FDHL_GLUJA
ID FDHL_GLUJA Reviewed; 544 AA.
AC M1VMF7;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Fructose dehydrogenase large subunit;
DE EC=1.1.5.14 {ECO:0000269|PubMed:23275508, ECO:0000269|PubMed:7462161};
DE AltName: Full=Fructose dehydrogenase subunit I;
GN Name=fdhL;
OS Gluconobacter japonicus.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=376620;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-24, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOTECHNOLOGY, SUBUNIT, AND SUBCELLULAR
RP 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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=24386392; DOI=10.1371/journal.pone.0084508;
RA Ramkissoon K.R., Miller J.K., Ojha S., Watson D.S., Bomar M.G.,
RA Galande A.K., Shearer A.G.;
RT "Rapid identification of sequences for orphan enzymes to power accurate
RT protein annotation.";
RL PLoS ONE 8:E84508-E84508(2013).
CC -!- FUNCTION: Catalytic subunit of fructose dehydrogenase, an enzyme that
CC catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose.
CC {ECO:0000269|PubMed:23275508, ECO:0000269|PubMed:24386392,
CC ECO:0000269|PubMed:7462161}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + keto-D-fructose = 5-dehydro-D-fructose + a
CC ubiquinol; Xref=Rhea:RHEA:22304, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:16389, ChEBI:CHEBI:17011, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:48095; EC=1.1.5.14;
CC Evidence={ECO:0000269|PubMed:23275508, ECO:0000269|PubMed:7462161};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:23275508, ECO:0000305|PubMed:7462161};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.02 M for D-fructose {ECO:0000269|PubMed:7462161};
CC Note=Measured for the whole complex.;
CC pH dependence:
CC Optimum pH is 4.0. {ECO:0000269|PubMed:7462161};
CC -!- SUBUNIT: Heterotrimer composed of FdhL, FdhS and FdhC.
CC {ECO:0000269|PubMed:23275508, ECO:0000269|PubMed:7462161}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23275508,
CC ECO:0000269|PubMed:7462161}.
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}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AB728565; BAM93252.1; -; Genomic_DNA.
DR AlphaFoldDB; M1VMF7; -.
DR SMR; M1VMF7; -.
DR PRIDE; M1VMF7; -.
DR KEGG; ag:BAM93252; -.
DR BioCyc; MetaCyc:MON-21743; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0047904; F:fructose 5-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0006000; P:fructose metabolic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; FAD; Flavoprotein; Membrane;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:23275508"
FT CHAIN 2..544
FT /note="Fructose dehydrogenase large subunit"
FT /id="PRO_0000425552"
FT ACT_SITE 478
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 14..30
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 544 AA; 59731 MW; 4CC6246C03ED4A4E CRC64;
MSNETLSADV VIIGAGICGS LLAHKLVRNG LSVLLLDAGP RRDRSQIVEN WRNMPPDNKS
QYDYATPYPS VPWAPHTNYF PDNNYLIVKG PDRTAYKQGI IKGVGGTTWH WAASSWRYLP
NDFKLHSTYG VGRDYAMSYD ELEPYYYEAE CEMGVMGPNG EEITPSAPRQ NPWPMTSMPY
GYGDRTFTEI VSKLGFSNTP VPQARNSRPY DGRPQCCGNN NCMPICPIGA MYNGVYAAIK
AEKLGAKIIP NAVVYAMETD AKNRITAISF YDPDKQSHRV VAKTFVIAAN GIETPKLLLL
AANDRNPHGI ANSSDLVGRN MMDHPGIGMS FQSAEPIWAG GGSVQMSSIT NFRDGDFRSE
YAATQIGYNN TAQNSRAGMK ALSMGLVGKK LDEEIRRRTA HGVDIYANHE VLPDPNNRLV
LSKDYKDALG IPHPEVTYDV GEYVRKSAAI SRQRLMDIAK AMGGTEIEMT PYFTPNNHIT
GGTIMGHDPR DSVVDKWLRT HDHSNLFLAT GATMAASGTV NSTLTMAALS LRAADAILND
LKQG
