ID E1GUW2_9BACT Unreviewed; 569 AA.
AC E1GUW2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Acyl-CoA dehydrogenase, C-terminal domain protein {ECO:0000313|EMBL:EFN91559.1};
GN ORFNames=HMPREF9018_0604 {ECO:0000313|EMBL:EFN91559.1};
OS Prevotella amnii CRIS 21A-A.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=679191 {ECO:0000313|EMBL:EFN91559.1, ECO:0000313|Proteomes:UP000016016};
RN [1] {ECO:0000313|EMBL:EFN91559.1, ECO:0000313|Proteomes:UP000016016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIS 21A-A {ECO:0000313|EMBL:EFN91559.1,
RC ECO:0000313|Proteomes:UP000016016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (SEP-2010) 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:EFN91559.1}.
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DR EMBL; ADFQ01000031; EFN91559.1; -; Genomic_DNA.
DR RefSeq; WP_008448151.1; NZ_ADFQ01000031.1.
DR AlphaFoldDB; E1GUW2; -.
DR eggNOG; COG1960; Bacteria.
DR Proteomes; UP000016016; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.20.120.470; Acyl-CoA dehydrogenase, C-terminal domain; 1.
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; IPR020964; Acyl-CoA_dehydrogenase_C.
DR InterPro; IPR036797; Acyl-CoA_dehydrogenase_C_sf.
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; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12186; AcylCoA_dehyd_C; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF158494; PG0775 C-terminal 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}.
FT DOMAIN 52..169
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 173..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 283..444
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 453..563
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12186"
SQ SEQUENCE 569 AA; 64674 MW; 91DEDFAA0E198E54 CRC64;
MANYYTEHPE IEFHLDHPLM KRIVELKERN YADKEKYEEA PVCYEDAIEN YKRILDVTGE
IAGETIAPNS EEVDLEGPHL IDNRMHYASK TLENLEATRK AGLWGVSMPR RYGGLNLPNV
VFSMMSEMIS AGDGGFQNIW SLQSCIDTLY EFGNEEQRQK YIPRICAGET MSMDLTEPDA
GSDLQRVMLK ASFDEKENCW RLNGVKRFIT NGDSDIHLVL ARSEEGTKDG RGLSMFIYDK
RNGGVDVRHI ENKLGIHGSP TCELVYKNAK AELCGNTRLG LIKYVMALMN GARLGIAAQS
VGVSQEAYNE ALAYAKERAQ FGKKIINMPP VYDMLSRMKA KLDAGRSLLY QTARYVDLYK
ALEDIARFEK LSPEERQEMK KYTRLADAFT PIAKGMNSEY VNQNTYDSIS VHGGSGFIME
YKCQRLYRDA RIFSIYEGTT QLQVVAANRY VMNGTYLGIM REMLAEPVSK DMQPLSKRIE
KMVEEYESSI NKVKEMESQD AQDLLARRLY DITAEIIMAL LIIADASKAP ELFAKSAHIF
VQMAEENITG KIAYINNFKV TDLVNFEQK
//
