ID W7YLD0_9BACT Unreviewed; 568 AA.
AC W7YLD0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:GAF03154.1};
GN ORFNames=JCM21142_41818 {ECO:0000313|EMBL:GAF03154.1};
OS Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Saccharicrinis.
OX NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF03154.1, ECO:0000313|Proteomes:UP000019402};
RN [1] {ECO:0000313|EMBL:GAF03154.1, ECO:0000313|Proteomes:UP000019402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF03154.1,
RC ECO:0000313|Proteomes:UP000019402};
RA Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., Kitamura K.,
RA Iida T., Darby A., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a Facultative
RT Anaerobe Isolated from Marine Mud.";
RL Genome Announc. 2:e00206-14(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:GAF03154.1}.
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DR EMBL; BAMD01000018; GAF03154.1; -; Genomic_DNA.
DR RefSeq; WP_027472103.1; NZ_KI912107.1.
DR AlphaFoldDB; W7YLD0; -.
DR STRING; 869213.GCA_000517085_02508; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9802867at2; -.
DR Proteomes; UP000019402; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
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; 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; PF08028; Acyl-CoA_dh_2; 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.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019402}.
FT DOMAIN 56..169
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 172..268
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 294..440
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT DOMAIN 452..562
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12186"
SQ SEQUENCE 568 AA; 64366 MW; B3C8B4A4FA6D2893 CRC64;
MANFFTDNPD LKFHLTHPMM EKIVALKERN FADKDKFDYA PMDFEDAMDS YEKVLEIVGE
ICGDIVAPNA ESVDQEGPKI VNNEVKYAKG TQENLDALVE AGLMGITLPR KYEGLNFPIV
PYIMAADIVS RADAGFVNIW GLQDCAETIN EFADEAQKQK YLPRISNGET AAMDLTEPDA
GSDLQAVQLK ATYNEEDGKW YLNGVKRFIT NGDGHVSLVL ARSEEGTHDG RGLSMFIYDR
NEKAVIVRRL ENKMGIKGSP TCELVFKNAP AELVGSRKMG LIKYVMALMN GARLGIGAQS
IGVSESAYRE GVAYAKERKQ FGKSIIEFPA VYEMLSTMKA KLDASRTLLY ETSRMVDIYK
TYMHISEERK LEPEERKEMK RYQKMADFFT PLLKGMSSEY SNQLAYDSLQ IHGGSGFMKD
YPIERIYRDA RITSIYEGTT QLQVVAAIRG VTTGGYLDRI REYEAMELRP ELHGLRRTLI
GMTEEYVHAV KTVVDVKDNE YIDFHARRLV EMAGHIIMGY LLLLDTQRDE KFKVSTEIYI
RMGKSENHAR AEFIHSFELD DLGAYKQA
//
