FDHC_GLUJA
ID FDHC_GLUJA Reviewed; 486 AA.
AC M1V1V5;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Fructose dehydrogenase cytochrome subunit;
DE AltName: Full=Fructose dehydrogenase subunit II;
DE Flags: Precursor;
GN Name=fdhC;
OS Gluconobacter japonicus.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=376620;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOTECHNOLOGY, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 12302 / IAM 1816 / JCM 20278 / NBRC 3260;
RX PubMed=23275508; DOI=10.1128/aem.03152-12;
RA Kawai S., Goda-Tsutsumi M., Yakushi T., Kano K., Matsushita K.;
RT "Heterologous overexpression and characterization of a flavoprotein-
RT cytochrome c complex fructose dehydrogenase of Gluconobacter japonicus
RT NBRC3260.";
RL Appl. Environ. Microbiol. 79:1654-1660(2013).
RN [2]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 12302 / IAM 1816 / JCM 20278 / NBRC 3260;
RX PubMed=7462161; DOI=10.1128/jb.145.2.814-823.1981;
RA Ameyama M., Shinagawa E., Matsushita K., Adachi O.;
RT "D-fructose dehydrogenase of Gluconobacter industrius: purification,
RT characterization, and application to enzymatic microdetermination of D-
RT fructose.";
RL J. Bacteriol. 145:814-823(1981).
CC -!- FUNCTION: Cytochrome subunit of fructose dehydrogenase, an enzyme that
CC catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. In
CC the complex, mediates both the electron transfer to ubiquinone and the
CC anchoring of the complex to the membrane.
CC {ECO:0000269|PubMed:23275508}.
CC -!- SUBUNIT: Heterotrimer composed of FdhL, FdhS and FdhC.
CC {ECO:0000269|PubMed:23275508, ECO:0000269|PubMed:7462161}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Binds 3 heme c groups covalently per subunit. {ECO:0000305}.
CC -!- BIOTECHNOLOGY: This enzyme is commonly used in a number of research
CC projects to examine the electrochemical properties of enzyme-catalyzed
CC electrode reactions, named bioelectrocatalysis. Available as a
CC commercial product from Sigma Aldrich (catalog number F4892).
CC {ECO:0000269|PubMed:23275508}.
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DR EMBL; AB728565; BAM93251.1; -; Genomic_DNA.
DR AlphaFoldDB; M1V1V5; -.
DR KEGG; ag:BAM93251; -.
DR BioCyc; MetaCyc:MON-21744; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0006000; P:fructose metabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.760.10; -; 3.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR014353; Membr-bd_ADH_cyt_c.
DR Pfam; PF00034; Cytochrom_C; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR SUPFAM; SSF46626; SSF46626; 3.
DR PROSITE; PS51007; CYTC; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Heme; Iron; Membrane; Metal-binding; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..486
FT /note="Fructose dehydrogenase cytochrome subunit"
FT /id="PRO_0000425561"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 38..142
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 186..294
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 330..423
FT /note="Cytochrome c 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 52
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 55
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 56
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 201
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 204
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 205
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 343
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 346
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 347
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 486 AA; 52195 MW; 744F1264C82E3B3B CRC64;
MRYFRPLSAT AMTTVLLLAG TNVRAQPTEP TPASAHRPSI SRGHYLAIAA DCAACHTNGR
DGQFLAGGYA ISSPMGNIYS TNITPSKTHG IGNYTLEQFS KALRHGIRAD GAQLYPAMPY
DAYNRLTDED VKSLYAYIMT EVKPVDAPSP KTQLPFPFSI RASLGIWKIA ARIEGKPYVF
DHTHNDDWNR GRYLVDELAH CGECHTPRNF LLAPNQSAYL AGADIGSWRA PNITNAPQSG
IGSWSDQDLF QYLKTGKTAH ARAAGPMAEA IEHSLQYLPD ADISAIVTYL RSVPAKAESG
QTVANFEHAG RPSSYSVANA NSRRSNSTLT KTTDGAALYE AVCASCHQSD GKGSKDGYYP
SLVGNTTTGQ LNPNDLIASI LYGVDRTTDN HEILMPAFGP DSLVQPLTDE QIATIADYVL
SHFGNAQATV SADAVKQVRA GGKQVPLAKL ASPGVMLLLG TGGILGAILV VAGLWWLISR
RKKRSA
