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Database: UniProt
Entry: Q5ZX64_LEGPH
LinkDB: Q5ZX64_LEGPH
Original site: Q5ZX64_LEGPH 
ID   Q5ZX64_LEGPH            Unreviewed;       384 AA.
AC   Q5ZX64;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   SubName: Full=Acyl CoA dehydrogenase, short chain specific {ECO:0000313|EMBL:AAU26956.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:AAU26956.1};
GN   OrderedLocusNames=lpg0868 {ECO:0000313|EMBL:AAU26956.1};
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624 {ECO:0000313|EMBL:AAU26956.1, ECO:0000313|Proteomes:UP000000609};
RN   [1] {ECO:0000313|EMBL:AAU26956.1, ECO:0000313|Proteomes:UP000000609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513
RC   {ECO:0000313|Proteomes:UP000000609};
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(2004).
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; AE017354; AAU26956.1; -; Genomic_DNA.
DR   RefSeq; WP_010946604.1; NC_002942.5.
DR   RefSeq; YP_094903.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZX64; -.
DR   STRING; 272624.lpg0868; -.
DR   PaxDb; 272624-lpg0868; -.
DR   GeneID; 66490050; -.
DR   KEGG; lpn:lpg0868; -.
DR   PATRIC; fig|272624.6.peg.900; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_6; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000000609; Chromosome.
DR   GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; 1.
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; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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; 2.
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|RuleBase:RU362125,
KW   ECO:0000313|EMBL:AAU26956.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000609}.
FT   DOMAIN          6..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..215
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          227..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   384 AA;  42999 MW;  34C1FDE4DE581FAC CRC64;
     MHFNFTDEHL AFREMASEFA RNKLAPMADF WDEQGYFPIE TLREAAQLGM AGMVVREDIG
     GAQLSRLDAA LIFEQLATGC IPTSAYLSIH NMVASLVDRY GSQEIRKKWG PKLTSMEVIA
     SYCLTEPESG SDAASLKTRA VKEGEYYVLN GAKAFISGGS VSDVYLCMVR TGDESHHGIS
     CLLIEKNTPG LTFGKLEKKL GWRNQPTCML YFENCRVPIA NRVGEEGMGF KIALNALNGG
     RVNIASCSLG GALACLRMSQ SYMHERKQFG KPLTQMQALR FYFADMLTDY EAARLMVYRA
     AAAMDNDDPN APMYCAMGKR LATDVAFRIS DKAMQLHGGY GYLRDYQIER IFRDLRVHQI
     LEGTNEIMRE IIAKASLDEE YFIE
//
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