ID   A0A0W0VCL3_9GAMM        Unreviewed;       567 AA.
AC   A0A0W0VCL3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Short chain-specific acyl CoA dehydrogenase {ECO:0000313|EMBL:KTD17884.1};
GN   ORFNames=Ljor_2190 {ECO:0000313|EMBL:KTD17884.1};
OS   Legionella jordanis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=456 {ECO:0000313|EMBL:KTD17884.1, ECO:0000313|Proteomes:UP000055035};
RN   [1] {ECO:0000313|EMBL:KTD17884.1, ECO:0000313|Proteomes:UP000055035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL-540 {ECO:0000313|EMBL:KTD17884.1,
RC   ECO:0000313|Proteomes:UP000055035};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {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:KTD17884.1}.
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DR   EMBL; LNYJ01000011; KTD17884.1; -; Genomic_DNA.
DR   RefSeq; WP_058471601.1; NZ_RDQQ01000002.1.
DR   AlphaFoldDB; A0A0W0VCL3; -.
DR   STRING; 456.Ljor_2190; -.
DR   PATRIC; fig|456.5.peg.2358; -.
DR   OrthoDB; 9771038at2; -.
DR   Proteomes; UP000055035; 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; 2.40.110.20; -; 1.
DR   Gene3D; 6.10.250.600; -; 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; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR041504; AidB_N.
DR   PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF18158; AidB_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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000055035}.
FT   DOMAIN          60..158
FT                   /note="Adaptive response protein AidB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18158"
FT   DOMAIN          180..277
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          289..449
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   COILED          478..508
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   567 AA;  65204 MW;  CC804BBC18767F8E CRC64;
     MTELDAHQKA REHFSNWQQQ LRTNILLEDS SLMHSYRCYF ASEPEFLQEL QKFSIRVVTE
     LEPLVMENNL DANLPKLDQY DALGHRQDKV IHHPSYQAAG DVIYGSGLMH YLLKPGQMRK
     TLSLFLLSSH AGEAGHNCPI ACSAGIIRVL NHHQNKADSS LYLQKLSEPS FRENFTGAQF
     LTEIQGGSDV GTNASYAYQD DEQQWRIVGE KWFCSNANAE LILMTARFDK QKEGTKGLGL
     FLVPSRLANG EQNHYRIRRL KQKIGTRSMA TGEIDFEGAY AFPIEPIHEG IHLVMENVLH
     LSRMFNAFSV LGMARRAYQI AYYYAMNRVA FNHYIIDYPL VKETLAEIKA DNLAMLASIF
     HMAYLQDDLD KKPASEQDKE RQLLMRTLAN LNKYFTAKHS VENIHHCIDI LAGNGTIESF
     SSLPRLLRDC IVCENWEGTH FTLWMQLLRD IHKFHVDEII MQHLWQLLEQ QPENFEYKNM
     LKEKIEALRD ELSELKKLST EEQNLNIKGI VEQLATLNCA LTLALELKID QPPAAKKASL
     KLFLQKHLAC KHTKDKHYLM LLNEVLG
//