(data stored in SCRATCH zone)

SWISSPROT: Q145R5_PARXL

ID   Q145R5_PARXL            Unreviewed;       468 AA.
AC   Q145R5;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   SubName: Full=Putative cytochrome c {ECO:0000313|EMBL:ABE28924.1};
GN   ORFNames=Bxe_A4075 {ECO:0000313|EMBL:ABE28924.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28924.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28924.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28924.1,
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; ABE28924.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_A4075; -.
DR   EnsemblBacteria; ABE28924; ABE28924; Bxe_A4075.
DR   KEGG; bxb:DR64_1751; -.
DR   KEGG; bxe:Bxe_A4075; -.
DR   eggNOG; ENOG4105CE2; Bacteria.
DR   eggNOG; COG1529; LUCA.
DR   HOGENOM; HOG000178965; -.
DR   OMA; DWSIKDI; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR014353; Membr-bd_ADH_cyt_c.
DR   Pfam; PF00034; Cytochrom_C; 2.
DR   PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR   SUPFAM; SSF46626; SSF46626; 3.
DR   PROSITE; PS51007; CYTC; 3.
PE   4: Predicted;
DR   PRODOM; Q145R5.
DR   SWISS-2DPAGE; Q145R5.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000018-51, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     36     56       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       86    189       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   DOMAIN      231    341       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   DOMAIN      357    447       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   METAL       104    104       Iron (heme 1 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000018-51}.
FT   METAL       250    250       Iron (heme 2 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000018-51}.
FT   METAL       374    374       Iron (heme 3 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000018-51}.
FT   BINDING     100    100       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     103    103       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     246    246       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     249    249       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     370    370       Heme 3 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
FT   BINDING     373    373       Heme 3 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000018-50}.
SQ   SEQUENCE   468 AA;  50977 MW;  A34F0E7CD0E39882 CRC64;
     MKPTLRTPGS LRALRTTLLD TWFTATKRRR SRRTRAPLVS GLLIAGLIVA GSAALLRASH
     TPLIAEARAA DTTASAPGAS ADTRPDLVKR GEYLARAGDC VACHTAPRGK LFAGGLAMET
     PFGTLYSPNI TPDAQYGIGT WSQDAFFKMM RTGRTPDGTL IYPAMPIAQY TKVTRQDSDA
     IFAYLQTVAP VREPNHKHTL RFPFNQRNLL YGWRTLYFRE GEFQPDPTKS VEWNRGAYLV
     EGLGHCTMCH TKINMLGGSS QSEQFAGGLI PVQNWYAPSL TSDKDGGLGD WSIKDIVDLL
     QAGISDRGAV YGPMAEVTYH SLQYMTEEDV KSMAVYLKTL PDKSGRKSGP SAPTNTSVFA
     LGEKIYADKC ALCHGAKGEG KLQHYPPLAG NQSIEMDSSV NPIRIVLNGG FPPGTMRNPE
     PYGMPPFGQE LNDADAAAVV TYIRTAWGNH GQPVTSREVN ELRNAPLH
//

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