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Database: UniProt
Entry: C1AYD0_RHOOB
LinkDB: C1AYD0_RHOOB
Original site: C1AYD0_RHOOB 
ID   C1AYD0_RHOOB            Unreviewed;       733 AA.
AC   C1AYD0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:BAH54125.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:BAH54125.1};
GN   OrderedLocusNames=ROP_58780 {ECO:0000313|EMBL:BAH54125.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH54125.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH54125.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH54125.1,
RC   ECO:0000313|Proteomes:UP000002212};
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-2009) 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}.
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DR   EMBL; AP011115; BAH54125.1; -; Genomic_DNA.
DR   RefSeq; WP_015889619.1; NC_012522.1.
DR   AlphaFoldDB; C1AYD0; -.
DR   STRING; 632772.ROP_58780; -.
DR   KEGG; rop:ROP_58780; -.
DR   PATRIC; fig|632772.20.peg.6143; -.
DR   HOGENOM; CLU_018204_9_3_11; -.
DR   OMA; CMSIAGG; -.
DR   OrthoDB; 2431337at2; -.
DR   Proteomes; UP000002212; 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; 1.
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; 2.
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};
KW   Oxidoreductase {ECO:0000313|EMBL:BAH54125.1}.
FT   DOMAIN          6..89
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          207..351
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          389..463
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          467..562
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          623..719
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   733 AA;  77296 MW;  6E44FAF6D5FA27A2 CRC64;
     MTMGLTEEER DLRDSVRGWA TRTVTPDVLR EAVEAKTEQR PSFWTSLAEL GVLGLHLPEE
     AGGAGCGLVE LAVVTEELGR VLLPGPFLPT VLLGAVLHES GRAGELSGLA DGTTLGAVAL
     QPGSLRLVRD GGAVTLDGES GYVLGGQVGD LFLLAAADGD DTVFVALTPD RLGVTDLPSH
     DVVRRNATAA VTGLEIADAD VLQIDAQRVL DLAATLFAAE ASGVADWAVT TAADYARVRR
     QFGRPIGQFQ GVKHRVARML GLAEQARVCA WDAARAMNPG TGAAEASLAA AVAGATAPES
     AFSVTKDCIQ VLGGIGYTWE HDAHLYLRRA QSLRILLGST AFWRRRVARA TLGGARRVLG
     IDLPPEAAGL RAGIRAELAA AASLCEEERG TYLAEKGYTA PHLPAPWGRG AGAVEQLVIA
     EELRAAALKP HDMIIGNWVV PTLIAHGSDD QLQRFVPQSL RGDLVWCQLF SEPGAGSDLA
     GLTTRATKVD GGWVLRGQKV WTSMARDADW GICLARTDAS VPKHKGLSYF LIDMKASEGL
     DIRPLREITG EALFNEVFLD DVFVPDELLV GDPGDGWKLA RTTLANERVS LSHDSSLGSG
     GEALLTLAGE LPGGIDDEQL TVLGKVLCDA QSGGLMGLRT TLRSIAGGQP GAESSVAKLL
     GVEHIQQVWE VAMDWAGPRA LLGDRPRTSD TQMFLNSQCM SIAGGTTNVQ LNIIGERLLG
     LPRDPEPGQG AVA
//
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