTSRYR QSGLLPYSAL DRKTSFPLLR FPWQEVRESL KQFAAVTPAG
ELVQLAYVNP ETGAECLPTL GFSAIMLRPG ETIRLQRRSA SGVLHVVEGA GSVVVDDTRH
AFTEADTLAI PTHAAVTLSN ASSTEPTYLF MVDDAPLHRK LGIYEVFS
