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Database: UniProt
Entry: A0A240U7R9_9BURK
LinkDB: A0A240U7R9_9BURK
Original site: A0A240U7R9_9BURK 
ID   A0A240U7R9_9BURK        Unreviewed;       512 AA.
AC   A0A240U7R9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Cytochrome C oxidase Cbb3 {ECO:0000313|EMBL:ART53441.1};
GN   ORFNames=CBP34_02295 {ECO:0000313|EMBL:ART53441.1};
OS   Acidovorax carolinensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=553814 {ECO:0000313|EMBL:ART53441.1, ECO:0000313|Proteomes:UP000194432};
RN   [1] {ECO:0000313|EMBL:ART53441.1, ECO:0000313|Proteomes:UP000194432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA3 {ECO:0000313|EMBL:ART53441.1};
RA   Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H., Wright F.A.,
RA   Aitken M.D.;
RT   "Polyphasic characterization of four soil-derived phenanthrene-degrading
RT   Acidovorax strains and proposal of Acidovorax phenanthrenivorans sp. nov.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP021361; ART53441.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A240U7R9; -.
DR   KEGG; acin:CBP34_02295; -.
DR   Proteomes; UP000194432; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.140.10.20; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR003143; Cyt_cd1_C_sf.
DR   InterPro; IPR011048; Haem_d1_sf.
DR   PANTHER; PTHR47197:SF3; PE-PGRS FAMILY PROTEIN PE_PGRS17; 1.
DR   PANTHER; PTHR47197; PROTEIN NIRF; 1.
DR   Pfam; PF02239; Cytochrom_D1; 2.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Reference proteome {ECO:0000313|Proteomes:UP000194432}.
FT   DOMAIN          9..87
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   512 AA;  56029 MW;  11A2FFC55C5016E6 CRC64;
     MIAAPAAAKS TSDAAGLYRE HCASCHGAQR TGGMGPALLP ESLERLRRPE ALRVIQQGRT
     ATQMAGFAGT LPPADIAALA EWIYQPVSPA PAWSDADVRA SRVETAGAKD LPARPAWQAD
     PMNLFVVVEG GDHHVSLVDG DRFEVIHRFA SRYALHGGPK FTPDGRYVFF GSRDGWITKY
     DLWNLTVVAE VRAGLNMRNV AVSGDGRWVM AANYLPRTVV LFDADLQLVK RYDATTLDGK
     EASRVSAVYD AAPRKSFVVA LKDIPEVWEI SYDPKAAPIY DGLVHDYKMG EAIAKPGYQG
     VRRTPLDEPL DDFFFDQSYR HVLGSTRPKT GAADGAPTAQ VVNLDVRRKI AELPIAGMPH
     LGSGITFAWN GTTVLASPNL KGGAIDVIDM RTWRTVKTIP TPGPGFFLRS HEATRYAWAD
     SMMSPTAKDT LTLIDKATLE PVATLREPGR TLAHTEFTKD GRYALVSLWE MDGAIIVFDA
     QTLKEVKRLP MSKPVGKYNV WNKITRSEGT SH
//
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