ID Q13GD2_PARXL Unreviewed; 408 AA.
AC Q13GD2;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Bxe_C0984 {ECO:0000313|EMBL:ABE36857.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36857.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE36857.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE36857.1,
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., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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DR EMBL; CP000272; ABE36857.1; -; Genomic_DNA.
DR AlphaFoldDB; Q13GD2; -.
DR STRING; 266265.Bxe_C0984; -.
DR KEGG; bxe:Bxe_C0984; -.
DR PATRIC; fig|266265.5.peg.8746; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 6184213at2; -.
DR Proteomes; UP000001817; Chromosome 3.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
FT DOMAIN 25..96
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 253..382
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 408 AA; 44365 MW; 90FAFB3F49E66B73 CRC64;
MRHAMGITLV SPLSATLGFA ETIAHIALTA AERERNHRLP HEEIARLKEL GFGALRLPVD
AAGRGVSLSG LFVVARDVAA ADSNIAHAFR NHLWQVEAAL RRPDHPFHAH VLDLTRKKKT
VGLSFTDSDA VAAGARPSQV LSRLEWDEAR RVYIGSGEKV YATGNLYNDA FVGLAVESRE
GRTVQYVFDR GRGVSNDDDW QGFGQRLTGS GTAKFHAVTV PAAHVYPTDP PRTGDAAPWG
YTFHQVYLTS CIAGIVRRVA LDAVEVLRAR GRNFYHGDAA HPTDEPVLQT LLGRIRAYAA
SVEATADRAV AALQRAWDSY GTADEYDTTL AATLSAAEAK VVIDDLAPQI ASWLIDLGSG
SVVSRVGALD RHWRNIKVIA SHNPRLYKER LLGQNLLTGQ LPPTGAFF
//
