ID R4X4H2_9BURK Unreviewed; 431 AA.
AC R4X4H2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Gluconate 2-dehydrogenase {ECO:0000313|EMBL:BAN27307.1};
GN ORFNames=BRPE64_DCDS03710 {ECO:0000313|EMBL:BAN27307.1};
OS Caballeronia insecticola.
OG Plasmid p1 {ECO:0000313|EMBL:BAN27307.1,
OG ECO:0000313|Proteomes:UP000013966}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=758793 {ECO:0000313|EMBL:BAN27307.1, ECO:0000313|Proteomes:UP000013966};
RN [1] {ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC PLASMID=p1 {ECO:0000313|Proteomes:UP000013966};
RX PubMed=23833137; DOI=10.1128/genomeA.00441-13;
RA Shibata T.F., Maeda T., Nikoh N., Yamaguchi K., Oshima K., Hattori M.,
RA Nishiyama T., Hasebe M., Fukatsu T., Kikuchi Y., Shigenobu S.;
RT "Complete Genome Sequence of Burkholderia sp. Strain RPE64, Bacterial
RT Symbiont of the Bean Bug Riptortus pedestris.";
RL Genome Announc. 1:340-344(2013).
RN [2] {ECO:0000313|EMBL:BAN27307.1, ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RPE64 {ECO:0000313|EMBL:BAN27307.1};
RC PLASMID=p1 {ECO:0000313|EMBL:BAN27307.1,
RC ECO:0000313|Proteomes:UP000013966};
RX PubMed=29863457; DOI=10.1099/ijsem.0.002848;
RA Takeshita K., Tamaki H., Ohbayashi T., Meng X.-Y., Sone T., Mitani Y.,
RA Peeters C., Kikuchi Y., Vandamme P.;
RT "Burkholderia insecticola sp. nov., a gut symbiotic bacterium of the bean
RT bug Riptortus pedestris.";
RL Int. J. Syst. Evol. Microbiol. 68:2370-2374(2018).
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR000018-50};
CC Note=Binds 3 heme c groups covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR000018-50};
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DR EMBL; AP013061; BAN27307.1; -; Genomic_DNA.
DR RefSeq; WP_016348016.1; NC_021289.1.
DR AlphaFoldDB; R4X4H2; -.
DR KEGG; buo:BRPE64_DCDS03710; -.
DR PATRIC; fig|758793.3.peg.5518; -.
DR HOGENOM; CLU_028594_0_0_4; -.
DR OrthoDB; 9809720at2; -.
DR Proteomes; UP000013966; Plasmid p1.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 3.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR014353; Membr-bd_ADH_cyt_c.
DR PANTHER; PTHR35008:SF8; BLL4482 PROTEIN; 1.
DR PANTHER; PTHR35008; BLL4482 PROTEIN-RELATED; 1.
DR Pfam; PF00034; Cytochrom_C; 3.
DR PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR SUPFAM; SSF46626; Cytochrome c; 3.
DR PROSITE; PS51007; CYTC; 3.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000018-50};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000018-51};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000018-51}; Plasmid {ECO:0000313|EMBL:BAN27307.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..431
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004381259"
FT DOMAIN 34..137
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 178..293
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 318..408
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 48
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 51
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 52
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-51"
FT BINDING 195
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 198
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 199
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-51"
FT BINDING 331
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 334
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 335
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-51"
SQ SEQUENCE 431 AA; 46138 MW; 5A2614A2A2954607 CRC64;
MKNAFKPLFA ALFAFGVGFG TVPSASAADA ANDALVARGA YLAKAGDCVA CHSAPRGKPL
AGGLPMTTPL GAIYTTNITP DPDTGIGRYT EEDFTRAVRE GVAKDGHNLY PAMPYPSYAK
INDEDMHALY MYFMHGVTPV KQANRESDIK WPLNMRWPLK LWNVVFLDKG VYQNKPAKDV
AWNRGAYLIQ GLGHCGSCHT PRGIAFQEKG LDESNNAYLT GGVLDNWFAS NLTGEHNTGL
GRWSEQDVAV FLKTGANPHA SAFGSMTSVI NNSTQNLSDA DIAAMALYLK SLPASGGNGG
PQYSYDPKAT KVSLTRPAAT DSGARVYTAF CMHCHGVDGR GFAPMLAPLA GNPNVLEKDA
SSLINVTLNG TEDLVIHGIP APYPMPRYAP VLNDQQIADV LTFVRGAWNN NTAAVQPEDV
AKIRKATQAA R
//
