GRDC_RHOJR
ID GRDC_RHOJR Reviewed; 329 AA.
AC Q0SFL6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Gamma-resorcylate decarboxylase {ECO:0000303|PubMed:26319878};
DE Short=GRA decarboxylase {ECO:0000303|PubMed:26319878};
DE EC=4.1.1.103 {ECO:0000269|PubMed:26319878};
DE AltName: Full=2,6-dihydroxybenzoate decarboxylase {ECO:0000305};
GN Name=tsdA {ECO:0000303|PubMed:26319878};
GN OrderedLocusNames=RHA1_ro01859 {ECO:0000312|EMBL:ABG93670.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=RHA1;
RX PubMed=26319878; DOI=10.1128/aem.02422-15;
RA Kasai D., Araki N., Motoi K., Yoshikawa S., Iino T., Imai S., Masai E.,
RA Fukuda M.;
RT "Gamma-Resorcylate catabolic-pathway genes in the soil actinomycete
RT Rhodococcus jostii RHA1.";
RL Appl. Environ. Microbiol. 81:7656-7665(2015).
CC -!- FUNCTION: Involved in the gamma-resorcylate (2,6-dihydroxybenzoate)
CC catabolism (PubMed:26319878). Catalyzes the reversible decarboxylation
CC of gamma-resorcylate to resorcinol (PubMed:26319878).
CC {ECO:0000269|PubMed:26319878}.
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:26319878};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49465;
CC Evidence={ECO:0000269|PubMed:26319878};
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 -!- PATHWAY: Aromatic compound metabolism. {ECO:0000305}.
CC -!- INDUCTION: Induced in the presence of gamma-resorcylate.
CC {ECO:0000269|PubMed:26319878}.
CC -!- DISRUPTION PHENOTYPE: The mutant is unable to grow on gamma-resorcylate
CC as a sole energy and carbon source. {ECO:0000269|PubMed:26319878}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ACMSD family. {ECO:0000305}.
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DR EMBL; CP000431; ABG93670.1; -; Genomic_DNA.
DR RefSeq; WP_011594776.1; NC_008268.1.
DR STRING; 101510.RHA1_ro01859; -.
DR EnsemblBacteria; ABG93670; ABG93670; RHA1_ro01859.
DR KEGG; rha:RHA1_ro01859; -.
DR PATRIC; fig|101510.16.peg.1880; -.
DR eggNOG; COG2159; Bacteria.
DR HOGENOM; CLU_039329_5_0_11; -.
DR OMA; FAQNIWI; -.
DR BioCyc; MetaCyc:MON-19795; -.
DR Proteomes; UP000008710; Chromosome.
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; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..329
FT /note="Gamma-resorcylate decarboxylase"
FT /id="PRO_0000454505"
FT ACT_SITE 290
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 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q60GU1"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q60GU1"
SQ SEQUENCE 329 AA; 37348 MW; F81D2A25EC3A72BE CRC64;
MQGKIALEEH FAIPETLNDS AGFVPGTYWD ELQARLLDIQ DVRLKLMDEH NIETMILSLN
APAVQAIPER ERAIDIARRA NDVLAEECAK RPDRFRGFAA LPLQDPDAAA EELRRCVTEL
GFVGALVNGF SQSATVDGGS TPLYYDLPRY RPFWAEVERL DVPFYLHPRN PLNQDARIYE
GHPWLLGPTW AFAQETAVHA LRLMASGLFD EHPGLRIVLG HMGEGIPAML WRIDHRNAWV
DVPPAYPAKR RMVDYFTENF FVTTSGNFRT QTLIDLLLEL GSERVMFSTD WPFENINHAA
EWFDAASISE ADRLKIGRTN AATLFKLDR
