ID   GADH2_PECCY             Reviewed;         441 AA.
AC   O34215;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 47.
DE   RecName: Full=Gluconate 2-dehydrogenase cytochrome c subunit;
DE            Short=GADH cytochrome c subunit;
DE            Short=GA 2-DH cytochrome c subunit;
DE            EC=1.1.99.3;
DE   Flags: Precursor;
OS   Pectobacterium cypripedii (Erwinia cypripedii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=55209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-28, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 29267 / DSM 3873 / LMG 2657 / NCPPB 3004;
RX   MEDLINE=98012950; PubMed=9352901;
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
RT   29267 in Escherichia coli.";
RL   J. Bacteriol. 179:6566-6572(1997).
CC   -!- FUNCTION: Part of the heterotrimer that catalyzes the conversion
CC       of D-gluconate to 2-dehydro-D-gluconate.
CC   -!- CATALYTIC ACTIVITY: D-gluconate + acceptor = 2-dehydro-D-gluconate
CC       + reduced acceptor.
CC   -!- COFACTOR: FAD.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0;
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius;
CC   -!- SUBUNIT: Heterotrimer.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Periplasmic side (Potential).
CC   -!- PTM: Binds 3 heme groups per subunit (Potential).
CC   -!- SIMILARITY: Contains 3 cytochrome c domains.
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DR   EMBL; U97665; AAC45884.1; -; Genomic_DNA.
DR   PIR; C38575; C38575.
DR   HSSP; P56534; 1C6S.
DR   BRENDA; 1.1.99.3; 291533.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0033717; F:gluconate 2-dehydrogenase (acceptor) activity; IEA:EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR008168; Cyt_C_IC.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR014353; Membr-bd_AlcDH_cyt_c.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   ProDom; PD011584; CytC_adh; 2.
DR   PROSITE; PS51007; CYTC; 3.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Membrane; Metal-binding; Oxidoreductase; Repeat; Signal;
KW   Transport.
FT   SIGNAL        1     19
FT   CHAIN        20    441       Gluconate 2-dehydrogenase cytochrome c
FT                                subunit.
FT                                /FTId=PRO_0000045855.
FT   DOMAIN       26    129       Cytochrome c 1.
FT   DOMAIN      173    289       Cytochrome c 2.
FT   DOMAIN      312    403       Cytochrome c 3.
FT   METAL        44     44       Iron (heme 1 axial ligand) (By
FT                                similarity).
FT   METAL       192    192       Iron (heme 2 axial ligand) (By
FT                                similarity).
FT   METAL       329    329       Iron (heme 3 axial ligand) (By
FT                                similarity).
FT   BINDING      40     40       Heme 1 (covalent) (By similarity).
FT   BINDING      43     43       Heme 1 (covalent) (By similarity).
FT   BINDING     188    188       Heme 2 (covalent) (By similarity).
FT   BINDING     191    191       Heme 2 (covalent) (By similarity).
FT   BINDING     325    325       Heme 3 (covalent) (By similarity).
FT   BINDING     328    328       Heme 3 (covalent) (By similarity).
SQ   SEQUENCE   441 AA;  47097 MW;  0AF512CFA99DA123 CRC64;
     MMKSILALVL GTLSFAALAD DQANDALVKR GEYLARAGDC VACHSVKGGQ PFAGGLPMAT
     PIGTIYSTNI TPDKTTGIGD YSYDDFQKAV RHGVAKNGDT LYPAMPYPSY AVVSDEDMKA
     LYAYFMHGVA PVAQANKDSD IPWPLSMRWP LAIWRGVFAP DVKAFQPAAQ EDPVLARGRY
     LVEGLGHCGA CHTPRSITMQ EKALSNDGAH DYLSGSSAPI DGWTASNLRG DNRDGLGRWS
     EDDLRQFLRY GRNDHTAAFG GMTDVVEHSL QHLSDDDITA IARYLKSLGA KDASQTVFTQ
     DDQVAKALWK GDDSQTGASV YVDSCAACHK TDGSRLSALL PGAAWQPGGA GEPDPTSLIH
     IVLTGGTLPG VQGAPTAITM PAFGWRLNDQ QVADVVNFIR GSWGNGAKAT VTAKDVASLR
     KDETVQAHQG NADIKVLEQQ Q
//