ID B0T2A0_CAUSK Unreviewed; 596 AA.
AC B0T2A0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ABZ69269.1};
GN OrderedLocusNames=Caul_0131 {ECO:0000313|EMBL:ABZ69269.1};
OS Caulobacter sp. (strain K31).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ69269.1};
RN [1] {ECO:0000313|EMBL:ABZ69269.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31 {ECO:0000313|EMBL:ABZ69269.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) 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; CP000927; ABZ69269.1; -; Genomic_DNA.
DR AlphaFoldDB; B0T2A0; -.
DR STRING; 366602.Caul_0131; -.
DR KEGG; cak:Caul_0131; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_5; -.
DR OrthoDB; 9807883at2; -.
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}.
FT DOMAIN 2..33
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 37..157
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 162..272
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 467..592
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 596 AA; 64145 MW; 52538DA24AF3AA86 CRC64;
MTYQPPVREH AFLLRDVLNI DQHGNLPSFA DASFETVEQI LEAAAQFTGE VLAPLNHVGD
QQGCVWNKDF TVKTPDGFAA AYKQLCEGGW TGLGSDPAYG GQGLPHVVNL AFSEMSSSAN
MAFSMYPGLA HGAYSAIHTG GSDQQKDLYL PKMVSGEWTG TMNLTEPHCG TDLGLLRTKA
VPEADGSYRI TGQKIWISAG EHDMADNIVH LVLARIEGAP AGVKGISLFI VPKFLPKEDG
SVGPRNEGVK CVGLEEKMGI HGNATCVMQY EDAKGWLIGE ENSGLKLMFV MMNEARLGVG
LQGIAQAEAA YQAAVAFAKD RLQGRSLTGP KNPEGPADPI IVHPDVRRML LESKALIEGG
RAFLFWTALH GDLAHQHPDE ATRAKAEDYM GLMTPVLKGY LTDKGFKICS DAMQVHGGSG
FTEHFPASQY LRDVRIALIY EGTNGIQALD LVGRKLASKG GRAVMTFFQE VDQFIGENDG
DAELKPFVEA LAGVKAQLQD GTMWLMQNGL QNPDNAGAAS TDYMHLFGLT GLAYMWCLMV
KAANAKIAAG SSDPFFTTKI VTAKYFIERI LPDAGAHLAK LKTGSATLMA LPAEAF
//
