ID U4UYV8_9RHOB Unreviewed; 411 AA.
AC U4UYV8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ERL98944.1};
GN ORFNames=HIMB11_00753 {ECO:0000313|EMBL:ERL98944.1};
OS Rhodobacteraceae bacterium HIMB11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1366046 {ECO:0000313|EMBL:ERL98944.1, ECO:0000313|Proteomes:UP000016848};
RN [1] {ECO:0000313|EMBL:ERL98944.1, ECO:0000313|Proteomes:UP000016848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB11 {ECO:0000313|EMBL:ERL98944.1,
RC ECO:0000313|Proteomes:UP000016848};
RA Durham B.P., DeLong E.F., Rappe M.S.;
RT "Draft genome sequence of marine alphaproteobacterial strain HIMB11, the
RT first cultivated representative of a unique lineage within the Roseobacter
RT clade possessing a remarkably small genome.";
RL Submitted (AUG-2013) 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:ERL98944.1}.
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DR EMBL; AVDB01000002; ERL98944.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UYV8; -.
DR STRING; 1366046.HIMB11_00753; -.
DR PATRIC; fig|1366046.3.peg.758; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9775090at2; -.
DR Proteomes; UP000016848; 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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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 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|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000016848}.
FT DOMAIN 12..135
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 139..235
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 252..402
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 411 AA; 45776 MW; AEF62754A3EBD8CD CRC64;
MDLGISERVA PLIKAVRDMV ENEIAPLDAE YHALVGTHPT GDRFEHTDRQ LEILDGLKSL
ARERGLWNFW LTDSELGYGL STVEYAYLAE EMGKVGIAAE VFNCNAPDTG NMEVLERYGT
QEHKDRWLND LLDGKIRSAY VMTEPNTASS DAAQLSFEAK KDGDEWVLNG EKWWISGSGD
PRCALYIVMA CSDPDAPKHS RHTMFVMDAD TPGVEILRPM QVFGHDDAPH GHMHLRFTNV
RLPASAVVLG EGRGFEVAQG RLGPGRIHHC MRAIGQAEKA LEMMCKRGLA REAFGKKIIE
LGANYDIIAN ARMEIEMARL LCLKAAYMMD TAGVRAAQPW ISKIKVVAPL MAGKVIDEAM
QLHGAVGISQ DTDLAHMWTH VRTLRFADGP DAVHRRQVAR AELKKYSNEK R
//
