(data stored in SCRATCH zone)

SWISSPROT: Q13HM5_PARXL

ID   Q13HM5_PARXL            Unreviewed;       387 AA.
AC   Q13HM5;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:ABE36414.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:ABE36414.1};
GN   ORFNames=Bxe_C0513 {ECO:0000313|EMBL:ABE36414.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36414.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE36414.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE36414.1,
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP000272; ABE36414.1; -; Genomic_DNA.
DR   RefSeq; WP_011493670.1; NZ_CP008761.1.
DR   STRING; 266265.Bxe_C0513; -.
DR   EnsemblBacteria; ABE36414; ABE36414; Bxe_C0513.
DR   GeneID; 4010027; -.
DR   KEGG; bxb:DR64_7933; -.
DR   KEGG; bxe:Bxe_C0513; -.
DR   PATRIC; fig|266265.5.peg.8272; -.
DR   eggNOG; ENOG4105C1G; Bacteria.
DR   eggNOG; COG1960; LUCA.
DR   HOGENOM; HOG000131659; -.
DR   OMA; MNTMDRN; -.
DR   OrthoDB; 760677at2; -.
DR   BioCyc; BXEN266265:BXE_RS39095-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13HM5.
DR   SWISS-2DPAGE; Q13HM5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125,
KW   ECO:0000313|EMBL:ABE36414.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       10    119       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      123    220       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      232    378       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   387 AA;  41531 MW;  0E35BC48BF90A803 CRC64;
     MNSNLIETSA EHQQIYDSVA KITRAYGHAA FAKAGRRGEE ARELWQNLAE AGYLGISVPE
     EYGGSGQGVE ELAIVLEATA AQGCPMTSFV VLPIIVFVLS KHATEAQKRE ILPAIATGEK
     RLAFAITEPD AGTNTHNLKT NAVRTANGGW RLSGSKYYIT EAEVADALLV VARTGVDEAT
     GRGKLSLFLV PKHLKGVTLQ NLPTELIVPE RQASVFFDDV ELPADALIGA EGEGLRNVFA
     GLNPERIAVA ALCNGLTTYA LTKACEYAKV RKVWKTPIGA HQAVAHPLAE AYARLQLSKM
     ATQRAAQLYD AGRDAGDASN IAKLTASDTA VFALDRAIQT HGGNGFSQEF GLGDLWFVAR
     VQQTAPVSRE MVLNHIAQHN LGLPRSY
//

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