ID J3CSS7_9BURK Unreviewed; 607 AA.
AC J3CSS7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EJL77774.1};
GN ORFNames=PMI15_04580 {ECO:0000313|EMBL:EJL77774.1};
OS Polaromonas sp. CF318.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1144318 {ECO:0000313|EMBL:EJL77774.1, ECO:0000313|Proteomes:UP000007275};
RN [1] {ECO:0000313|EMBL:EJL77774.1, ECO:0000313|Proteomes:UP000007275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF318 {ECO:0000313|EMBL:EJL77774.1,
RC ECO:0000313|Proteomes:UP000007275};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJL77774.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKIV01000144; EJL77774.1; -; Genomic_DNA.
DR RefSeq; WP_007874489.1; NZ_AKIV01000144.1.
DR AlphaFoldDB; J3CSS7; -.
DR PATRIC; fig|1144318.3.peg.4418; -.
DR OrthoDB; 9764895at2; -.
DR Proteomes; UP000007275; Unassembled WGS sequence.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF3; ACYL-COA DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_DH_N; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 7..30
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 35..144
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 157..244
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 300..468
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 485..603
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 607 AA; 66207 MW; D7DB0FA2B28E424B CRC64;
MSLRPTLDFL LYHWLDAESL NRRARFADHS RETFDAVFDT CERIAREKYA PFNRTVDTQE
PHFDGEKVIL PQATHDAQKA YAASGMLSAA QDYEVGGMQL PYTVEAAANA FFAMASVSIG
SGLLTTGNAN LLMVHGTELQ KEVFAKNEFS GRFSGTMCLS EPQAGSSLSD VTTRAVPDGE
GFEADPLGAR YRLKGNKMWI SAGEHELTDN IIHLVLAKIP GPDGKLIAGT RGISLFIVPK
KMVNAKGELT GVRNDVALAG LNHKLGWRGT TNTLLNFGEG KYPVDGQAGA VGYLVGKPHE
GLRCMFHMMN EARIGVGTAA TMLGMAGYYA SLDYAKNRPQ GRPVGVGGKD ASQPQIRIIE
HADVKRMLLA QKAYCEGALA LELYCARLVD ENHTAEAQAA DDARLLLEVL TPIAKSWPSE
WCLEANSLAI QVHGGYGYTR DFPVEQYWRD NRLNMIHEGT HGIQAMDLLG RKVLMEGGRG
LQLLAARINA TIEKAIQRPE LAVHANALGK ALQHVGSATK AAWATGEPGE ALANAVPYMQ
AFGHTVLAWL WLDVALASLS LPQDAPHAGR MGAMRYFYHY ELPKIDAWLK VVESRDLTCA
DLPEEAF
//
