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Database: UniProt
Entry: A0A1X1QGG1_9GAMM
LinkDB: A0A1X1QGG1_9GAMM
Original site: A0A1X1QGG1_9GAMM 
ID   A0A1X1QGG1_9GAMM        Unreviewed;       594 AA.
AC   A0A1X1QGG1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ORU90247.1};
GN   ORFNames=A6F71_04580 {ECO:0000313|EMBL:ORU90247.1};
OS   Cycloclasticus sp. symbiont of Poecilosclerida sp. M.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=1840537 {ECO:0000313|EMBL:ORU90247.1, ECO:0000313|Proteomes:UP000193579};
RN   [1] {ECO:0000313|EMBL:ORU90247.1, ECO:0000313|Proteomes:UP000193579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Specimen M {ECO:0000313|EMBL:ORU90247.1};
RA   Rubin Blum M., Dubilier N.;
RT   "Short-chain alkanes fuel the metabolism of mussel and sponge
RT   Cycloclasticus symbionts from deep-sea gas and oil seeps.";
RL   Submitted (APR-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}.
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:ORU90247.1}.
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DR   EMBL; LWTN01000228; ORU90247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1QGG1; -.
DR   STRING; 1840537.A6F71_04580; -.
DR   Proteomes; UP000193579; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 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.
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:UP000193579}.
FT   DOMAIN          79..157
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          162..271
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          281..450
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          471..589
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   594 AA;  65150 MW;  6222F78DA705D223 CRC64;
     MATFKAPVED IKYLNNEFLD TSELSGIPMF DEMTPDLTDV IFEEAGKISE ALLFPLNRSG
     DEQGCSFNNG KVTTPDGFKE AYTEMTKSGW GNLTCNKQHG GQGLPHYIAN AVDEMIISSN
     MSFSIYMGLT IGAYNAIEKF ASEGLKQKFL PNMVSGKWSG TMCLTEPHCG TDLALIRTLA
     TPLSDGSYDI TGSKIFISAG EHDLTENILH LVLARTPGAP AGIKGISLFI VPKIKINKDD
     SLDEPNNVTC SGIEHKMGIK ASSTCAIEFK ESQGYLIGEL NKGMKAMFIM MNGARIHVGI
     QGLAQAHASY SGAVDYAKER LQGRSLTGIK HPDKVADPLI VHPNVRHMLM SMKAYTEGAR
     ALSTWLSFKL DVSHHAKTKQ QRQEADELVS LVTPVFKSFL TDIGETVTSL GIQVYGGHGY
     IRENGMEQYL RDARICKIYE GTNGIQALDL VGRKLPTHMG RYLRYFFHPL SNFLESHAEN
     ESMSAYIQPL TKSFFRLQTA TLVIAQKGLA NPDEAGAAAR DYLNIFGLVA LGYMWAKMAG
     QALNNSGNMP KNFYDAKLKT GLFFMQKLLP QTGSLLSSIM AGGHSTMSLN EDQF
//
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