(data stored in ACNUC7421 zone)

SWISSPROT: Q13I13_PARXL

ID   Q13I13_PARXL            Unreviewed;       204 AA.
AC   Q13I13;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=Cytochrome c-type protein {ECO:0000256|PIRNR:PIRNR000013};
GN   Name=napC {ECO:0000313|EMBL:ABE36276.1};
GN   ORFNames=Bxe_C0369 {ECO:0000313|EMBL:ABE36276.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36276.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36276.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36276.1,
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 4 heme groups per subunit.
CC       {ECO:0000256|PIRNR:PIRNR000013}.
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DR   EMBL; CP000272; ABE36276.1; -; Genomic_DNA.
DR   RefSeq; WP_011493536.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0369; -.
DR   EnsemblBacteria; ABE36276; ABE36276; Bxe_C0369.
DR   GeneID; 4009883; -.
DR   KEGG; bxb:DR64_8072; -.
DR   KEGG; bxe:Bxe_C0369; -.
DR   PATRIC; fig|266265.5.peg.8138; -.
DR   eggNOG; ENOG4105CUW; Bacteria.
DR   eggNOG; COG3005; LUCA.
DR   HOGENOM; HOG000275532; -.
DR   KO; K02569; -.
DR   OMA; CTGCHEM; -.
DR   OrthoDB; 1683334at2; -.
DR   BioCyc; BXEN266265:BXE_RS38430-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019333; P:denitrification pathway; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3820.10; -; 1.
DR   InterPro; IPR011031; Multihaem_cyt.
DR   InterPro; IPR036280; Multihaem_cyt_sf.
DR   InterPro; IPR024717; NapC/NirT/NrfH.
DR   InterPro; IPR005126; NapC/NirT_cyt_c_N.
DR   InterPro; IPR038266; NapC/NirT_cytc_sf.
DR   InterPro; IPR011885; NO3Rdtase_cyt_c_NapC/NirT.
DR   Pfam; PF03264; Cytochrom_NNT; 1.
DR   PIRSF; PIRSF000013; 4_hem_cytochrm_NapC; 1.
DR   SUPFAM; SSF48695; SSF48695; 1.
DR   TIGRFAMs; TIGR02161; napC_nirT; 1.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE   4: Predicted;
DR   PRODOM; Q13I13.
DR   SWISS-2DPAGE; Q13I13.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000013};
KW   Heme {ECO:0000256|PIRNR:PIRNR000013, ECO:0000256|PIRSR:PIRSR000013-1,
KW   ECO:0000256|SAAS:SAAS00881333};
KW   Iron {ECO:0000256|PIRNR:PIRNR000013, ECO:0000256|PIRSR:PIRSR000013-2,
KW   ECO:0000256|SAAS:SAAS00881267}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000013,
KW   ECO:0000256|PIRSR:PIRSR000013-2, ECO:0000256|SAAS:SAAS00881388};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|PIRNR:PIRNR000013}.
FT   TRANSMEM     21     39       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       47    184       MULTIHEME_CYTC. {ECO:0000259|PROSITE:
FT                                PS51008}.
FT   METAL        58     58       Iron (heme 1 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000013-2}.
FT   METAL        86     86       Iron (heme 2 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR000013-
FT                                2}.
FT   METAL       146    146       Iron (heme 3 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR000013-
FT                                2}.
FT   METAL       179    179       Iron (heme 4 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR000013-
FT                                2}.
FT   METAL       184    184       Iron (heme 2 axial ligand); via tele
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR000013-
FT                                2}.
FT   BINDING      52     52       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000013-1}.
FT   BINDING      55     55       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000013-1}.
FT   BINDING      82     82       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000013-1}.
FT   BINDING      85     85       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000013-1}.
FT   BINDING      98     98       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000013-1}.
FT   BINDING     142    142       Heme 3 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000013-1}.
FT   BINDING     145    145       Heme 3 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000013-1}.
FT   BINDING     175    175       Heme 4 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000013-1}.
FT   BINDING     178    178       Heme 4 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000013-1}.
SQ   SEQUENCE   204 AA;  23529 MW;  E305D1E8A0277E4A CRC64;
     MRDLIRRYWK TINRPTAYYS LGFLTLGGFI AGVVFWGAFN TAMELTNTEA FCTGCHEMRD
     NTYAELKTTI HYSNRSGFHA KCSDCHVPHE WTAKIARKMQ ASKEVWAKVF GVVNTREKFE
     DKRLELAEHE WARFKANDSL ECRNCHQFEY MDFTRQSPRA QEAHQRFLAT GERTCIDCHK
     GIAHQLPNMT QAQADADAKQ AAGH
//

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