ID A9I434_BORPD Unreviewed; 776 AA.
AC A9I434;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Probable acyl-CoA dehydrogenase {ECO:0000313|EMBL:CAP44244.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:CAP44244.1};
GN OrderedLocusNames=Bpet3898 {ECO:0000313|EMBL:CAP44244.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP44244.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP44244.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; AM902716; CAP44244.1; -; Genomic_DNA.
DR AlphaFoldDB; A9I434; -.
DR STRING; 94624.Bpet3898; -.
DR KEGG; bpt:Bpet3898; -.
DR eggNOG; COG1960; Bacteria.
DR Proteomes; UP000001225; Chromosome.
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 CDD; cd00567; ACAD; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 2.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 2.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
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_sf.
DR PANTHER; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAP44244.1}.
FT DOMAIN 10..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 228..366
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 405..513
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 518..611
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 623..771
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 374..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 84352 MW; 93A4B4EAEC7A051A CRC64;
MSQPDTAMID AIRDSARDFL QRRDQKQRKR QDAPPDRDYW REIAEVGWLG MAVPESLGGL
DLGWHAMAAV MEEAGRAQLP EPLVACAVLP SAVLARLDDD AGAQARRQLL QDICAGQRIV
GLAWQETDGQ LEAGEATGAF GASVTLREGA YVLNGEKRHV IPGDGVDGWL VSADGEQGPA
LFYVAAGTPG VTAAVYRRAD GARACHLSLE SATLPPQALL ARQGVLDAID AALDLGRLMQ
AAELTGAARQ VLADSVAYLN TRQQFGKPLA SFQALQHRLV DAVMQVELAA NSLLNALNGL
AHADNVATRA AASRVKARAA RAGLEAARLA VQLHGAIGYT DECDVSLYFR SALHLAAWLG
NATAHRQRFG ALAPAPAAPD EDAAQDSTAA EDFPRQADWN AMPEAEFRAM LRRFFRAHYP
AHLRHVPWRL HWDEIKDWYY TLSRQGWIAP SWPREHGGMA LSPARLIAYI EEAERYGVAR
APDQGLVMLG PILLRYGTQA QRDRFLPGIL SGQDVWAQGY SEPNAGSDLA ALRCEAVVDG
DDLIVTGQKT WSTLAQDATH MFMLVRTDKT VKKQAGISFL LVDLRSPGVS RRPIRTLSGH
EEFCEVFFDQ VRVPRDNLVG ELNAGWGIAK ALLGFERLFS GSPKHANHAL QQIFGVARQR
GLLADAAFAD RLAELRLDAA DLTAMYEVFA DMARAGRPLP PELSLLKIWA TETHERLGAL
LIQATDEYGG AAMEESHGRV HALAPYINAL AATIFSGTNE IQRNIYAKQV LGLQGA
//
