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Database: UniProt
Entry: A0A1M7HRK9_9BACT
LinkDB: A0A1M7HRK9_9BACT
Original site: A0A1M7HRK9_9BACT 
ID   A0A1M7HRK9_9BACT        Unreviewed;       602 AA.
AC   A0A1M7HRK9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SHM31048.1};
GN   ORFNames=SAMN04488057_10128 {ECO:0000313|EMBL:SHM31048.1};
OS   Cyclobacterium lianum.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=388280 {ECO:0000313|EMBL:SHM31048.1, ECO:0000313|Proteomes:UP000184513};
RN   [1] {ECO:0000313|EMBL:SHM31048.1, ECO:0000313|Proteomes:UP000184513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6102 {ECO:0000313|EMBL:SHM31048.1,
RC   ECO:0000313|Proteomes:UP000184513};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FRCY01000001; SHM31048.1; -; Genomic_DNA.
DR   RefSeq; WP_073089838.1; NZ_FRCY01000001.1.
DR   AlphaFoldDB; A0A1M7HRK9; -.
DR   STRING; 388280.SAMN04488057_10128; -.
DR   OrthoDB; 1489360at2; -.
DR   Proteomes; UP000184513; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184513}.
FT   DOMAIN          32..144
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          149..243
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          255..418
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          468..571
FT                   /note="Acyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21263"
SQ   SEQUENCE   602 AA;  65970 MW;  E3DBE39219B2F52F CRC64;
     MEPLTKNKAL NGGEYLIRES AAADVFIPES FSEEQKMMAA ASQEFLDREI LPHMEEIDSM
     KNPDLVPQIL KKAGELGLLA ISVPETYGGL GMSFNTSMLI ADIIGAAGSF STTYGAHTGI
     GILPVLYYGT DQQKEKYLPK LSNAEWAACY CLTEPDAGSD ANSGQTRAVL NEEGTHYLIN
     GQKMWISNAG FADFFIVFAK VDDDKNLTAF LVEKTFGGIS MNEEEKKMGI KGSSTRQVFF
     RDCPVPVGNM LSERGQGFKI AVNILNIGRI KLGAGVLGGC RRLLGLSIQY ASERKQFGVP
     INSFGAIKAK LAEMAIKTYA CESLCYRAGQ DIEDRIAALE AAGMEASKAK LKGVEEFAIE
     CAIAKVHGSE VLDFVADQGV QIFGGMGYSA EAPMERAYRD ARISRIYEGT NEINRILMVG
     MLLKRAMKGE LAIMDAGKQV GEELKAVPDF TSRDYSAPLS REKAILQNLK KVFLMIGGQA
     AKNLGDQLES EQEIMMHLAD IMIEIYAAES TLLRTEKLLS EKGTEAVKTH LAASRVYLYE
     AVDKINVAGK EAIYAFTSGD EQKLLLMGLK RFTKTDAVNT KMLRREVADA LIAEGRYFFF
     YA
//
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