ID   CDHC_PSEU3              Reviewed;         167 AA.
AC   D7REY5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Caffeine dehydrogenase subunit gamma;
DE            EC=1.17.5.2;
DE   AltName: Full=Caffeine dehydrogenase small subunit;
GN   Name=cdhC;
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; ADH15881.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7REY5; -.
DR   SMR; D7REY5; -.
DR   KEGG; ag:ADH15881; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0034875; F:caffeine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   SUPFAM; SSF47741; SSF47741; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.
FT   CHAIN           1..167
FT                   /note="Caffeine dehydrogenase subunit gamma"
FT                   /id="PRO_0000418589"
FT   DOMAIN          4..80
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         42
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         47
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         50
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         62
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   167 AA;  18034 MW;  090A17DBCA952B1A CRC64;
     MSSHVISLTV NGQAIERKVD SRTLLADFLR DELRLTGTHV GCEHGVCGAC TIQFDGEPAR
     SCLMLAVQAE GHSIRTVEAL AVDGCLGALQ QAFHEKHGLQ CGFCTPGLLM TLDYALTADL
     HIDFSSDKEI RELISGNLCR CTGYQNIINA IKSVSPTTEI AKSEELV