ID C0ZN58_RHOE4 Unreviewed; 736 AA.
AC C0ZN58;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=RER_04020 {ECO:0000313|EMBL:BAH31110.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31110.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH31110.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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}.
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DR EMBL; AP008957; BAH31110.1; -; Genomic_DNA.
DR RefSeq; WP_020905914.1; NC_012490.1.
DR AlphaFoldDB; C0ZN58; -.
DR KEGG; rer:RER_04020; -.
DR PATRIC; fig|234621.6.peg.843; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_9_3_11; -.
DR Proteomes; UP000002204; Chromosome.
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; 2.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 2.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2.
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:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
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; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 7..99
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 220..341
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 481..575
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 587..731
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 736 AA; 78410 MW; 0DB00BF92FFA053E CRC64;
MALPLLEDHR DLAEAVAAFA NRFGGIADTR SNVKRYAAGD RPDSWDGLVR QGLHAVHLPE
QYGGDGAGLA ELAVVVEQLG DALYPGPYVP TVIASGILAT AAGPAAETML TELAAGATGA
VCTGTRLRAA RSDAGWTVSG SADPALGLPG ADVVLVRANS EDGELWFRLE PSTSAAVVIE
DGVDLTRSIG TLTLTDHQVE AGLIVDGLQA HRTELIVNTV LAAEASGIAG WALRTAVDYV
KSRQQFGRPV GSFQAVQHKA AMMLVRSEIA CAAAWDAARS EEHDEDQQKL VSAQAALAAL
PVGIENALEC VTLLGGIGFT WEHDAHLYWR RAISIAAVAG SEVKWAHTLG DRSADSERDF
SFVDPEMLPE LREQVRRVLD EVALLPDDGT TSASWAPAKG RARRARFADA KLVAPHYRAP
YGLGAGPREQ AVIAHEFAMR GWAQPSTVIG EWVLPTILEH GDAEQQDRFV EPSLRADIIW
CQLFSEPGAG SDLAGLSTKA RKVDGGWVLS GQKVWNSGAH EADWGVCLAR SDADAPKHRG
LSYFLVDMTS KGVDVRPLKQ ATGKSEFNEV FLDEVFVPDD CLVAEPGQGW KLAATTLSNE
RLSMGSTLHH GSSRLFRQVI ADASHDCPRE DAVEGLGRSI SRELALSAMN LRGVSARLAG
QEPGAEISVS KVYNALAQRE GSRDLLRLLG PRAAVVDPSA NYAIDHIGLP SILFGGGTVE
IQLNVIAQRV LGLPRS
//
