(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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
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
//

If you have problems or comments...

PBIL Back to PBIL home page