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Database: UniProt
Entry: A0A136JYI4_9BACT
LinkDB: A0A136JYI4_9BACT
Original site: A0A136JYI4_9BACT 
ID   A0A136JYI4_9BACT        Unreviewed;       380 AA.
AC   A0A136JYI4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KXK02217.1};
GN   ORFNames=UZ17_ACD001001587 {ECO:0000313|EMBL:KXK02217.1};
OS   Acidobacteria bacterium OLB17.
OC   Bacteria; Acidobacteriota.
OX   NCBI_TaxID=1617423 {ECO:0000313|EMBL:KXK02217.1, ECO:0000313|Proteomes:UP000070331};
RN   [1] {ECO:0000313|EMBL:KXK02217.1, ECO:0000313|Proteomes:UP000070331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB17 {ECO:0000313|EMBL:KXK02217.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Dutilh B.E., Jetten M.S.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (OCT-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:KXK02217.1}.
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DR   EMBL; LLEU01000030; KXK02217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136JYI4; -.
DR   STRING; 1617423.UZ17_ACD001001587; -.
DR   PATRIC; fig|1617423.3.peg.1652; -.
DR   Proteomes; UP000070331; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01158; SCAD_SBCAD; 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; IPR006089; Acyl-CoA_DH_CS.
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   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   380 AA;  41438 MW;  CE26AA676F7290A0 CRC64;
     MNFDLSPEQE QIKLSIREFA ESEIKPHVME WDETQHFPAE LRPKLAELGL LGILFPEELG
     GAGMGYVEYA TIIEELGRMD GSVGLSVAAH NSLCSNHIYM FGSDEQKAKY LARLAKGESF
     GAWGLTEAQA GSDSAGTRTT AVPTDGGWIV NGSKNFITHA ISCDTLVAVA VTDKEKGNHG
     ISAFIFDKSM EGFRGDKKEN KLGMRASETA SVVFEDCRVP RENLLGNEGE GFKQAMQVLD
     GGRISIAALS VGIAQGAYEA AVRYAKERQQ FGRPIADFQA IQFKLADMAT QIECSRLLTL
     KAAALKDAKR PVTQASAMAK LYASETAVRV SEECVQIHGG YGYTKDYPAE KYWRDSKLCT
     IGEGTSEIQR IVIAKNLLRA
//
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