ID A0A1M6B9B3_9BURK Unreviewed; 782 AA.
AC A0A1M6B9B3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Acyl-coenzyme A dehydrogenase {ECO:0000256|ARBA:ARBA00020144};
DE EC=1.3.8.7 {ECO:0000256|ARBA:ARBA00012033};
DE EC=1.3.8.8 {ECO:0000256|ARBA:ARBA00012040};
GN ORFNames=SAMN04488135_12430 {ECO:0000313|EMBL:SHI45247.1};
OS Pollutimonas bauzanensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pollutimonas.
OX NCBI_TaxID=658167 {ECO:0000313|EMBL:SHI45247.1, ECO:0000313|Proteomes:UP000184226};
RN [1] {ECO:0000313|EMBL:SHI45247.1, ECO:0000313|Proteomes:UP000184226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10190 {ECO:0000313|EMBL:SHI45247.1,
RC ECO:0000313|Proteomes:UP000184226};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC ChEBI:CHEBI:83727; EC=1.3.8.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC ChEBI:CHEBI:83726; EC=1.3.8.7;
CC Evidence={ECO:0000256|ARBA:ARBA00034035};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; FQXE01000024; SHI45247.1; -; Genomic_DNA.
DR RefSeq; WP_073110008.1; NZ_FQXE01000024.1.
DR AlphaFoldDB; A0A1M6B9B3; -.
DR STRING; 658167.SAMN04488135_12430; -.
DR OrthoDB; 9802447at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000184226; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; 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; 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 InterPro; IPR015396; FadE_C.
DR PANTHER; PTHR48083:SF18; ACYL-COENZYME A DEHYDROGENASE; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF09317; ACDH_C; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02771; Acyl-CoA_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:ARBA00022827};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000184226};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..194
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 321..468
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 475..763
FT /note="Acyl-CoA dehydrogenase C-terminal bacterial-type"
FT /evidence="ECO:0000259|Pfam:PF09317"
SQ SEQUENCE 782 AA; 85811 MW; 1FBB5FC23E6D57BF CRC64;
MSTFLIILAG IVIAAFIVLG LRPLRYAILS RRMFALYRSI LPQMSDTERD ALEAGTVWWE
SELFRGKPQW SRLHAIPKPA LTQEERDFLD NEVETACAMI DDWQVTQELR DMPQEVWQYI
KENRFLSLII PKEYGGRGFS ALAHSQVVTK LSTRNSALSV TVMVPNSLGP AELLLHYGTD
EQKNHYLPRL ATGEEIPAFA LTSPWAGSDA AAIPDSGIVC KGEWQGREVL GMRVTWDKRY
ITLAPVCTLL GLAFRLYDPD GLLGDKKDLG ITCALVPATH PGVETGRRHF PLDAMFMNGP
TRGADVFMPL EFIIGGAAMA GQGWRMLMEC LAAGRSISLP SSFTGMAKMT ARAVGAYCLV
RNQFRTPIGK FEGIEEALAR IGGNTYLIDA ARSMTAIAVD LGEKPSVVSA IVKYHLTERG
RSVVNDGMDI IGGKGICLGP QNFLGRAYQQ IPVGITVEGA NILTRSLIIF GQGAIRCHPF
VLAEMHAARH PDPEQGLRDF DQAFWGHVRY TLGNVWRSLG HGLTGARFVK IDTDVAPEMA
RYYRQLSRFS SAFAVFADTA MLVLGGSLKM RERLSARLGD ILSQMYLISA TLKRYEDDGR
QAADAPLAHW AIQDAMHRLQ AAFDGVLANF PNRAIARGLR VLVFPFGHPC AQPTDKLGQA
VARILIRPGA ARDRLTHDCY VPKDAMEPVG AIEAAFAASL GTEAIDAKIR QFEKSGRLAD
NPAANVRDIA QAVYAAGGIS EAEYEIVRQR NALRDRVIAV DDFPFDLRGA SGQAPAPERK
VA
//
