ID A0A011MGI3_9PROT Unreviewed; 597 AA.
AC A0A011MGI3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Acyl-CoA dehydrogenase, short-chain specific {ECO:0000313|EMBL:EXI68953.1};
DE EC=1.3.8.1 {ECO:0000313|EMBL:EXI68953.1};
GN ORFNames=AW08_00779 {ECO:0000313|EMBL:EXI68953.1};
OS Candidatus Accumulibacter adjunctus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI68953.1, ECO:0000313|Proteomes:UP000020218};
RN [1] {ECO:0000313|EMBL:EXI68953.1, ECO:0000313|Proteomes:UP000020218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
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:EXI68953.1}.
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DR EMBL; JFAX01000003; EXI68953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011MGI3; -.
DR STRING; 1454001.AW08_00779; -.
DR PATRIC; fig|1454001.3.peg.723; -.
DR Proteomes; UP000020218; 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:UP000020218}.
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..236
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 483..593
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 597 AA; 63529 MW; 36F0C54E6A7DE4A8 CRC64;
MSEYIAPVRD MQFVLKELAG LEQVAQLPGC EEATPDLVDA VLEEAARFAE EVLSPLNWPG
DQEGARWHDK TVTMPAGFKE AYRLFAESGW TALGSEPEWG GQGLPKVVAA AVGEMWKSAN
HSFSLCPLLT SGAIEALVLS GSEELKRTYV EKMVSGVWTG TMNLTEPNAG SDLAAVRTRA
EPQDDGSYRI CGQKIFITYG EHDLAENIVH LVLARTPTAP EGVKGISLFI VPKFMVNADG
SLGARNDAYC VSIEHKLGIH ASPTAIMAFG DHAGAVGHLV GEENRGLEYM FIMMNAARFG
VGLEGVAACE RAYQRARDYA RDRIQCTDIG VRGGPKVPII RHPDVRRMLM TMKSRAEATR
ALAYVVAAAH DAAVHHPDAG ERKRNQAFVD LMIPVVKGWS TESGVSMASI GVQVHGGMGY
VEETGAAQHL RDAQISTIYE GTTGIQANDL IGRKMAREGG ATLQAVIGLM RGVAGELGAR
SGDDFAALQR RFSAAIDALA AAGEWLVANY GKDVRAASAG AVPFLMLLGV VAGGWQMARA
ALVAQTKIDA GDADPFYPAK IGTARFYADH VLSQASGLAS SVTDGAAGVL ALPEDMF
//
