ID   GRAA_RHIS5              Reviewed;         409 AA.
AC   A1IIX2;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=FADH(2)-dependent resorcinol hydroxylase, oxygenase component {ECO:0000305};
DE            EC=1.14.14.27 {ECO:0000269|PubMed:17158677};
GN   Name=graA {ECO:0000303|PubMed:17158677};
OS   Rhizobium sp. (strain MTP-10005).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=267998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP   AND INDUCTION.
RC   STRAIN=MTP-10005;
RX   PubMed=17158677; DOI=10.1128/jb.01675-06;
RA   Yoshida M., Oikawa T., Obata H., Abe K., Mihara H., Esaki N.;
RT   "Biochemical and genetic analysis of the gamma-resorcylate (2,6-
RT   dihydroxybenzoate) catabolic pathway in Rhizobium sp. strain MTP-10005:
RT   identification and functional analysis of its gene cluster.";
RL   J. Bacteriol. 189:1573-1581(2007).
CC   -!- FUNCTION: Involved in the gamma-resorcylate (2,6-dihydroxybenzoate)
CC       catabolism (PubMed:17158677). Oxygenase component of the resorcinol
CC       hydroxylase, which catalyzes the FADH(2)-dependent conversion of
CC       resorcinol to hydroxyquinol (PubMed:17158677).
CC       {ECO:0000269|PubMed:17158677}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FADH2 + O2 + resorcinol = benzene-1,2,4-triol + FAD + H(+) +
CC         H2O; Xref=Rhea:RHEA:50228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16971, ChEBI:CHEBI:27810,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.14.14.27;
CC         Evidence={ECO:0000269|PubMed:17158677};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50229;
CC         Evidence={ECO:0000269|PubMed:17158677};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000305}.
CC   -!- SUBUNIT: The FADH(2)-dependent resorcinol hydroxylase is composed of
CC       two subunits, GraA (the oxygenase component) and GraD (the reductase
CC       component). Both subunits are required for activity.
CC       {ECO:0000269|PubMed:17158677}.
CC   -!- INDUCTION: Induced in the presence of gamma-resorcylate.
CC       {ECO:0000269|PubMed:17158677}.
CC   -!- SIMILARITY: Belongs to the HpaH/HsaA monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB266210; BAF44522.1; -; Genomic_DNA.
DR   KEGG; ag:BAF44522; -.
DR   BioCyc; MetaCyc:MON-19792; -.
DR   BRENDA; 1.14.14.27; 14628.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR013107; Acyl-CoA_DH_C.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..409
FT                   /note="FADH(2)-dependent resorcinol hydroxylase, oxygenase
FT                   component"
FT                   /id="PRO_0000454489"
SQ   SEQUENCE   409 AA;  43305 MW;  0623437C78497431 CRC64;
     MNDMSHAPQP AQTKPHVRLV GRVAGVADLF RSSARQTEEA RRVPASHIAA LRGIGYFDIV
     KPRAFGGQGG EFAELVEANI ELSAACASTG WVAGLLSAHQ WLLAMFPEEA QADVWDENPD
     ALLCGSYAPV KMAEAADGGY RLSGKWAFAS GCENAQWSLC AAILPPQAKG RPVPAFLLVP
     ASQYAIEDTW HVVGLAGTVS KTLVLDDVFV PKHRVLTFPD ATSGHTPGGR FYAQEGLFNM
     PLLTGIPSCL ASTGVGAAKG ALAAYVDHVG GRVTRGAVAG GNNRMAEFPT IQLRVAEAAA
     SVDAACEILL RDVARAQALS QARLEGRAEF SVDDRLLSRR GQSFSVSFSL RAVQALNDST
     GGVGLDLSNP VQRAWRDANA VGRHISMNWD AVGTMIGQSM LGLEPKGQY