(data stored in SCRATCH zone)
SWISSPROT: B1K8V1_BURCC
ID B1K8V1_BURCC Unreviewed; 475 AA.
AC B1K8V1;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 08-MAY-2019, entry version 64.
DE SubName: Full=Gluconate 2-dehydrogenase (Acceptor) {ECO:0000313|EMBL:ACA92448.1};
DE EC=1.1.99.3 {ECO:0000313|EMBL:ACA92448.1};
GN OrderedLocusNames=Bcenmc03_3292 {ECO:0000313|EMBL:ACA92448.1};
OS Burkholderia cenocepacia (strain MC0-3).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92448.1, ECO:0000313|Proteomes:UP000002169};
RN [1] {ECO:0000313|Proteomes:UP000002169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT 3.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- PTM: Binds 3 heme groups per subunit.
CC {ECO:0000256|PIRSR:PIRSR000018-50}.
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DR EMBL; CP000959; ACA92448.1; -; Genomic_DNA.
DR RefSeq; WP_011547847.1; NC_010515.1.
DR EnsemblBacteria; ACA92448; ACA92448; Bcenmc03_3292.
DR KEGG; bcm:Bcenmc03_3292; -.
DR HOGENOM; HOG000178965; -.
DR OMA; GDYSFED; -.
DR BioCyc; BCEN406425:G1GBC-3496-MONOMER; -.
DR Proteomes; UP000002169; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0033717; F:gluconate 2-dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 3.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR008168; Cyt_C_IC.
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 PRINTS; PR00605; CYTCHROMECIC.
DR SUPFAM; SSF46626; SSF46626; 3.
DR PROSITE; PS51007; CYTC; 3.
PE 4: Predicted;
DR PRODOM; B1K8V1.
DR SWISS-2DPAGE; B1K8V1.
KW Complete proteome {ECO:0000313|Proteomes:UP000002169};
KW Heme {ECO:0000256|PIRSR:PIRSR000018-50, ECO:0000256|PROSITE-
KW ProRule:PRU00433};
KW Iron {ECO:0000256|PIRSR:PIRSR000018-51, ECO:0000256|PROSITE-
KW ProRule:PRU00433};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000018-51, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Oxidoreductase {ECO:0000313|EMBL:ACA92448.1}.
FT DOMAIN 63 166 Cytochrome c. {ECO:0000259|PROSITE:
FT PS51007}.
FT DOMAIN 210 325 Cytochrome c. {ECO:0000259|PROSITE:
FT PS51007}.
FT DOMAIN 348 438 Cytochrome c. {ECO:0000259|PROSITE:
FT PS51007}.
FT METAL 81 81 Iron (heme 1 axial ligand).
FT {ECO:0000256|PIRSR:PIRSR000018-51}.
FT METAL 229 229 Iron (heme 2 axial ligand).
FT {ECO:0000256|PIRSR:PIRSR000018-51}.
FT METAL 365 365 Iron (heme 3 axial ligand).
FT {ECO:0000256|PIRSR:PIRSR000018-51}.
FT BINDING 77 77 Heme 1 (covalent). {ECO:0000256|PIRSR:
FT PIRSR000018-50}.
FT BINDING 80 80 Heme 1 (covalent). {ECO:0000256|PIRSR:
FT PIRSR000018-50}.
FT BINDING 225 225 Heme 2 (covalent). {ECO:0000256|PIRSR:
FT PIRSR000018-50}.
FT BINDING 228 228 Heme 2 (covalent). {ECO:0000256|PIRSR:
FT PIRSR000018-50}.
FT BINDING 361 361 Heme 3 (covalent). {ECO:0000256|PIRSR:
FT PIRSR000018-50}.
FT BINDING 364 364 Heme 3 (covalent). {ECO:0000256|PIRSR:
FT PIRSR000018-50}.
SQ SEQUENCE 475 AA; 50504 MW; 7A6B6C49EF07099A CRC64;
MKRTMNHHNA ARPVSPLRRA LAIGTAWAAF GLAGGGAFAQ PASTPSAASG AVAAPAAQSA
DANLIKRGEY LARAGDCIAC HTASGGKPFA GGLKFDTPIG GIYSTNITPD PKTGLGGWTY
EDFTRAVREG VRKNGDTMYP AMPFPSYARL TDDDMKALYA YFMHGVAPVE HENRKVDIVW
PLSMRWPLGI WRKMFAPSPK PFDAASYTDP VVARGAYLVQ GLGHCGACHT PRAPTMQERG
LTDADGLDFL AGGAAIDGWV PTSLRGEPRT GLGTWSETEI VQFLKTGRTL RTAAFGGMTD
VVGHSMQHMT DDDLNAIARY LKTLPPRVQG EQPHVYDAAA AKALQTGDAS KPGAAVYRDN
CMACHRSDGH GYTRVFPALA GNPVVQGDDP TSLIHVVLEG SALQGTRTAP STFTMPPFGW
RLSDQEVADV SNFVRTSWGN TGASVTAAQV AKVRKSVPST RPEPPPGARF PQASR
//
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