ID A0A1G8QMH4_9RHOB Unreviewed; 385 AA.
AC A0A1G8QMH4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SAMN05421850_1089 {ECO:0000313|EMBL:SDJ05801.1};
OS Lutimaribacter saemankumensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Lutimaribacter.
OX NCBI_TaxID=490829 {ECO:0000313|EMBL:SDJ05801.1, ECO:0000313|Proteomes:UP000199340};
RN [1] {ECO:0000313|EMBL:SDJ05801.1, ECO:0000313|Proteomes:UP000199340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28010 {ECO:0000313|EMBL:SDJ05801.1,
RC ECO:0000313|Proteomes:UP000199340};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNEB01000008; SDJ05801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8QMH4; -.
DR STRING; 490829.SAMN05421850_1089; -.
DR OrthoDB; 9775090at2; -.
DR Proteomes; UP000199340; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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 PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 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:UP000199340}.
FT DOMAIN 13..122
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 126..222
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 235..383
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 385 AA; 42337 MW; 8AECB5CFB5C4C552 CRC64;
MGLFTPTASW VMDEHRMFAD AVSRVFDDAL VPNIEKWVDQ GRVDREFWEL AGAQGIIGGS
VPEAYGGAGG GMGFDAIAVY EQGAVGDCGW GYSIQSIVLH YLLTYGSEEQ KQRWVPDLVA
GKRVAAIAMT EPGCGSDLQA VKTTAEKDGN QYRINGSKTF ITNGQTADLI VVVAKTDKAA
GAKGVSLIVV EADQVEGFRR GRNLKKLGMK ANDTSELFFE DVKVPQTNLL GAEEGQGFYQ
LMRQLPWERL VIAITALGSI DFALSETIKY VQERKAFGQR LMDFQNTRFK LAEMKTKAEV
LRAFVNDCIG RAEAGTLDAA TASMAKYWGS ETQNEVMHEC LQLFGGYGFM MEYPIARLYA
DARVQMIYGG TNEIMKELIA RSIDV
//
