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Database: UniProt
Entry: D3Q0W0_STANL
LinkDB: D3Q0W0_STANL
Original site: D3Q0W0_STANL 
ID   D3Q0W0_STANL            Unreviewed;       553 AA.
AC   D3Q0W0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ADD43710.1};
GN   OrderedLocusNames=Snas_4058 {ECO:0000313|EMBL:ADD43710.1};
OS   Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS   NBRC 102104 / LLR-40K-21).
OC   Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC   Stackebrandtia.
OX   NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD43710.1, ECO:0000313|Proteomes:UP000000844};
RN   [1] {ECO:0000313|EMBL:ADD43710.1, ECO:0000313|Proteomes:UP000000844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC   LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX   PubMed=21304662; DOI=10.4056/sigs.47643;
RA   Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA   Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT   40K-21).";
RL   Stand. Genomic Sci. 1:292-299(2009).
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|RuleBase:RU362125}.
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DR   EMBL; CP001778; ADD43710.1; -; Genomic_DNA.
DR   RefSeq; WP_013019281.1; NC_013947.1.
DR   AlphaFoldDB; D3Q0W0; -.
DR   STRING; 446470.Snas_4058; -.
DR   KEGG; sna:Snas_4058; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_492503_0_0_11; -.
DR   OrthoDB; 6637748at2; -.
DR   Proteomes; UP000000844; 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   CDD; cd00567; ACAD; 1.
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; 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; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF43; ACYL-COA DEHYDROGENASE; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 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:UP000000844}.
FT   DOMAIN          156..243
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          275..405
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   553 AA;  59782 MW;  A1FDE6CEEB855A35 CRC64;
     MTTLMTATSS LPSLFDELCL GRIRWDLLRP FPIQGATDRA HGEAVTGELN RVLAKYGEPH
     HTDTSALITK ELLCDLAAPE LLGPRPAETE LSDTNLFRLL ETAADWTPAL GTATAVNRLL
     GAWSYLPLTQ DGRLREFILA NTPGRVGAGA DTDLSGAGSR LRSVTATPVD DGSAFLLNGT
     KAFVTNAPIA DIIDVSATVV DDAQPRVVLF FLTTDTPGVE IGHRHDLTGP DGLPNGMVRL
     TDVRVPREHI LGDADLGWQS IPDLTSLMVR ARFFVVSAPS LSLIKHCVRS AAEFAARRLV
     DQVPLVEYDY IEHLLAGIGA ERFAAQSLVD WCTLATGRAN TIPEQRVAKN LMSMACWRVA
     DQATSIMGAQ GVETAAGKRD RGAPAAGSVE HALRTARAMR VAGGVDFLVD YLAGCAGVFP
     LHYDAAQPVG SSTVIPADLP DPLRGHAEFL TWEVHRFAER ARAFVRRYPD PAQLHERQAI
     PILMNRIASE LLAMVLTVAR AGDPGTDPLP VDLANTYCAR ARRRIADAFR ELNDGTPPGR
     RRIVRELLKG VSK
//
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