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Database: UniProt
Entry: B9B3X9_9BURK
LinkDB: B9B3X9_9BURK
Original site: B9B3X9_9BURK 
ID   B9B3X9_9BURK            Unreviewed;       432 AA.
AC   B9B3X9;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Cytochrome c family protein {ECO:0000313|EMBL:EEE01144.1};
GN   ORFNames=BURMUCGD1_0540 {ECO:0000313|EMBL:EEE01144.1};
OS   Burkholderia multivorans CGD1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=513051 {ECO:0000313|EMBL:EEE01144.1, ECO:0000313|Proteomes:UP000005493};
RN   [1] {ECO:0000313|EMBL:EEE01144.1, ECO:0000313|Proteomes:UP000005493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGD1 {ECO:0000313|EMBL:EEE01144.1,
RC   ECO:0000313|Proteomes:UP000005493};
RX   PubMed=23105085; DOI=10.1128/JB.01306-12;
RA   Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA   Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA   Holland S.M., Goldberg J.B.;
RT   "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT   Granulomatous Disease Burkholderia multivorans Isolates.";
RL   J. Bacteriol. 194:6356-6357(2012).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEE01144.1}.
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DR   EMBL; ACFB01000003; EEE01144.1; -; Genomic_DNA.
DR   RefSeq; WP_006398367.1; NZ_ACFB01000003.1.
DR   AlphaFoldDB; B9B3X9; -.
DR   GeneID; 66527575; -.
DR   Proteomes; UP000005493; Unassembled WGS sequence.
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; 2.
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}.
FT   DOMAIN          46..149
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          191..301
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          321..411
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         60
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         63
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         64
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         206
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         209
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         210
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         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         337
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         338
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   432 AA;  46686 MW;  BEEEE549C621B7AB CRC64;
     MKRKSLFALS AVAIVAAAAL VPVLWSGNDT LHGASAVAAT PADQAALIKK GEYLARVGDC
     IACHTVRGGK PFAGGLPMAT PFGTMYTPNI TPDDQNGIGK WTSDDFYRAM HTGRSKDGSL
     LYPGFPFASY TKVTRADSDA IYAYLRSVAP VSVPSRPHEL KFPFNNRNLL IGWRTLFFKE
     GEYKPDPTKS VEWNRGAYLV EGLGHCSMCH TSINMMGGPV NSAAFAGGLI PLQNWYAPSL
     TNDKELGLGD WHVQELSDLL QAGVSNKGAV FGPMADVVHN SLQYMTDEDT RAMSTYLKSI
     PQKAEAPKNM QYEPSKQFGN ALFEQGKKIY ADNCATCHAE NGAGKPPAYP PLAGNHSIVM
     ESAVNPIRMV LNGGYPPSTF KNPRPYGMPP FAQSLSNQEV AAVVTYIRMS WGNNGTPISP
     QQVSDLRSAP LD
//
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