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
//