ID A0A2A7UT24_COMTR Unreviewed; 393 AA.
AC A0A2A7UT24;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Pimeloyl-CoA dehydrogenase large subunit {ECO:0000313|EMBL:PEH88428.1};
GN ORFNames=CRM82_07265 {ECO:0000313|EMBL:PEH88428.1};
OS Comamonas terrigena.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=32013 {ECO:0000313|EMBL:PEH88428.1, ECO:0000313|Proteomes:UP000220246};
RN [1] {ECO:0000313|Proteomes:UP000220246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_394 {ECO:0000313|Proteomes:UP000220246};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:PEH88428.1}.
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DR EMBL; PDEA01000001; PEH88428.1; -; Genomic_DNA.
DR RefSeq; WP_066539800.1; NZ_UIGV01000002.1.
DR AlphaFoldDB; A0A2A7UT24; -.
DR STRING; 1219032.GCA_001515545_03150; -.
DR GeneID; 80800391; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000220246; 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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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 Coiled coil {ECO:0000256|SAM:Coils}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000220246}.
FT DOMAIN 6..121
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 127..219
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 231..391
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT COILED 241..268
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 393 AA; 43559 MW; 22E2F51AA860A2E3 CRC64;
MDLAFTPEEQ AFREEVRAWI HEHLDPAAAR KVREGLRLTR DDIQGWAKTL GKKGWLAYGW
PKEFGGPGWT AVQKHLFAEE LAKAGAPSIV PFGPVMVAPV IQAFGTPAQQ QRFLPGIASG
EVWWSQGYSE PGSGSDLASV KTRAERQGDF YIVNGQKTWT TLGQHGDWMF NLVRTSNEGK
PQTGISFLLI DMKSPGVTVR PIKLLDGECE VNEVFFDNVK VPADQLIGEE NKGWTYAKHL
LAHERTNIAD VNRAKRELER LKRVARAEGV WEDPRFRDQI ALLEVDVVAL EMLVLRVLSA
EKSGKNPLDI AGLLKIKGSE IQQRYTELLM LAGGPYSLPL VYEAMEAGWQ GDFPGGTVGL
APLASSYFNM RKTTIYGGSN EVQRNIVAQT VLG
//
