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
//