GRDC_RHIRD
ID GRDC_RHIRD Reviewed; 327 AA.
AC Q60FX6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Gamma-resorcylate decarboxylase {ECO:0000303|PubMed:15474471};
DE EC=4.1.1.103 {ECO:0000269|PubMed:15474471};
DE AltName: Full=2,6-dihydroxybenzoate decarboxylase {ECO:0000303|PubMed:15474471};
DE AltName: Full=Reversible gamma-RA decarboxylase {ECO:0000303|PubMed:15474471};
GN Name=rdc {ECO:0000303|PubMed:15474471};
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND MUTAGENESIS OF HIS-164 AND HIS-218.
RC STRAIN=WU-0108;
RX PubMed=15474471; DOI=10.1016/j.bbrc.2004.09.091;
RA Ishii Y., Narimatsu Y., Iwasaki Y., Arai N., Kino K., Kirimura K.;
RT "Reversible and nonoxidative gamma-resorcylic acid decarboxylase:
RT characterization and gene cloning of a novel enzyme catalyzing
RT carboxylation of resorcinol, 1,3-dihydroxybenzene, from Rhizobium
RT radiobacter.";
RL Biochem. Biophys. Res. Commun. 324:611-620(2004).
CC -!- FUNCTION: Involved in the gamma-resorcylate (2,6-dihydroxybenzoate)
CC catabolism (PubMed:15474471). Catalyzes the reversible decarboxylation
CC of gamma-resorcylate to resorcinol (PubMed:15474471). Also catalyzes
CC the decarboxylation of 2,3-dihydroxybenzoate to catechol, but does not
CC act on 2-hydroxybenzoic acid 3-hydroxybenzoic acid, 4-hydroxybenzoic
CC acid, 3,4-dihydroxybenzoic acid, 2,5-dihydroxybenzoic acid, 2,3,4-
CC trihydroxybenzoic acid, 3,4,5-trihydroxybenzoic acid, 4-aminobenzoic
CC acid, o-hydroxyphenylacetic acid and vanillic acid (PubMed:15474471).
CC Resorcinol and catechol can both be carboxylated by the reverse
CC reaction (PubMed:15474471). {ECO:0000269|PubMed:15474471}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6-dihydroxybenzoate + H(+) = CO2 + resorcinol;
CC Xref=Rhea:RHEA:49464, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:27810, ChEBI:CHEBI:131450; EC=4.1.1.103;
CC Evidence={ECO:0000269|PubMed:15474471};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49465;
CC Evidence={ECO:0000269|PubMed:15474471};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-dihydroxybenzoate + H(+) = catechol + CO2;
CC Xref=Rhea:RHEA:21492, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:18135, ChEBI:CHEBI:36654;
CC Evidence={ECO:0000269|PubMed:15474471};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q60GU1};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q60GU1};
CC -!- ACTIVITY REGULATION: Insensitive to oxygen. Decarboxylation and
CC carboxylation are inhibited by AgNO(3) and by diethyl pyrocarbonate, a
CC histidine residue-specific inhibitor. Decarboxylation is also inhibited
CC by HgCl(2) and activated by MgCl(2). {ECO:0000269|PubMed:15474471}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 mM for gamma-resorcylate (for decarboxylation)
CC {ECO:0000269|PubMed:15474471};
CC KM=0.035 mM for resorcinol (for carboxylation)
CC {ECO:0000269|PubMed:15474471};
CC KM=0.035 mM for catechol (for carboxylation)
CC {ECO:0000269|PubMed:15474471};
CC pH dependence:
CC Optimum pH is 7.0 for decarboxylation. {ECO:0000269|PubMed:15474471};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius for decarboxylation.
CC Optimum temperature is 45 degrees Celsius for carboxylation.
CC {ECO:0000269|PubMed:15474471};
CC -!- PATHWAY: Aromatic compound metabolism. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15474471}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ACMSD family. {ECO:0000305}.
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DR EMBL; AB185333; BAD61045.1; -; Genomic_DNA.
DR SMR; Q60FX6; -.
DR BRENDA; 4.1.1.103; 200.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR032465; ACMSD.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR21240; PTHR21240; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Direct protein sequencing; Lyase; Metal-binding; Zinc.
FT CHAIN 1..327
FT /note="Gamma-resorcylate decarboxylase"
FT /id="PRO_0000454503"
FT ACT_SITE 287
FT /evidence="ECO:0000250|UniProtKB:Q60GU1"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q60GU1"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q60GU1"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q60GU1"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q60GU1"
FT MUTAGEN 164
FT /note="H->Q: Loss of both decarboxylation and carboxylation
FT activities."
FT /evidence="ECO:0000269|PubMed:15474471"
FT MUTAGEN 218
FT /note="H->Q: Loss of both decarboxylation and carboxylation
FT activities."
FT /evidence="ECO:0000269|PubMed:15474471"
SQ SEQUENCE 327 AA; 37431 MW; 9F89EE385BC3EAF2 CRC64;
MQGKVALEEH FAIPETLQDS AGFVPGDYWK ELQHRLLDIQ DTRLKLMDAH GIETMILSLN
APAVQAIPDR KKAIEIARRA NDVLAEECAR RPDRFLAFAA LPLQDPDAAT QELQRCVNDL
GFVGALVNGF SQEGDGQTPL YYDLPQYRPF WGEVEKLDVP FYLHPRNPLP QDSRIYDGHP
WLLGPTWAFA QETAVHALRL MASGLFDAHP RLNIILGHMG EGLPYMMWRI DHRNAWVKLP
PRYPAKRRFV DYFNENFHIT TSGNFRTQTL IDAILEIGAD RILFSTDWPF ENIDHASDWF
NATTIAEADR VKIGRTNARR LFKLDGR
