GNTDO_RALSP
ID GNTDO_RALSP Reviewed; 355 AA.
AC O86041;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Gentisate 1,2-dioxygenase {ECO:0000303|PubMed:11133965};
DE Short=GDO {ECO:0000303|PubMed:11133965};
DE EC=1.13.11.4 {ECO:0000269|PubMed:11133965};
DE AltName: Full=Naphthalene degradation protein I;
GN Name=nagI {ECO:0000312|EMBL:AAD12619.1};
OS Ralstonia sp.
OG Plasmid pWWU2 {ECO:0000312|EMBL:AAD12619.1}.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=54061;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD12619.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=U2 {ECO:0000312|EMBL:AAD12619.1};
RX PubMed=11133965; DOI=10.1128/jb.183.2.700-708.2001;
RA Zhou N.Y., Fuenmayor S.L., Williams P.A.;
RT "nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding
RT enzymes for gentisate catabolism.";
RL J. Bacteriol. 183:700-708(2001).
CC -!- FUNCTION: Catalyzes the oxygen-dependent ring fission of gentisate
CC between the carboxyl and proximal hydroxyl groups at positions 1 and 2
CC of the aromatic ring to form maleylpyruvate. Can also catalyze
CC oxidation of alkyl- and halogenated gentisates. Exhibits higher
CC affinity for 3-substituted gentisates than for gentisate but has higher
CC activity with gentisate. {ECO:0000269|PubMed:11133965}.
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:11133965};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.4 uM for gentisate {ECO:0000269|PubMed:11133965};
CC KM=10.7 uM for 3-methylgentisate {ECO:0000269|PubMed:11133965};
CC KM=5.3 uM for 3-bromogentisate {ECO:0000269|PubMed:11133965};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC {ECO:0000269|PubMed:11133965}.
CC -!- SIMILARITY: Belongs to the gentisate 1,2-dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; AF036940; AAD12619.1; -; Genomic_DNA.
DR AlphaFoldDB; O86041; -.
DR SMR; O86041; -.
DR PRIDE; O86041; -.
DR BioCyc; MetaCyc:MON-14769; -.
DR SABIO-RK; O86041; -.
DR UniPathway; UPA00082; -.
DR GO; GO:0047922; F:gentisate 1,2-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:1901170; P:naphthalene catabolic process; IDA:UniProtKB.
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; Oxidoreductase; Plasmid.
FT CHAIN 1..355
FT /note="Gentisate 1,2-dioxygenase"
FT /id="PRO_0000421467"
SQ SEQUENCE 355 AA; 39886 MW; F16D986FCBA08FB2 CRC64;
MLDEEERITM SHELGRLEDL PQDYRDELKQ LNLVPLWPSL RAVLPPNVPT RQTQPTYWSY
QTLKPLLLKA GELTPIEKAE RRVLVLANPG HGLEKMQASA AIYLGMQLLL PGEWAPSHRH
TPNAVRMIVE GEGAYTTVDG EKCPMSRGDL ILTPTGLWHE HGHDGNEPVV WLDVLDLPLV
YYMEASYHID GERQQVDPGR GDCAWTRAGV VPTPVFQRSD KRYPLLRYPW ADTRAALLSL
AADQPEQECV QVTYVNPETG DDAENILGFY ALMLKPGQTL RLPVRSPAVV FHQIEGRSEA
RIAESTFALR EADTCCAPGY TEVTLKNLSA DQPSFIFMAD ESPLHRKLGV FENRG