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Database: UniProt
Entry: A0A0J5GW26_9BACI
LinkDB: A0A0J5GW26_9BACI
Original site: A0A0J5GW26_9BACI 
ID   A0A0J5GW26_9BACI        Unreviewed;       594 AA.
AC   A0A0J5GW26;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KMJ58874.1};
GN   ORFNames=AB685_07295 {ECO:0000313|EMBL:KMJ58874.1};
OS   Bacillus sp. LL01.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1665556 {ECO:0000313|EMBL:KMJ58874.1, ECO:0000313|Proteomes:UP000036436};
RN   [1] {ECO:0000313|EMBL:KMJ58874.1, ECO:0000313|Proteomes:UP000036436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL01 {ECO:0000313|EMBL:KMJ58874.1,
RC   ECO:0000313|Proteomes:UP000036436};
RA   Vilo C., Galetovic A., Araya J., Gomez Silva B., Dong Q.;
RT   "Draft Genome Sequence of a Bacillus Bacterium from the Atacama Desert
RT   Wetlands Metagenome.";
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}.
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:KMJ58874.1}.
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DR   EMBL; LFEL01000002; KMJ58874.1; -; Genomic_DNA.
DR   RefSeq; WP_047969931.1; NZ_LFEL01000002.1.
DR   AlphaFoldDB; A0A0J5GW26; -.
DR   PATRIC; fig|1665556.3.peg.2429; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000036436; 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   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; IPR049426; Acyl-CoA-dh-like_C.
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; PF21263; Acyl-CoA-dh_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.
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          31..143
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          147..239
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          252..415
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          463..566
FT                   /note="Acyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21263"
SQ   SEQUENCE   594 AA;  65393 MW;  D4AE239A0EA73F1F CRC64;
     MSNTLENVIK GGSFLLDDIA AEKVFTPEDF SDEHKLIAKT TEEFVLNEVV PNLEEIEHHN
     FDISVKLLKE AGELGLLGAD VQEEYGGFGL DKISSSLITE KFSRAGGFSL SYGAHVGIGS
     LPIVLFGNED QKQKYLPKLS SGELLAAYAL TEPGSGSDAL GAKTTAKLND EGTHYVLNGE
     KQWITNAGFA DVFVVYAKVD GEHFSAFIVE REFGGVSTGP EEKKMGIKGS STRTLILEDA
     LVPKENLLGE IGRGHVIAFN ILNIGRYKLA VGTVGGSKRG IELAATYANQ RQQFKTPIAK
     FSLIQEKLAN MATKTYATES SVYRTVGLFE DSMGRLTKEE EKDPNAVAKA VAEYAIECSL
     NKVFGSETLD YVVDEAVQIH GGYGFMAEYE VERMYRDSRI NRIFEGTNEI NRLLVPGTFL
     RKALKGELPL IQKAQSLQEE LMMLMPEEVG DGVLEQEKYL VKNAKKIAIL MTGLVAQKYG
     KALEREQELL VNIADIISNV YAMESAVLRT EKAIAKSGED KNKLKVLYTQ VFCQEAFNQI
     EADAKETLVA AETGDTLRMM ISALRKFTRH TPINVVAKKR EIAAVVLDVQ KYTV
//
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