ID A0A0U5KXG6_9GAMM Unreviewed; 421 AA.
AC A0A0U5KXG6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Gluconate 2-dehydrogenase cytochrome c subunit {ECO:0000313|EMBL:CUU22826.1};
DE EC=1.1.99.3 {ECO:0000313|EMBL:CUU22826.1};
GN ORFNames=EM595_0589 {ECO:0000313|EMBL:CUU22826.1};
OS Duffyella gerundensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Duffyella.
OX NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU22826.1, ECO:0000313|Proteomes:UP000059419};
RN [1] {ECO:0000313|Proteomes:UP000059419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Blom J.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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; LN907827; CUU22826.1; -; Genomic_DNA.
DR RefSeq; WP_067427724.1; NZ_LN907827.1.
DR AlphaFoldDB; A0A0U5KXG6; -.
DR STRING; 1619313.EM595_0589; -.
DR GeneID; 84614417; -.
DR KEGG; ege:EM595_0589; -.
DR PATRIC; fig|1619313.3.peg.612; -.
DR OrthoDB; 9811281at2; -.
DR Proteomes; UP000059419; Chromosome 1.
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; Cytochrome c-like domain; 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 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 PRINTS; PR00605; CYTCHROMECIC.
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};
KW Oxidoreductase {ECO:0000313|EMBL:CUU22826.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059419};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..421
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006860915"
FT DOMAIN 31..134
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 177..285
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 309..399
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 45
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 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 49
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 192
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 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 196
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 322
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 325
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 326
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 421 AA; 45171 MW; 915484D0B7B1A425 CRC64;
MKLLNLKTFF LANAMLLGAV SVQAQAEDEA QLIKQGEYLS RLGDCMACHS VAGKPAYSGG
LAIDSNLGRI YSTNITPDKE HGIGNYSEQQ FNDAVRKGVL PDGTGLYPAM PYPDYAKISD
ADMHALYTYF MKGVQPSAEQ PPETSLSFPF SQRWGMRFWN WAFTSDKAFK PIGGASAEIN
RGAYIVESLG HCGSCHTPRG LGMNEKALDS GDGDFLAGGN LNGWEVPSLR GLPRWNEKEI
VDYLQTGRND KAAVGGEMTS VVEHSSSHMT DADLQAIAAY LKFLGGNPPL QAGDANAAQA
TEAKLTAAKN LSEGERLYLD NCGACHFVTG KGAPGIFPEL DQATLVNAGD PTGLIHTILV
GAQQPSTEKA PSTLAMPGFG NRLNDDEVAK LATFVRQGWS NKAPAVTKEQ VAEVRKSLHH
E
//
