(data stored in SCRATCH zone)
SWISSPROT: E6S6S7_INTC7
ID E6S6S7_INTC7 Unreviewed; 386 AA.
AC E6S6S7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 16-JAN-2019, entry version 29.
DE SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:ADU46813.1};
GN OrderedLocusNames=Intca_0257 {ECO:0000313|EMBL:ADU46813.1};
OS Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS NBRC 12989 / 7 KIP).
OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU46813.1, ECO:0000313|Proteomes:UP000008914};
RN [1] {ECO:0000313|EMBL:ADU46813.1, ECO:0000313|Proteomes:UP000008914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC {ECO:0000313|Proteomes:UP000008914};
RX PubMed=21304734; DOI=10.4056/sigs.1263355;
RA Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Intrasporangium calvum type strain (7
RT KIP).";
RL Stand. Genomic Sci. 3:294-303(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|RuleBase:RU362125}.
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DR EMBL; CP002343; ADU46813.1; -; Genomic_DNA.
DR RefSeq; WP_013491135.1; NC_014830.1.
DR STRING; 710696.Intca_0257; -.
DR EnsemblBacteria; ADU46813; ADU46813; Intca_0257.
DR KEGG; ica:Intca_0257; -.
DR eggNOG; ENOG4105EDX; Bacteria.
DR eggNOG; ENOG410XS2V; LUCA.
DR HOGENOM; HOG000131668; -.
DR OrthoDB; 760677at2; -.
DR BioCyc; ICAL710696:GH9U-261-MONOMER; -.
DR Proteomes; UP000008914; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.540.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
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.
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; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
PE 3: Inferred from homology;
DR PRODOM; E6S6S7.
DR SWISS-2DPAGE; E6S6S7.
KW Complete proteome {ECO:0000313|Proteomes:UP000008914};
KW FAD {ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000008914}.
FT DOMAIN 22 131 Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT PF02771}.
FT DOMAIN 136 229 Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT PF02770}.
FT DOMAIN 289 383 Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT PF00441}.
SQ SEQUENCE 386 AA; 42155 MW; E6E6C798F792861D CRC64;
MAREPRAPIV PPVVVEGEVL RGLRLEVREF LAGQIESGRF TPHVDTWLTR WDRDFTRELG
RRGWLGMVIP EEYGGQGRTY LERFVVTEEL LVVGAPVAAH WVAERQIGPS LLRFGTEEQK
RHFLPRISRG DLVFGIGMSE PDSGSDLASV RTRAQQVDGG WRLTGTKVWT SGAHEADAFF
ALARSAPLDP AHRHQGLSQF IVDLRAPGVE IRPIISMGGD HHFNEVHLDG VLVPDDRVLG
TIGEGWQQVT SELGFERSGP ERYLSTFQLL AAAAEAMEAG VLPLDPGLGR HVARVAALHQ
MSFAVSTALE AHADADTAAA AVKVLGTTTE GDIADYVDTL TATGWIEDEE LHTLLHAAIL
QRPGFTLRGG TNEILRGVIA RGLGMR
//
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