(data stored in ACNUC7421 zone)

SWISSPROT: Q145T6_PARXL

ID   Q145T6_PARXL            Unreviewed;       447 AA.
AC   Q145T6;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   SubName: Full=Putative cytochrome c {ECO:0000313|EMBL:ABE28903.1};
GN   ORFNames=Bxe_A4096 {ECO:0000313|EMBL:ABE28903.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28903.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28903.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28903.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- PTM: Binds 3 heme groups per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000018-50}.
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DR   EMBL; CP000270; ABE28903.1; -; Genomic_DNA.
DR   RefSeq; WP_011486730.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4096; -.
DR   EnsemblBacteria; ABE28903; ABE28903; Bxe_A4096.
DR   GeneID; 4003369; -.
DR   KEGG; bxb:DR64_1772; -.
DR   KEGG; bxe:Bxe_A4096; -.
DR   PATRIC; fig|266265.5.peg.387; -.
DR   HOGENOM; HOG000178965; -.
DR   OMA; MACHRED; -.
DR   OrthoDB; 1297285at2; -.
DR   BioCyc; BXEN266265:BXE_RS01835-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
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; -; 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   Pfam; PF00034; Cytochrom_C; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   SUPFAM; SSF46626; SSF46626; 3.
DR   PROSITE; PS51007; CYTC; 3.
PE   4: Predicted;
DR   PRODOM; Q145T6.
DR   SWISS-2DPAGE; Q145T6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Heme {ECO:0000256|PIRSR:PIRSR000018-50, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Iron {ECO:0000256|PIRSR:PIRSR000018-51, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000018-51, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    447       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004182712.
FT   DOMAIN       43    146       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   DOMAIN      190    307       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   DOMAIN      334    424       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   METAL        61     61       Iron (heme 1 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000018-51}.
FT   METAL       209    209       Iron (heme 2 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000018-51}.
FT   METAL       351    351       Iron (heme 3 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000018-51}.
FT   BINDING      57     57       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING      60     60       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     205    205       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     208    208       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     347    347       Heme 3 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     350    350       Heme 3 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
SQ   SEQUENCE   447 AA;  47605 MW;  26954AE6F35F6C65 CRC64;
     MNMIPDRLKQ YLIPVFALIC SGTPGAANAQ APGTVPAPTT VDAQLAQGAY LAKAGDCAAC
     HTANKAQPFA GGLPLATPFG TLYSTNITPD ASTGIGSYSY DDFATALRQG IAKDGHRLYP
     AMPYPSYAKI DDADMHALYR YFTQGVKPVE QTNRASALRF PFNVRVLMSI WDRWYAHDHP
     AYRADPHQSV EWNRGAYLVQ GLAHCGACHT PHGMLGQETA LDDKDNTVFL SGNTLAGWYA
     PNLRGHPLQT SDSSKVSGKA DLVAYLRSGR LHDGAAFGPM TEVIDDSTQY LHDDDLNAIA
     TYLTSPALQA RATPTVAPQT TYTDRTASAL RAGHVDSAGA RLYLDNCAAC HRTDGTGAMP
     AFPSLNGNAA VLSDDPASLI HIVLSGSHMP STAAAPTPLA MPDFGWRLTD RQIADLLSFV
     RGSWGNRATD VSAAEVAKVR AVTVGAK
//

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