ID A0A0H5DTD0_9BACT Unreviewed; 580 AA.
AC A0A0H5DTD0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ELAC_1757 {ECO:0000313|EMBL:CRX39084.1};
OS Estrella lausannensis.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Criblamydiaceae;
OC Estrella.
OX NCBI_TaxID=483423 {ECO:0000313|EMBL:CRX39084.1, ECO:0000313|Proteomes:UP000220251};
RN [1] {ECO:0000313|Proteomes:UP000220251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB-30 {ECO:0000313|Proteomes:UP000220251};
RA Bertelli C.;
RL Submitted (JUN-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}.
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DR EMBL; CWGJ01000025; CRX39084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5DTD0; -.
DR OrthoDB; 9802447at2; -.
DR Proteomes; UP000220251; 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; IPR049448; ACAD9/ACADV-like_C.
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; PF21343; ACAD9-ACADV_C; 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 Reference proteome {ECO:0000313|Proteomes:UP000220251}.
FT DOMAIN 57..157
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 161..261
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 274..421
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 486..533
FT /note="ACAD9/ACADV-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21343"
SQ SEQUENCE 580 AA; 63935 MW; 558F94C4756D5999 CRC64;
MDKDQIKMAE ELFFSEENKP SAAKLLYKGV FDSRAYFPFP DPSPEEKKNS ERYIASLKTH
LDKHLDPVKI DKEAIIPAET IKKLAEIGLF GISVPKEHGG LGMSQYSYCK AIEEVASRCG
STAILINAHQ SIGLKGILLF GNDAQKKRYL PPLAKGEQIA AFSLTEPNAG SDASGIETRA
VFDPERKVYR ISGRKQWTSN GSIASVLTLM AKTEVTGPKG KEDKVTAFII TPDMKGFKIL
HPGLEKVGIK GTRTTNLELT DLEVPEENIL GPLGGGLKVC LTALDFGRTT FGAMCLGASK
YCLERALSWS VERIQFRRPL ASFSLVQKKL AEMAALTFAL DATTYMTAGL IDQGQEDVML
ESAMLKVFAS ESLWSTLYDT MQIFGGRSFF TDQPFERMMR DARLNMIGEG SNEVLRAFIS
AVGLREAGAP LKEALSSLTS SPFSSGVILA NALKNLMGLS KRPSIPNKIA LIEKECAEIS
RFIPLFSKVC IKSLMKYKEG VIEKQLLLNR LTNVAIALYT SMAVISRIQD GVQDPLYRNP
EKVARFYLRW AIDTMRLNLE NIDNGEDCLV NDLSATLTGK
//
