ID A0A177HWR1_9ACTN Unreviewed; 652 AA.
AC A0A177HWR1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OAH15363.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:OAH15363.1};
GN Name=mmgC_3 {ECO:0000313|EMBL:OAH15363.1};
GN ORFNames=STSP_12840 {ECO:0000313|EMBL:OAH15363.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH15363.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH15363.1, 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:OAH15363.1}.
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DR EMBL; LOHS01000046; OAH15363.1; -; Genomic_DNA.
DR RefSeq; WP_067273197.1; NZ_LOHS01000046.1.
DR AlphaFoldDB; A0A177HWR1; -.
DR STRING; 1716141.STSP_12840; -.
DR PATRIC; fig|1716141.3.peg.1357; -.
DR OrthoDB; 8876745at2; -.
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 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; IPR013786; AcylCoA_DH/ox_N.
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:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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 ECO:0000313|EMBL:OAH15363.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077381}.
FT DOMAIN 68..173
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 178..274
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 286..444
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 71411 MW; B6B937A3025664AF CRC64;
MSAPTKRPDV TTRRPAVTER EARQVAEAAR EQDWRKPSFA KELFLGRFRL DLIHPHPTPP
DEDAQRGEEF LAKLRDFCET KIDGARIERE AQIPDEVIQG LKELGALGMK IDTKYGGLGL
SQVYYNKALA LVGSASPAIG ALLSAHQSIG VPQPLKLFGT QEQKDAFLPR CARTDITAFL
LTEPDVGSDP ARLATTAVPD GDDYILDGVK LWTTNGVVAD LLVVMARVPK SEGHRGGITA
FVVEAGSEGI TVENRNAFMG LRGIENGVTR FHQVRVPAAN RIGQEGAGLK IALTTLNTGR
LSLPAMCAGA GKWCLKIARE WSAAREQWGK PIAHHEAVGE KISFIAATTF ALEAVLDLAS
QMADENRNDI RIEAALAKLY GSEMAWLMAD ELVQIRGGRG FETAESLAAR GERAVPAEQI
LRDLRINRIF EGSTEIMHLL IAREAVDAHL SVAGDLIDPE KSLSDKAKAG AKAGGFYARW
LPKLVAGPGQ LPRAYADFHP AGHVDLSTHL RYVERSARKL ARSTFYGMSR WQGRMETKQG
FLGRVVDIGA ELFAMSAACV RAEMLRTTEE YGREAYQLAD AFCQQSRIRV DELFARLWTN
TDDLDRKVVK GVMSGMYTWL ESGIIDPSGE GPWIADATPG PARRENVHRP IG
//
