GenomeNet

Database: UniProt
Entry: A0A2T4JKQ8_9RHOB
LinkDB: A0A2T4JKQ8_9RHOB
Original site: A0A2T4JKQ8_9RHOB 
ID   A0A2T4JKQ8_9RHOB        Unreviewed;       592 AA.
AC   A0A2T4JKQ8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PTE18453.1};
GN   ORFNames=C5F46_04680 {ECO:0000313|EMBL:PTE18453.1};
OS   Phaeovulum veldkampii DSM 11550.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Phaeovulum.
OX   NCBI_TaxID=1185920 {ECO:0000313|EMBL:PTE18453.1, ECO:0000313|Proteomes:UP000241899};
RN   [1] {ECO:0000313|EMBL:PTE18453.1, ECO:0000313|Proteomes:UP000241899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11550 {ECO:0000313|EMBL:PTE18453.1,
RC   ECO:0000313|Proteomes:UP000241899};
RA   Meyer T.E., Miller S., Lodha T., Gandham S., Chintalapati S.,
RA   Chintalapati V.R.;
RT   "Rhodobacter veldkampii.";
RL   Submitted (MAR-2018) 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:PTE18453.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PZKF01000007; PTE18453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4JKQ8; -.
DR   OrthoDB; 9807883at2; -.
DR   Proteomes; UP000241899; 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:UP000241899}.
FT   DOMAIN          4..31
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          43..154
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          161..269
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          281..445
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          461..587
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   592 AA;  62697 MW;  B2EEE872316CD307 CRC64;
     MPAYTAPIRD MQFLLHEVLN IATAGVPGYD ELEPDFTGAV LEAAGKVASE VLAPLNRSGD
     AEGCRLENGI VRTPKGFKAA FAAMKEGGWT ALDSDPEFGG QGMPYLMGTA VGEIFVSANM
     AFNMYQGLTH GAVSAIEAHG SPEQKATYLP PMIACDWTGT MNLTEPHCGT DLGLMRTRAE
     PQPDGSYRIT GEKIFISAGE HDLAENIIHL VLAKAPGGGE GTRGVSLFIV PKFLVNPDGS
     LGPRNAVSAG KIEHKMGIHG NATCVMNYDG ATGYLLGDLH KGMRAMFTMM NEARLGVGLQ
     GYAVAEAAYQ NAVIYAKDRL QGRAVTGAAN PTGPADPLIV HPDIRRTLMD QKSFVEGARA
     FTFWGASLID RSRRQGDAGA EALISLLTPV LKGFLTDKGF ETAVSAQQVW GGHGYIEDNG
     MAQFVRDARI AMIYEGANGV QALDLVGRKL AADGGKPVMA FFDLVKSFVK EHEADAGLKA
     EFLGPLKAAS KDLQAAAMIF LEKAATDPNG ALSGASDFLH MFGHTCLGLM WAQMAVAAQT
     ALTEGRGDPA FLNAKIVTGR HYMARHLPAT ALHLARIQAG GDTVMALAPE AF
//
DBGET integrated database retrieval system