ID   CDHA_PSEU3              Reviewed;         791 AA.
AC   D7REY3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Caffeine dehydrogenase subunit alpha;
DE            EC=1.17.5.2;
DE   AltName: Full=Caffeine dehydrogenase large subunit;
GN   Name=cdhA;
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   -!- COFACTOR:
CC       Name=Mo-molybdopterin cytosine dinucleotide; Xref=ChEBI:CHEBI:71308;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor
CC       per subunit. {ECO:0000250};
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}.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; HM053473; ADH15879.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7REY3; -.
DR   SMR; D7REY3; -.
DR   PRIDE; D7REY3; -.
DR   KEGG; ag:ADH15879; -.
DR   GO; GO:0034875; F:caffeine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR   InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   PANTHER; PTHR11908; PTHR11908; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SUPFAM; SSF54665; SSF54665; 1.
DR   SUPFAM; SSF56003; SSF56003; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Molybdenum; NAD; Oxidoreductase.
FT   CHAIN           1..791
FT                   /note="Caffeine dehydrogenase subunit alpha"
FT                   /id="PRO_0000418590"
FT   BINDING         257
FT                   /ligand="Mo-molybdopterin cytosine dinucleotide"
FT                   /ligand_id="ChEBI:CHEBI:71308"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   BINDING         371
FT                   /ligand="Mo-molybdopterin cytosine dinucleotide"
FT                   /ligand_id="ChEBI:CHEBI:71308"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   BINDING         548
FT                   /ligand="Mo-molybdopterin cytosine dinucleotide"
FT                   /ligand_id="ChEBI:CHEBI:71308"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   791 AA;  85820 MW;  17AB4E4939704E8E CRC64;
     MFADINKGDA FGTWVGKSVP RREDADILAG RAEYIADIKL PGMLEAAFLR SPFAHARIVS
     IDVSQALALP GVYDVMVGAD IPDYVKPLPL MITYQNHRET PTSPLARDIV RYAGEPVAVV
     AAINRYVAED ALELIVVKYE ELPVVASIDA SLAVDGPRLY EGWPDNVVAK VSSEIGDVDA
     AMASADLVFE ERFEIQRCHP APLETRGFIA QWDFKGENLN VWNGTQIINQ CRDFMSEVLD
     IPASKIRIRS PRLGGGFGAK FHFYVEEPAI VLLAKRVKAP VRWIEDRLEA FSATVHAREQ
     VIDVKLCAMN DGRITGIVAD IKGDLGASHH TMSMGPVWLT SVMMTGVYLI PNARSVAKAI
     VTNKPPSGSY RGWGQPQANF AVERMVDLLA HKLQLDPAAV RRINYVPEAR MPYTGLAHTF
     DSGRYEVLHD RALKTFGYEA WLERQAAAQA QGRRIGIGMS FYAEVSAHGP SRFLNYVGGR
     QGGYDIARIR MDTTGDVYVY TGLCDMGQGV TNSLAQIAAD ALGLNPDDVT VMTGDTALNP
     YTGWGTGASR SITIGGPAVM RAATRLREKI LSIARHWLQA DPDTLVLANR GVMVRDDPGR
     YVSFASIGRA AYCQIIELPE DVEPGLEAVG VFDTVQLAWP YGMNLVAVEV DEDTGAVSFL
     DCMLVHDMGT IVNPMIVDGQ LHGGIAQGIA QALYEELRYD ENGQLGTGSF ADFLMPTASE
     IPNMRFDHMV TESPLIPGGM KGVGEGGTIG TPAAVVNAIE NALRPITNSK LNRTPVTPDR
     ILTAISAGAC A