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Database: UniProt
Entry: A0A364Y5H2_9BACT
LinkDB: A0A364Y5H2_9BACT
Original site: A0A364Y5H2_9BACT 
ID   A0A364Y5H2_9BACT        Unreviewed;       375 AA.
AC   A0A364Y5H2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DQQ10_05895 {ECO:0000313|EMBL:RAW02082.1};
OS   Pseudochryseolinea flava.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC   Pseudochryseolinea.
OX   NCBI_TaxID=2059302 {ECO:0000313|EMBL:RAW02082.1, ECO:0000313|Proteomes:UP000251889};
RN   [1] {ECO:0000313|EMBL:RAW02082.1, ECO:0000313|Proteomes:UP000251889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDU1-6 {ECO:0000313|EMBL:RAW02082.1,
RC   ECO:0000313|Proteomes:UP000251889};
RA   Li Y., Wang J.;
RT   "Chryseolinea flavus sp. nov., a member of the phylum Bacteroidetes
RT   isolated from soil.";
RL   Submitted (JUN-2018) 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:RAW02082.1}.
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DR   EMBL; QMFY01000002; RAW02082.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364Y5H2; -.
DR   OrthoDB; 1170793at2; -.
DR   Proteomes; UP000251889; 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; 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; 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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000251889}.
FT   DOMAIN          17..95
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          121..207
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          268..350
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   375 AA;  40968 MW;  27BB376555B3E2F8 CRC64;
     MVLAAINLPS ILKELAPEIE KQGQDCDVEN KFAEKNFRLL KERDVYKALI PIELGGGGVQ
     YADVCYFLKN LARLCPSTSL ALSMHMHLVA VLVFKHLNGD AMATTTLKAV AEKDLTLLST
     GGGDWVSSNG TARKVDGGYT INCTKSFCSG APMADVAVMS CAYNDGTKEQ VLHFSVSLTT
     QGVEIVNDWN AMGMRGTGSN TIHFKDVFVP EEKITLIRER GKWHQLWNVV STLAFPVFVS
     PYAGIVEEII NRTVALIAKK SDCESFCASS LGEMHNHYQI VNMALQRLID NANNLSISPS
     NNSAATALQA KSIITQHGRL SAQAAMEALG GKSYYQKTGI ERLYRDLLAG EFHPMQSSKQ
     KEMLGYHLIG RTLAG
//
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