ID   GADH1_PANCY             Reviewed;         615 AA.
AC   O34214;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Gluconate 2-dehydrogenase flavoprotein;
DE            EC=1.1.99.3;
DE   AltName: Full=GA 2-DH dehydrogenase subunit;
DE            Short=GADH dehydrogenase subunit;
DE   Flags: Precursor;
OS   Pantoea cypripedii (Pectobacterium cypripedii) (Erwinia cypripedii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=55209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-37, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 29267 / DSM 3873 / CIP 105195 / LMG 2657 / NCPPB 3004;
RX   PubMed=9352901; DOI=10.1128/jb.179.21.6566-6572.1997;
RA   Yum D.-Y., Lee Y.-P., Pan J.-G.;
RT   "Cloning and expression of a gene cluster encoding three subunits of
RT   membrane-bound gluconate dehydrogenase from Erwinia cypripedii ATCC 29267
RT   in Escherichia coli.";
RL   J. Bacteriol. 179:6566-6572(1997).
CC   -!- FUNCTION: Part of the heterotrimer that catalyzes the conversion of D-
CC       gluconate to 2-dehydro-D-gluconate. This subunit functions as the
CC       dehydrogenase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + D-gluconate = 2-dehydro-D-gluconate + AH2;
CC         Xref=Rhea:RHEA:12769, ChEBI:CHEBI:13193, ChEBI:CHEBI:16808,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:18391; EC=1.1.99.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|PubMed:9352901};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:9352901};
CC   -!- SUBUNIT: Heterotrimer.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; U97665; AAC45885.1; -; Genomic_DNA.
DR   PIR; B38575; B38575.
DR   AlphaFoldDB; O34214; -.
DR   SMR; O34214; -.
DR   STRING; 55209.HA50_01500; -.
DR   BioCyc; MetaCyc:MON-18005; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0033717; F:gluconate 2-dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
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; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:9352901"
FT   CHAIN           23..615
FT                   /note="Gluconate 2-dehydrogenase flavoprotein"
FT                   /id="PRO_0000045854"
FT   ACT_SITE        542
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
SQ   SEQUENCE   615 AA;  67242 MW;  B9E1A84FD035609A CRC64;
     MERGERVSVP VSGYSRGEGV TVANELKKVD AVVVGFGWAG AIMAKELTEA GLNVVALERG
     PHRDTYPDGA YPQSIDELTY NIRKKLFQDL SKSTVTIRHD ASQTAVPYRQ LAAFLPGTGT
     GGAGLHWSGV HFRVDPVELN LRSHYEARYG KNFIPEGMTI QDFGVSYNEL EPFFDQAEKV
     FGTSGSAWTI KGKMIGKEKG GNFYAPDRSS DFPLPAQKRT YSAQLFAQAA ESVGYHPYDM
     PSANTSGPYT NTYGAQMGPC NFCGYCSGYA CYMYSKASPN VNILPALRQE PKFELRNNAY
     VLRVNLTGDK KRATGVTYLD GQGREVVQPA DLVILSAFQF HNVHLMLLSG IGQPYNPITN
     EGVVGRNFAY QNISTLKALF DKNTTTNPFI GAGGAGVAVD DFNADNFDHG PYGFVGGSPF
     WVNQAGTKPV SGLPTPKGTP NWGSQWKAAV ADTYNHHISM DAHGAHQSYR ANYLDLDPNY
     KNVYGQPLLR MTFDWQDNDI RMAQFMVGKM RKITEAMNPK MIIGGAKGPG THFDTTVYQT
     THMSGGAIMG EDPKTSAVNR YLQSWDVPNV FVPGASAFPQ GLGYNPTGMV AALTYWSAKA
     IREQYLKNPG PLVQA