ID B1Z5J8_BURA4 Unreviewed; 426 AA.
AC B1Z5J8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Gluconate 2-dehydrogenase (Acceptor) {ECO:0000313|EMBL:ACB68044.1};
DE EC=1.1.99.3 {ECO:0000313|EMBL:ACB68044.1};
GN OrderedLocusNames=BamMC406_5601 {ECO:0000313|EMBL:ACB68044.1};
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB68044.1, ECO:0000313|Proteomes:UP000001680};
RN [1] {ECO:0000313|Proteomes:UP000001680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680};
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 3 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) 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};
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; CP001027; ACB68044.1; -; Genomic_DNA.
DR RefSeq; WP_012371988.1; NC_010557.1.
DR AlphaFoldDB; B1Z5J8; -.
DR KEGG; bac:BamMC406_5601; -.
DR HOGENOM; CLU_028594_0_1_4; -.
DR OrthoDB; 9809720at2; -.
DR Proteomes; UP000001680; Chromosome 3.
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; 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; 2.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
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};
KW Oxidoreductase {ECO:0000313|EMBL:ACB68044.1}.
FT DOMAIN 44..147
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 189..296
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 315..403
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 58
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 61
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 62
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 204
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 207
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 208
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 328
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 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 332
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 426 AA; 45521 MW; 6FF643D5FFDADBE9 CRC64;
MKHKRLWFGA TGVAIAGLAI AVGIMVRPSI APIEPPARAS FDPQLVRAGA RVVALGDCVV
CHTAKDGKPF AGGLPLATPF GTIYATNITP DADTGIGRWS RDAFSRALRT GIARDGHPLY
PAFPYIHFTR MSDDEITAAY AYLMTREPVQ ASTPKNDLIF PLNFRPLVAF WNVLFLHEGA
STPDPAQSAQ WNRGKALVDG LGHCASCHSP LNAIGGEKAG KAFDGGIVDG WEAPPLNTLG
HAARPWTQAQ LVAYLRTGRA SEHGAAAGPM LPVTRDLATV PAEDVEAIAA YILSIQKPAG
ARPETAGAGR NPTTPAGQRG AALFQASCAQ CHGPAAPMQS IGERPTLAFS TAVAADTPRN
AIQMMFNGIG WHGEDTLNYM PSYLDQYDDR QIADLAAYIR ETYSDRPAWS DVESLAAKLR
KEDRTR
//