ID A0A2A4B5J6_9SPHN Unreviewed; 600 AA.
AC A0A2A4B5J6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PCD03225.1};
GN ORFNames=COC42_02060 {ECO:0000313|EMBL:PCD03225.1};
OS Sphingomonas spermidinifaciens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1141889 {ECO:0000313|EMBL:PCD03225.1, ECO:0000313|Proteomes:UP000218366};
RN [1] {ECO:0000313|EMBL:PCD03225.1, ECO:0000313|Proteomes:UP000218366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9NM-10 {ECO:0000313|EMBL:PCD03225.1,
RC ECO:0000313|Proteomes:UP000218366};
RA Feng G., Zhu H.;
RT "Sphingomonas spermidinifaciens 9NM-10, whole genome shotgun sequence.";
RL Submitted (SEP-2017) 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:PCD03225.1}.
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DR EMBL; NWMW01000001; PCD03225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4B5J6; -.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000218366; 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; IPR020953; Acyl-CoA_DH_N_bac.
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 Pfam; PF12418; AcylCoA_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:UP000218366}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 80..158
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 163..271
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..451
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 474..592
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 600 AA; 64675 MW; 09D40C9815CAAAEF CRC64;
MPQYTPPVRD TRFVLDHVVG LDRHANLPGF ANATPDMVDA VLEEGGRFVA EVLFPLNHSG
DQEGCTRHPD GSVTTPKGFK EAYDQLREAG WMTLGAPEEF GGQGMPHTVS TAFEEYMISA
NMAFAMYPGL THGAIAALLA KGSDEQKALY VPRMVSGEWG GTMNLTEPHC GTDLGLIKTK
AEPQADGSYA ITGTKIFISS GEHDLTSNII HLVLAKTPGA PDSVKGISLF VVPKFMVNED
GSLGERNTLS CGSIEHKMGI HGNSTCVMNY DGAKGWMVGE ENKGLAAMFI MMNAARLGVG
LQGLGVAEVA YQNAVQYAHD RRQGRALTGP KEPDEKADTL FVHPDVRRML MEAKALTEGL
RALCLWGALQ VDLSHKAPDD AERQLADDLI GLLTPVIKGY GTDKGYEIAT SAQQVYGGHG
YIAEWGMEQY VRDARIAQIY EGTNGVQAMD LVGRKLAQNG GRAVQAFFKL VGDEITAAKQ
DEGSADFAAR LERALNELQA ATMWFLQNGM KNPEHVGAGA HSYMHLMGIV ATGLMWLRMA
RAAAKLIAAG EGDAKFLNAK LVTARFYAER ILPDAGALRR KIEGGAESIM ALEPELFMAA
//
