ID A0A074M492_ERYLO Unreviewed; 580 AA.
AC A0A074M492;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KEO89471.1};
GN ORFNames=EH31_12560 {ECO:0000313|EMBL:KEO89471.1};
OS Erythrobacter longus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO89471.1, ECO:0000313|Proteomes:UP000027647};
RN [1] {ECO:0000313|EMBL:KEO89471.1, ECO:0000313|Proteomes:UP000027647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO89471.1,
RC ECO:0000313|Proteomes:UP000027647};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL Submitted (APR-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:KEO89471.1}.
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DR EMBL; JMIW01000005; KEO89471.1; -; Genomic_DNA.
DR RefSeq; WP_034960609.1; NZ_JMIW01000005.1.
DR AlphaFoldDB; A0A074M492; -.
DR STRING; 1044.EH31_12560; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000027647; 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; 1.10.540.10; 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; 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 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:UP000027647}.
FT DOMAIN 39..157
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 162..272
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 288..450
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 479..572
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 580 AA; 61177 MW; D5E257469C12AE2C CRC64;
MTPFTPPTQD QLLAIRVNAG IEQLAASEKF AHAESDLVEA IVEGVGQFAA GEFAPLNRIG
DLEGAKLENG VVRLPDGFKE AYEGYVEQGW NSIGSSTDFG GQGLPFTLAC NVLENLGAAN
MAFSLLPMLS VGAVEALEHH GNEAQQSMYL PDLISGKWSG TMNLTEPAAG SDVGALRSTA
EPITDGEHAG KYKIKGQKIY ITWGDHTLAE NIIHLVLARL PGAPEGTRGI SLFVVPKYHV
NADGSLGPHN DLRPVSLEHK LGINASPTCV MSYGDNDNCI GELVGAENRG LMAMFTMMNN
ARINVGNQGV QIGERATQQA IAYAIDRVQS ARAGSPDKTP VAIIEHPDVR RMILRMKALT
EGARALLYYC AGQVDRGTLG DSEARTRAEI LVPLLKAWGT DVGVEVAGIG VQIHGGMGFV
EETGAAQHWR DSRIAPIYEG TNGIQAADLV TRKLGMEGGE AILALFADIA RDASGEPALA
VLAQDCAAIA QWMRDEASLD DRLAGSVPFC TMASVAVAGW QLMKQAEAVA AGAAPALLET
KPVTARFFLD RIVPEAAGLK ASATAGAEGL YTLSPEALAS
//
