ID A0A1M4TRX2_9ACTN Unreviewed; 416 AA.
AC A0A1M4TRX2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SAMN02745225_00710 {ECO:0000313|EMBL:SHE47047.1};
OS Ferrithrix thermotolerans DSM 19514.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Acidimicrobiaceae; Ferrithrix.
OX NCBI_TaxID=1121881 {ECO:0000313|EMBL:SHE47047.1, ECO:0000313|Proteomes:UP000184295};
RN [1] {ECO:0000313|Proteomes:UP000184295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19514 {ECO:0000313|Proteomes:UP000184295};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQUL01000006; SHE47047.1; -; Genomic_DNA.
DR RefSeq; WP_072788771.1; NZ_FQUL01000006.1.
DR AlphaFoldDB; A0A1M4TRX2; -.
DR STRING; 1121881.SAMN02745225_00710; -.
DR GeneID; 78385455; -.
DR OrthoDB; 3964153at2; -.
DR Proteomes; UP000184295; 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; cd01152; ACAD_fadE6_17_26; 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; 1.
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:SF3; ACYL-COA DEHYDROGENASE FADE29; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000184295}.
FT DOMAIN 7..124
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 128..221
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 234..394
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 416 AA; 45893 MW; A490130DDAF37C00 CRC64;
MDITYPESAE KFRAKVRDFL ASNLPKDWRG VGGLSRDEAA DFTEKWRNVL YREGYLAVGW
PKEYGGAGLS QLEQVVLAEE FTRAGVPSGG PNDAFGIQML GNTLIRWGTE EQKKRFLPRI
LSGEDRWCQG YSEPNAGSDL ANLACRAVLD GDEWVINGQK IWTSAGHLAN WIFVLTRTDP
EAPKHKGISF LLCPMDQPGV EVRPIKMISG ESEFNEVFFT DARTSKDNIV GAPGEGWSVA
MTLLGYERGE AAATIPIRFR AELDRLLELA KETGASSNPV FRDRLAYCYS KVEIMRYLGY
RTLTSFLSGG APGPEASISK LYWSEYHKVV TELAVDMLGL EALVPSGRKP TSAFQTDDIG
APNSSNSWVM TYLNARAGTI YAGTSQIQKN ILGELVLGLP KEPRLDKGPW NASSSK
//
