(data stored in ACNUC7421 zone)

SWISSPROT: Q13R28_PARXL

ID   Q13R28_PARXL            Unreviewed;       272 AA.
AC   Q13R28;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 67.
DE   SubName: Full=Putative carbon monoxide dehydrogenase, middle subunit {ECO:0000313|EMBL:ABE33461.1};
DE            EC=1.2.99.2 {ECO:0000313|EMBL:ABE33461.1};
GN   ORFNames=Bxe_B2530 {ECO:0000313|EMBL:ABE33461.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33461.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33461.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33461.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., 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).
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DR   EMBL; CP000271; ABE33461.1; -; Genomic_DNA.
DR   RefSeq; WP_011490829.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13R28; -.
DR   STRING; 266265.Bxe_B2530; -.
DR   EnsemblBacteria; ABE33461; ABE33461; Bxe_B2530.
DR   GeneID; 4006974; -.
DR   KEGG; bxb:DR64_4857; -.
DR   KEGG; bxe:Bxe_B2530; -.
DR   PATRIC; fig|266265.5.peg.5175; -.
DR   eggNOG; ENOG4105FG6; Bacteria.
DR   eggNOG; COG1319; LUCA.
DR   HOGENOM; HOG000244728; -.
DR   KO; K03519; -.
DR   OMA; AGYAKMR; -.
DR   OrthoDB; POG091H0F7Y; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; SSF55447; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
DR   PRODOM; Q13R28.
DR   SWISS-2DPAGE; Q13R28.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Oxidoreductase {ECO:0000313|EMBL:ABE33461.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        1    170       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   272 AA;  28740 MW;  5C03E9CB1D2BB8FA CRC64;
     MYETTYLRAA SLDEAVAWLR EHEEARPLSG GMTLIPTLKQ RLAAPSHLVD LTRIDALRGV
     SVEGNVLRVG ALTRHAEVAA SPVVASAIPA LAQLAGVIAD PQVRNRGTMG GSVANNDPAA
     DYPCAVLALG AQVITSQRRL AADDFFVDTF ETALDAGELV VGFEYPIPLR GAYAKFRQPA
     SGYAVVGVFI AQFADAVRVA VTGAGASVFR WSEAEAALGA DLSDAALANL KMDDLALPDD
     DNGSAAYRAH LIETYTRRAL QSLLAQPLRQ PA
//

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