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Database: UniProt
Entry: A0A0W1DXN1_9SPHN
LinkDB: A0A0W1DXN1_9SPHN
Original site: A0A0W1DXN1_9SPHN 
ID   A0A0W1DXN1_9SPHN        Unreviewed;       407 AA.
AC   A0A0W1DXN1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KTE22827.1};
GN   ORFNames=ATE67_02610 {ECO:0000313|EMBL:KTE22827.1};
OS   Sphingopyxis sp. H050.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759072 {ECO:0000313|EMBL:KTE22827.1, ECO:0000313|Proteomes:UP000053439};
RN   [1] {ECO:0000313|Proteomes:UP000053439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050 {ECO:0000313|Proteomes:UP000053439};
RA   Gomez-Alvarez V., Revetta R.P.;
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:KTE22827.1}.
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DR   EMBL; LNRZ01000001; KTE22827.1; -; Genomic_DNA.
DR   RefSeq; WP_058815102.1; NZ_LNRZ01000001.1.
DR   AlphaFoldDB; A0A0W1DXN1; -.
DR   STRING; 1759072.ATE67_02610; -.
DR   OrthoDB; 9780544at2; -.
DR   Proteomes; UP000053439; 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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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   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          7..122
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          126..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          232..386
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   407 AA;  45016 MW;  4208839F39B4A8B1 CRC64;
     MNLEYGPEYE RFRDEVRDFL AGNRHRAPHA SQRAARPDAA AVAWQKLLIE HGYTARTIPR
     EYGGYGAEPD ILKARIIAEE FARAGVPAGL SNQGISMLVP TLLELGTEEQ KRRWIEPTLR
     GEIVWCQGYS EPGAGSDLAS LRTSAREEDG HFVINGQKIW TSTARQADMI FCLVRTEAEA
     PKHAGISYLI FPMDLPGIEV RPLKTMTGHA EFNETFFTDV RVPVDQIVGQ RGQGWFVANA
     TLGHERGMLG DPDALENRLL ALIRLMRDER VGSARAIEDP VLRDRLVALQ AEVAAMKYNG
     MRVLSNQLKG DAGGMAKLIV KLQSCELAHQ ISALAIDAMG EMGILYSDSP RVREGGTWQW
     NYMFQLGLII GGGTAQIQKN IIAERGLDMP REPRLALASA EGRKDVA
//
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