ID A0A076N4M3_AMYME Unreviewed; 380 AA.
AC A0A076N4M3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Pimeloyl-CoA dehydrogenase, large subunit {ECO:0000313|EMBL:AIJ24942.1};
GN ORFNames=AMETH_4850 {ECO:0000313|EMBL:AIJ24942.1};
OS Amycolatopsis methanolica 239.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ24942.1, ECO:0000313|Proteomes:UP000062973};
RN [1] {ECO:0000313|EMBL:AIJ24942.1, ECO:0000313|Proteomes:UP000062973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=239 {ECO:0000313|EMBL:AIJ24942.1,
RC ECO:0000313|Proteomes:UP000062973};
RA Tang B.;
RT "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL Submitted (JUL-2014) 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 ---------------------------------------------------------------------------
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; CP009110; AIJ24942.1; -; Genomic_DNA.
DR RefSeq; WP_017983778.1; NZ_CP009110.1.
DR AlphaFoldDB; A0A076N4M3; -.
DR STRING; 1068978.AMETH_4850; -.
DR KEGG; amq:AMETH_4850; -.
DR PATRIC; fig|1068978.7.peg.5215; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_9_0_11; -.
DR OrthoDB; 4759677at2; -.
DR Proteomes; UP000062973; Chromosome.
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; 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 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:UP000062973}.
FT DOMAIN 7..118
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..209
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 228..371
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 380 AA; 41784 MW; 75A9996FBD07EE20 CRC64;
MYIELTAPQR KLRDELREYF AGLITPEERQ ALLRERHGEV YRRIVRRMGS DGRLGAGWPE
EYGGGGFGDL EQHIFADEAA RADVQLPSVT LQTVGPTLQE YGTPEQKAFF LPKILAGEVH
FAIGYTEPGA GTDLASLRTT AVRDGDSYLV NGQKIFTTGG HDADYVWLAV RTDPDAPKHK
GISILIVDTS DPGYSWTPII TCDGAHHVNA TYYSDVRVPV SMRVGEENQG WKLITTQLNH
ERVMLGPAGR IGGLYDRVRA WAAERDLLGE PDVRRALGET LAVVRINELL NWQVAAAELD
VADASATKVF GSDRIQRVAR LVEENVARHG DLSDPGTAAL AEWLDVLARR NIVLTFGGGV
NEIQRELIAT AGLGLPRVPR
//
