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Database: UniProt
Entry: A0A1S8FF32_9BURK
LinkDB: A0A1S8FF32_9BURK
Original site: A0A1S8FF32_9BURK 
ID   A0A1S8FF32_9BURK        Unreviewed;       610 AA.
AC   A0A1S8FF32;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OOG39702.1};
GN   ORFNames=B0B52_13755 {ECO:0000313|EMBL:OOG39702.1};
OS   Polaromonas sp. A23.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG39702.1, ECO:0000313|Proteomes:UP000218978};
RN   [1] {ECO:0000313|EMBL:OOG39702.1, ECO:0000313|Proteomes:UP000218978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A23 {ECO:0000313|EMBL:OOG39702.1,
RC   ECO:0000313|Proteomes:UP000218978};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:OOG39702.1}.
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DR   EMBL; MUNO01000026; OOG39702.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8FF32; -.
DR   STRING; 1944133.B0B52_13755; -.
DR   OrthoDB; 9764895at2; -.
DR   Proteomes; UP000218978; 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; 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; 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   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218978}.
FT   DOMAIN          7..30
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          157..244
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          300..467
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          485..606
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   610 AA;  66278 MW;  10340F149A9CC0A5 CRC64;
     MSLRPTLDFL LYQWLNAESL NQRERFADHS RETFDAVFDT CERIAREKYA PFNRLVDTQE
     PQFDGEKVIL PQATHDANKA YAGSGMLSAA QDYEEGGMQL PYTIEAAANC FFAMASVSMG
     SSLLTKGNAN LLLVHGTEAQ KAVFARNEFA GRFSGTMCLS EPQAGSSLSD ITTRAVPDGA
     DFEAEPLGPR YRLKGNKMWI SAGEHELTEN IIHLVLAKIP GPDGKLIAGT RGISLFIVPK
     KMVGADGQLT GERNDVALAG LNHKLGWRGT TNTLLNFGEG KYPVGGEAGA VGYLVGKPHE
     GLRCMFHMMN EARIGVGTAA VMLGMAGYYA SLDYAKNRPQ GRPVGPAGKD SAQPQVRIVE
     HADVKRMLLA QKSYCEGALA LELYCARLVD EQHTAEPQAA DEARLLLEVL TPIAKSWPSE
     WCLEANSLAI QIHGGYGYTR DFPVEQYWRD NRLNMIHEGT HGIQATDLLG RKVLMEGGKG
     LQLLAARINS TIERAIQVPE LAAHASALGQ ALLQVGATTK AAWATGNPTD ALANAVPYMQ
     GFGHTVLAWI WLDVALAALK ADATKSIAVT AGKLGALRYF YHYELPKIDA WLKVVATRDL
     TCAELPEEAF
//
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