ID A0A011N7Z7_9PROT Unreviewed; 597 AA.
AC A0A011N7Z7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Acyl-CoA dehydrogenase, short-chain specific {ECO:0000313|EMBL:EXI71081.1};
DE EC=1.3.8.1 {ECO:0000313|EMBL:EXI71081.1};
GN ORFNames=AW07_03827 {ECO:0000313|EMBL:EXI71081.1};
OS Candidatus Accumulibacter sp. SK-11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454000 {ECO:0000313|EMBL:EXI71081.1, ECO:0000313|Proteomes:UP000020226};
RN [1] {ECO:0000313|EMBL:EXI71081.1, ECO:0000313|Proteomes:UP000020226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-11 {ECO:0000313|Proteomes:UP000020226};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:EXI71081.1}.
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DR EMBL; JFAW01000032; EXI71081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011N7Z7; -.
DR STRING; 1454000.AW07_03827; -.
DR PATRIC; fig|1454000.3.peg.3137; -.
DR Proteomes; UP000020226; Unassembled WGS sequence.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 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, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000020226}.
FT DOMAIN 4..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 40..156
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 162..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 284..450
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 481..593
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 597 AA; 63665 MW; C65E80CC83A00355 CRC64;
MSEYIAPVRD MQFVLRELAG LEQVAQLPGC EEATPDLVDA ILEEASRFAG EVLSPLNWPG
DQEGARWHDK TVTMPPGFKE AYKLFAESGW TALGSEPEWG GQGLPRLVAA AVGEMWKSAN
HSFSLCPLLT SGAIEALVLS GSDELKRTYV EKMVSGVWTG TMNLTEPNAG SDLAAVRTRA
EPQADGSYRI FGQKIFITYG EHDMAENIIH LVLARTPTAP EGVKGISLFV VPKFMVNEDG
SLGARNDAYC VSIEHKLGIH ASPTSIMAFG DHSGAVGHLV GEENRGLEYM FIMMNAARFG
VGLEGVAACE RAYQRARDYA RDRVQCTDIG VRGGPKVSII THPDVRRMLM TMKSRAEATR
ALAYVVAAAH DAAVRHPDAG ERKRNQAFVD LMIPVVKGWS TESGVSMASI GVQVHGGMGY
VEETGAAQHL RDAQISTIYE GTTGIQANDL IGRKMAREGG ATLKAVISLM RGAADELGDR
SGGDFAAIQR RFSAAVDALA EAGEWLVATY GSDVRAASAG AVPFLMLLGV VAGGWQMARA
ALVAQAKIDA GDADPFYPAK IVTTRFYADH VLSQAAGLAS SVTEGAAGVL ALPEDMF
//
