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Database: UniProt
Entry: W5TPL7_9NOCA
LinkDB: W5TPL7_9NOCA
Original site: W5TPL7_9NOCA 
ID   W5TPL7_9NOCA            Unreviewed;       396 AA.
AC   W5TPL7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AHH19196.1};
GN   ORFNames=NONO_c44120 {ECO:0000313|EMBL:AHH19196.1};
OS   Nocardia nova SH22a.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH19196.1, ECO:0000313|Proteomes:UP000019150};
RN   [1] {ECO:0000313|EMBL:AHH19196.1, ECO:0000313|Proteomes:UP000019150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH22a {ECO:0000313|EMBL:AHH19196.1};
RX   PubMed=24747905;
RA   Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT   "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT   Analysis of the Complete Genome of Nocardia nova SH22a.";
RL   Appl. Environ. Microbiol. 80:3895-3907(2014).
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}.
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DR   EMBL; CP006850; AHH19196.1; -; Genomic_DNA.
DR   RefSeq; WP_025350604.1; NZ_CP006850.1.
DR   AlphaFoldDB; W5TPL7; -.
DR   STRING; 1415166.NONO_c44120; -.
DR   KEGG; nno:NONO_c44120; -.
DR   PATRIC; fig|1415166.3.peg.4531; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_9_0_11; -.
DR   OrthoDB; 5167280at2; -.
DR   Proteomes; UP000019150; 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:SF4; ACYL-COA DEHYDROGENASE FADE34; 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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019150}.
FT   DOMAIN          17..108
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          114..208
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          220..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   396 AA;  43295 MW;  7E920855C36A3702 CRC64;
     MSTDIDAARV AEAARGVVRE HDPRSVPVSE FLGACFDAGL SWVHFPEGHG GLGVSRGLQA
     VADAIFQEAG APVPYSLNPI GFGMAAPTLQ EHARGDELKR KWLRPLASLD DIWCQLFSEP
     GAGSDLAGLA TSAVRDGDEW VVNGQKVWTT LAHRASWALL IARTDPDVVK HKGLTYFVVD
     MRAPGVDVRP LRQMTGDAEF NEVYLTDVRI PDAHRLGAVG DGWRVAMTTL MNERNSIGAS
     GTRRGDGTIA DAVALWAQRP DLHTPVRRDR LARLWLRSEA QRLTSERSRA TATVDGPGPE
     GSIGKLVGAE LNQQVYEFCM DLLGTEGLLY GDYAMRRIDT VEDYPLVQQR FLRSRANTIE
     GGTSEVLRNI LGERILGLPG DLRADSGRPW REVPRG
//
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