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Database: UniProt
Entry: I0ALX3_IGNAJ
LinkDB: I0ALX3_IGNAJ
Original site: I0ALX3_IGNAJ 
ID   I0ALX3_IGNAJ            Unreviewed;       381 AA.
AC   I0ALX3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AFH49980.1};
GN   OrderedLocusNames=IALB_2277 {ECO:0000313|EMBL:AFH49980.1};
OS   Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS   Mat9-16).
OC   Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC   Ignavibacteriaceae; Ignavibacterium.
OX   NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH49980.1, ECO:0000313|Proteomes:UP000007394};
RN   [1] {ECO:0000313|EMBL:AFH49980.1, ECO:0000313|Proteomes:UP000007394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC   {ECO:0000313|Proteomes:UP000007394};
RX   PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA   Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA   Bryant D.A.;
RT   "Complete genome of Ignavibacterium album, a metabolically versatile,
RT   flagellated, facultative anaerobe from the phylum Chlorobi.";
RL   Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH49980.1; -; Genomic_DNA.
DR   RefSeq; WP_014561129.1; NC_017464.1.
DR   AlphaFoldDB; I0ALX3; -.
DR   STRING; 945713.IALB_2277; -.
DR   GeneID; 78243879; -.
DR   KEGG; ial:IALB_2277; -.
DR   PATRIC; fig|945713.3.peg.2284; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_10; -.
DR   OrthoDB; 9764422at2; -.
DR   Proteomes; UP000007394; Chromosome.
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; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007394}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..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   381 AA;  41725 MW;  67987EF9AA57A873 CRC64;
     MEFNFTEEQL MIQESARDFA QNEIAPSAVE RDIKAEFPYE IVKKMGELGF MGMMVPPEFG
     GAGLDTVSYV LAMIEISKVD ASVGVIMSVN NSLVCYGLEK YGSPYIKEKY LIPLAKGEKL
     GAFALSEPEA GSDATKQKTT ADKDGNYYVL NGIKNWITNG TTADYVLVMA TTDKSKGHKG
     ISTFVVEKGY EGFGHGVKED KLGIRSSDTC SLTFENCRVP AQNLVWEEGK GFNFAMNTLN
     GGRIGIAAQA IGIAEASLEA ALKYSKQRKA FGQEIANFQA IQFKLADMAV KVDAAKLLTL
     KAAALKDAAK PYYKEAAMAK LYASKIAVEC ALEAIQIHGG YGYVREYLVE RYLRDAKITE
     IYEGTSEIQR IVIARALLDQ K
//
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