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Database: UniProt
Entry: A0A2G8TG72_9BURK
LinkDB: A0A2G8TG72_9BURK
Original site: A0A2G8TG72_9BURK 
ID   A0A2G8TG72_9BURK        Unreviewed;       617 AA.
AC   A0A2G8TG72;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PIL45042.1};
GN   ORFNames=CR105_11290 {ECO:0000313|EMBL:PIL45042.1};
OS   Massilia eurypsychrophila.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1485217 {ECO:0000313|EMBL:PIL45042.1, ECO:0000313|Proteomes:UP000230390};
RN   [1] {ECO:0000313|EMBL:PIL45042.1, ECO:0000313|Proteomes:UP000230390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 30074 {ECO:0000313|EMBL:PIL45042.1,
RC   ECO:0000313|Proteomes:UP000230390};
RA   Wang H.;
RT   "Massilia psychrophilum sp. nov., a novel purple-pigmented bacterium
RT   isolated from Tianshan glacier, Xinjiang Municipality, China.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:PIL45042.1}.
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DR   EMBL; PDOC01000005; PIL45042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8TG72; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000230390; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; 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:SF3; ACYL-COA DEHYDROGENASE-RELATED; 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; 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   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230390}.
FT   DOMAIN          4..34
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          162..279
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          302..467
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          487..613
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   617 AA;  67516 MW;  0592CBD9A4FAD13E CRC64;
     MQSKILSRRD LDFLLFEWLD VESLTTRKRF EDHSRETFSA ALDTAEQVAT DLFAPHNKKS
     DNNEPHFDGT TVTIIPEVKT ALDAFAAAGL LAAGQDYEFD GMQLPSVMEK ATVAWFTAAN
     VATSAYIFLT VANANTLLKC ATPRQVEQYV RPMFAGQFFG TMCLSEPQAG SSLSDITTRA
     EPDPVDGADG ERQYRLTGNK MWISAGEHDL AGNIVHLVLA KIPGPDGRPI AGVKGISLFI
     VPKFVLDENG APGEHNDVVL AGLNHKMGNR GTTNCLLNFG EGKYKPHGKA GAIGYLVGNV
     HQGLANMFHM MNEARIGVGL GAAVLGVTGY LHALDYARNR PQGRHPAEKD PVKPQVAIIG
     HTDVRRMLLA QKAYAEGALA LVLYCARLVD EQRSAESDEA RRHAGQLLDF LTPIAKSWPS
     QWCVEANSLA IQVHGGYGYT REYNVEQFYR DNRLNAIHEG THGIHGLDLL GRKVSIQDGA
     LFRAVSAEIG KTISNAREHG ASAELQAYAD ELDAIWQRVA TVTAALYAAG DMNKTLANAS
     VYLEAVGHAV VAWIWLEQAM LAERQLTSAA DTDQDFYRGK LQACRYFFKW ELPKVGPQLA
     LLASIDTTTL DMQDAWF
//
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