ID   CDHB_PSEU3              Reviewed;         295 AA.
AC   D7REY4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Caffeine dehydrogenase subunit beta;
DE            EC=1.17.5.2;
DE   AltName: Full=Caffeine dehydrogenase medium subunit;
GN   Name=cdhB;
OS   Pseudomonas sp. (strain CBB1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=765715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A CAFFEINE DEHYDROGENASE,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC   STRAIN=CBB1;
RX   PubMed=17981969; DOI=10.1128/jb.01390-07;
RA   Yu C.L., Kale Y., Gopishetty S., Louie T.M., Subramanian M.;
RT   "A novel caffeine dehydrogenase in Pseudomonas sp. strain CBB1 oxidizes
RT   caffeine to trimethyluric acid.";
RL   J. Bacteriol. 190:772-776(2008).
CC   -!- FUNCTION: Catalyzes the hydrolitical oxidation of 1,3,7-
CC       trimethylxanthine (caffeine) by incorporation of an oxygen atom
CC       originating from a water molecule into position C-8 to produce 1,3,7-
CC       trimethyluric acid (TMU). Coenzyme Q0 is the preferred electron
CC       acceptor and coenzyme Q2 can also be used, but oxygen and NADP cannot.
CC       {ECO:0000269|PubMed:17981969}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + caffeine + H2O = 1,3,7-trimethylurate + a
CC         ubiquinol; Xref=Rhea:RHEA:47148, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:27732, ChEBI:CHEBI:691622; EC=1.17.5.2;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.7 uM for caffeine (at 35 degrees Celsius and pH 7)
CC         {ECO:0000269|PubMed:17981969};
CC         Note=kcat is 10 min(-1) with caffeine as substrate.;
CC       pH dependence:
CC         Optimum pH is 70. {ECO:0000269|PubMed:17981969};
CC       Temperature dependence:
CC         30-min incubation at 70 degrees Celsius drastically reduces the
CC         enzyme activity to 11% of the initial value, and 77% of the activity
CC         remains after 30 min of incubation at 42 degrees Celsius.
CC         {ECO:0000269|PubMed:17981969};
CC   -!- SUBUNIT: Heterotrimer composed of an alpha (CdhA), a beta (CdhB) and a
CC       gamma (CdhC) subunit. {ECO:0000269|PubMed:17981969}.
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DR   EMBL; HM053473; ADH15880.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7REY4; -.
DR   SMR; D7REY4; -.
DR   KEGG; ag:ADH15880; -.
DR   GO; GO:0034875; F:caffeine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; SSF55447; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..295
FT                   /note="Caffeine dehydrogenase subunit beta"
FT                   /id="PRO_0000418588"
FT   DOMAIN          1..178
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   BINDING         32..36
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         111..115
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   295 AA;  32401 MW;  A7A5AA7A00C606D1 CRC64;
     MKPTAFDYIR PTSLPEALAI LAEHSDDVAI LAGGQSLMPL LNFRMSRPAL VLDINDISEL
     QQVRCENDTL YVGSMVRHCR VEQEEIFRST IPLMSEAMTS VAHIQIKTRG TLGGNLCNAH
     PASEMPAVIT ALGASMVCKS EKRGERVLTP EEFFEGALQN GLQSDELLCE IRIPVPSQYV
     GWAFEEVARR HGDFAQCGAA VLIGAEDRKI DYARIALCSI GETPIRFHAL EQWLIGRPVG
     NDLPADVKLH CREILDVAED STMTAENRAK LASAVTSRAI ARAADRIVHL DVKRG