ID A0A177HWB0_9ACTN Unreviewed; 608 AA.
AC A0A177HWB0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OAH14909.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:OAH14909.1};
GN Name=mmgC_5 {ECO:0000313|EMBL:OAH14909.1};
GN ORFNames=STSP_17460 {ECO:0000313|EMBL:OAH14909.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH14909.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH14909.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAH14909.1}.
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DR EMBL; LOHS01000053; OAH14909.1; -; Genomic_DNA.
DR RefSeq; WP_067274227.1; NZ_LOHS01000053.1.
DR AlphaFoldDB; A0A177HWB0; -.
DR STRING; 1716141.STSP_17460; -.
DR PATRIC; fig|1716141.3.peg.1830; -.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000077381; Unassembled WGS sequence.
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; cd01153; ACAD_fadE5; 1.
DR Gene3D; 2.40.110.20; -; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR034188; FadE5-like.
DR PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF12418; AcylCoA_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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000077381}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 162..271
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 286..451
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 471..604
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 608 AA; 66334 MW; 83B9D3E23658935C CRC64;
MGHYKSNLRD IEFNLFEVLG RDKLYGTGPF AEMDTDTAKS ILDELTRLAE NELAESFADA
DRNPPVFDPE TNTAPVPASF KKSYKAFMDS EYWRLGLPEE IGGTTAPPSL IWSYAELILG
ANPAVWMYSS GPAFAGILFD EGNEVQKKIA QIAVERTWGS TMVLTEPDAG SDVGAGRTKA
IQQEDGSWHI EGVKRFITSG EHDMEENILH YVLARPEGAG PGTKGLSLFL VPKYLFDFET
GELGERNGVY ATNVEHKMGL KASNTCEMTF GDKHPAKGWL IGDKHDGIRQ MFRIIEFARM
MVGTKAISTL STGYLNALEY AKERVQGPDL ANFMDKTAPK VTITHHPDVR RSLMTQKAYA
EGMRALVLYT ASIQDAIAVK EAAGEDVSQE HALNDLLLPI VKGYGSEKGY EQLAQSLQTF
GGSGFLQEYP IEQYIRDAKI DTLYEGTTAI QGQDYFFRKI VRNQGAALNS LAEEIKKFLA
IGTGGDELAA ARDQLAKAAV ELEAIVGVML TDLAATEQDV KNIYKVGLNT TRLLLASGDV
VVGYLLLKGA AVAAEKLPAA SAKDKAFYTG KIAAAKFFAA NILPGVAVQR QLAEAVELDL
MDLDEAAF
//
