(data stored in ACNUC7421 zone)

SWISSPROT: Q13IY3_PARXL

ID   Q13IY3_PARXL            Unreviewed;       288 AA.
AC   Q13IY3;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   SubName: Full=Putative carbon monoxide dehydrogenase, medium chain (CoxM) {ECO:0000313|EMBL:ABE35956.1};
DE            EC=1.2.7.4 {ECO:0000313|EMBL:ABE35956.1};
GN   ORFNames=Bxe_C0029 {ECO:0000313|EMBL:ABE35956.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE35956.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE35956.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE35956.1,
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).
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DR   EMBL; CP000272; ABE35956.1; -; Genomic_DNA.
DR   RefSeq; WP_011493216.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0029; -.
DR   EnsemblBacteria; ABE35956; ABE35956; Bxe_C0029.
DR   GeneID; 4009817; -.
DR   KEGG; bxb:DR64_8396; -.
DR   KEGG; bxe:Bxe_C0029; -.
DR   PATRIC; fig|266265.5.peg.7808; -.
DR   eggNOG; ENOG4105FG6; Bacteria.
DR   eggNOG; COG1319; LUCA.
DR   HOGENOM; HOG000244728; -.
DR   KO; K03519; -.
DR   OMA; MMKLRMA; -.
DR   OrthoDB; 1017413at2; -.
DR   BioCyc; BXEN266265:BXE_RS36895-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0043885; F:carbon-monoxide dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; 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; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
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; Q13IY3.
DR   SWISS-2DPAGE; Q13IY3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00990854,
KW   ECO:0000313|EMBL:ABE35956.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN        1    177       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   288 AA;  30841 MW;  C761E5F4C5D81F35 CRC64;
     MIPRPFEYHV PRTLPEALAL LGEYGDEAKL LAGGHSLLPM MKLRFAEPGH LIDLGKLAEL
     KGIREADDEI RIGAMTTENE LIWSELLQTR CPLIVEGARQ ISDPQVRYRG TLGGDLSHGD
     PGNDHPALMM ALGASFVLAG EQGERVVSAA SFFVSTYTTL LEPGEIMTEI RIPTPPAGTG
     YCYAKLKRKT GDFATAAAAV TLRIGTAAVG EVRIALTNVA ETAIRATAAE QYLQGKPLDE
     PAIAEAARLA MAVCAPVADL RGDVEYKTAM AGEMTRRALI TAYARAAH
//

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