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Database: UniProt
Entry: A0A1Q7YCB2_9CYAN
LinkDB: A0A1Q7YCB2_9CYAN
Original site: A0A1Q7YCB2_9CYAN 
ID   A0A1Q7YCB2_9CYAN        Unreviewed;       599 AA.
AC   A0A1Q7YCB2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OLE52911.1};
GN   ORFNames=AUI36_17905 {ECO:0000313|EMBL:OLE52911.1};
OS   Cyanobacteria bacterium 13_1_40CM_2_61_4.
OC   Bacteria; Cyanobacteriota.
OX   NCBI_TaxID=1805101 {ECO:0000313|EMBL:OLE52911.1, ECO:0000313|Proteomes:UP000186010};
RN   [1] {ECO:0000313|EMBL:OLE52911.1, ECO:0000313|Proteomes:UP000186010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLE52911.1}.
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DR   EMBL; MNHI01002333; OLE52911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7YCB2; -.
DR   Proteomes; UP000186010; 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; 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          33..145
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          149..242
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          254..419
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          465..568
FT                   /note="Acyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21263"
SQ   SEQUENCE   599 AA;  64844 MW;  011D34AD499EC583 CRC64;
     MATTTIPRTA IKGGSFLIES CRPEEIFSPA DLSDDQKLIG QTAEEFVTKE VLPLANELEQ
     HKEGLMPELV RKAAELGLMG GGIPEEYGGS GLDKISATVL AEKLSAYASF SVTHGAHAGI
     GTLPIVYFGT EEQKKKYLPK LASGELIAAY CLSEPQAGSD AQNARTRAVL SPDGKHWILN
     GQKMWITNGG FADVYIVFAK VNGEKFSCFI VERGHPGFSV GAEEKKMGIK GSSTVPIFFE
     NCQVPRENLL HEIGRGHIVA FNILNVGRYS LGAYCVGGTK KVLETSSKYA KERTAFGKPI
     GEFGLVRAKL AEMAIRTYAV ESMLYRSAGM IEGAMSAAGA AADKTQQLMK VLEEYAIESS
     INKVYGSEVL SFVVDEAVQI YGGYGFHEDY PVARTYRDSR INRIFEGTNE INRLLIIQML
     LKRALSGALP LMAAGAKLQE EILAGPQFEE AATGPFAEDE RAVANAKKTF LLAAGAAVQK
     HREQLADQQE IVGALANIVM EVYGMESSLR RAQKGVAARG EASAAAMVDA ARVFLYDAAD
     RVEKEARTAL SAVGEGDMLR TQLAVLKRFS KREPVDTVAL RRRVAAAVQA GDRYPFEGR
//
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