ID A0A120GCA4_9SPHN Unreviewed; 579 AA.
AC A0A120GCA4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KWV94826.1};
GN ORFNames=ASS64_06365 {ECO:0000313|EMBL:KWV94826.1};
OS Erythrobacter sp. AP23.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=499656 {ECO:0000313|EMBL:KWV94826.1, ECO:0000313|Proteomes:UP000058666};
RN [1] {ECO:0000313|EMBL:KWV94826.1, ECO:0000313|Proteomes:UP000058666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP23 {ECO:0000313|EMBL:KWV94826.1,
RC ECO:0000313|Proteomes:UP000058666};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. AP23.";
RL Submitted (NOV-2015) 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:KWV94826.1}.
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DR EMBL; LNBY01000015; KWV94826.1; -; Genomic_DNA.
DR RefSeq; WP_067692068.1; NZ_LNBY01000015.1.
DR AlphaFoldDB; A0A120GCA4; -.
DR STRING; 499656.ASS64_06365; -.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000058666; 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}.
FT DOMAIN 79..156
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 161..271
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 287..449
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 476..572
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 579 AA; 61616 MW; 219D901553B152C5 CRC64;
MTYTPATQDQ LLAIRVNAGI EELARSEKFA AAEPDMVEAI VGGIGEFAAG EWAPLNRVGD
LEGAKLKNGL VRLPDGFAEA YAHYVEQGWN AISGPVEFGG QGLPFTLSCN VLENLGTANM
AFNLLPMLSV GAIESLEHHG SRELQEKYLP KLVSGEWSGT MNLTEPQAGS DVGALRTTAE
PIAEGEHAGK YRIKGQKIYI TWGEHELSKN IIHLVLARLP DAPEGSRGIS LFIVPKYHVK
EDGSPGPRND LRCVSIEHKL GINASPTCVM SYGDNDDCIG ELVGAENRGL MAMFTMMNNA
RINVGNQGVQ IGERATQQAQ LYARDRIQSA RAGSPDKAPV AILEHPDVRR MLLRMRALTE
GARALLYYTA GQVDRGTLGD AAARARGEVL TPLIKAWGTD IGIEVASLGV QVHGGMGFVE
ETGAAQHWRD SRIAPIYEGT NGIQAADLVT RKLGLDGGEA LSALIADIAR DAGEHPTLAA
LVADCQAVAN WMREEASLDD RLAGSVPFCT MLAVSVAGWQ LLRQLRAIEA GDAPGLAASK
SASARFFLDR IVPEASGLKA AATAGAEPLY ALSADQLVG
//
