ID   RES4H_CORGL             Reviewed;         530 AA.
AC   Q8NR94; Q6M615;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=NADPH-dependent resorcinol 4-hydroxylase {ECO:0000305};
DE            EC=1.14.13.219 {ECO:0000269|PubMed:16963551};
DE   AltName: Full=Resorcinol hydroxylase {ECO:0000303|PubMed:16963551};
GN   OrderedLocusNames=Cgl1158 {ECO:0000312|EMBL:BAB98551.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=16963551; DOI=10.1128/aem.01494-06;
RA   Huang Y., Zhao K.X., Shen X.H., Chaudhry M.T., Jiang C.Y., Liu S.J.;
RT   "Genetic characterization of the resorcinol catabolic pathway in
RT   Corynebacterium glutamicum.";
RL   Appl. Environ. Microbiol. 72:7238-7245(2006).
CC   -!- FUNCTION: Involved in resorcinol degradation. Catalyzes the NADPH-
CC       dependent conversion of resorcinol into hydroxyquinol through
CC       hydroxylation. {ECO:0000269|PubMed:16963551}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 + resorcinol = benzene-1,2,4-triol + H2O +
CC         NADP(+); Xref=Rhea:RHEA:48828, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16971, ChEBI:CHEBI:27810,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.219;
CC         Evidence={ECO:0000269|PubMed:16963551};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48829;
CC         Evidence={ECO:0000269|PubMed:16963551};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Mutant loses the ability to grow on resorcinol,
CC       but its ability to grow on hydroxyquinol is the same as that of the
CC       wild-type strain. {ECO:0000269|PubMed:16963551}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000036; BAB98551.1; -; Genomic_DNA.
DR   RefSeq; NP_600384.1; NC_003450.3.
DR   RefSeq; WP_011014163.1; NC_006958.1.
DR   STRING; 196627.cg1309; -.
DR   DNASU; 1019141; -.
DR   KEGG; cgl:Cgl1158; -.
DR   PATRIC; fig|196627.13.peg.1135; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_009665_20_2_11; -.
DR   OMA; ASYRFHA; -.
DR   BioCyc; MetaCyc:G18NG-10730-MON; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0018677; F:pentachlorophenol monooxygenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..530
FT                   /note="NADPH-dependent resorcinol 4-hydroxylase"
FT                   /id="PRO_0000454473"
SQ   SEQUENCE   530 AA;  59195 MW;  D989081DCC50B1F6 CRC64;
     MSPNNFDTDV CIVGGGPTGT LLAVLLGQKG HRVTILEKWP TFYERPRAVT FDHEIARILG
     YIGIDSENDE AIDYHSDSYD WKNAAGETLL EVDWTSMTDS GWRTRYWFYQ PELEKRLRDL
     ALTMDFVDIR CGFTAVGLSQ DENSAIIHGI VTDTPENIPA DAQREDIRAK YVIGADGANS
     FVRNSLGLEM NDLGYFFDWL ILDLKPTQDI DYGTDHWQLC DPKRPTTIVP GGPGRRRWEF
     MALPGEDLKE LASEESAWNL LEPWDVTPGK AILERSAVYR FQARWAQEWR SGRALIAGDA
     AHLMPPFAGE GMCAGLRDSL ALAWRLDLVL SGKSDDALLD TYGEERREHV HYYIDFSMDL
     GNVICITDED EARLRDERMI KELEAQDGVP VNTDVAHLGP GIWDKDSSHG GELAKQGIVE
     YQGRKARFDD AVGRGWAVLG LNTDPREVLD EDSLVALDAI GAIVESVGDA TSAVLDVEGL
     YTRWLKEAGA TFIITRPDFY VYSTAVDAEQ LQTQIKQLSD LLHLNSVVGA