ID   TSDB_RHOJR              Reviewed;         530 AA.
AC   Q0SFL5;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Probable NADH-specific resorcinol 4-hydroxylase;
DE            EC=1.14.13.220 {ECO:0000305|PubMed:26319878};
GN   Name=tsdB; OrderedLocusNames=RHA1_ro01860 {ECO:0000312|EMBL:ABG93671.1};
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, AND DISRUPTION PHENOTYPE.
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: Single-component hydroxylase that is part of the gamma-
CC       resorcylate (GRA) degradation pathway. GRA is initially converted by
CC       GRA decarboxylase to resorcinol, which is hydroxylated by resorcinol 4-
CC       hydroxylase. {ECO:0000305|PubMed:26319878}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 + resorcinol = benzene-1,2,4-triol + H2O +
CC         NAD(+); Xref=Rhea:RHEA:49684, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16971, ChEBI:CHEBI:27810,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.220;
CC         Evidence={ECO:0000305|PubMed:26319878};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49685;
CC         Evidence={ECO:0000269|PubMed:26319878};
CC   -!- DISRUPTION PHENOTYPE: The mutant bacteria is unable to grow on GRA
CC       (PubMed:26319878). Only 25% of the resorcinol is degraded compared to
CC       wild-type (PubMed:26319878). {ECO:0000269|PubMed:26319878}.
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; CP000431; ABG93671.1; -; Genomic_DNA.
DR   RefSeq; WP_011594777.1; NC_008268.1.
DR   AlphaFoldDB; Q0SFL5; -.
DR   SMR; Q0SFL5; -.
DR   STRING; 101510.RHA1_ro01860; -.
DR   EnsemblBacteria; ABG93671; ABG93671; RHA1_ro01860.
DR   KEGG; rha:RHA1_ro01860; -.
DR   PATRIC; fig|101510.16.peg.1881; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_009665_20_2_11; -.
DR   OMA; ASYRFHA; -.
DR   BioCyc; MetaCyc:MON-19788; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019505; P:resorcinol metabolic process; IDA:UniProtKB.
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   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..530
FT                   /note="Probable NADH-specific resorcinol 4-hydroxylase"
FT                   /id="PRO_0000446130"
SQ   SEQUENCE   530 AA;  57772 MW;  AF24D6D86EC005AE CRC64;
     MSAFAQPPGA GRKAVDVAIV GSGPTGMALA ALLGCQGRSV VVLERYTGLY NLPRAAAFDD
     ETMRTFQKLG VAEKMLPGTN VQRGYVWVNG DDEVLLDIEF DNPGRCGWPA QYMMYQPHLE
     SVLDELITSL PTVEIRRGMT VESVDQQDGD DVLVRATDVE GSAYLVRARY VVGCDGGNGV
     VRQFAGGELD DYGFFENWLV CDFQLNRDVP DLPTFRQVCD PAEPIAIVNI GPRFHRFSFR
     LESAANREEV VHPDKVWPRV ATYLTPEDAE LVRVANYTFR SCITTQWRHR RILLAGDAAH
     QMPPFLAQGM VSGIRDARNL AWKLDMVLAG HPDSLLDTYQ AEREPHVRYI TEKAIELGRV
     QTMRDTALAA QRDAQMIAAR KANQKPDKLR YPALSGGLIA NHGDMFPQGL VSTSSTTALF
     DEIAGTGWLV VADGPQVLSG IAEGDRTAFT EIGGKEVIFG LTSMFDGAPV SDTAGVYTRW
     FAAHECVAAI VRPDGYVFGL ARDAAELAGL AKELVAAVAP VPSRPPAPTA