ID A0A0I9Y8R4_9MYCO Unreviewed; 599 AA.
AC A0A0I9Y8R4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KLO36137.1};
GN ORFNames=ABH38_13065 {ECO:0000313|EMBL:KLO36137.1};
OS Mycobacterium haemophilum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO36137.1, ECO:0000313|Proteomes:UP000036334};
RN [1] {ECO:0000313|EMBL:KLO36137.1, ECO:0000313|Proteomes:UP000036334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA Greninger A.L., Cunningham G., Miller S.;
RT "Genome sequence of Mycobacterium haemophilum.";
RL Submitted (MAY-2015) 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:KLO36137.1}.
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DR EMBL; LDPR01000010; KLO36137.1; -; Genomic_DNA.
DR RefSeq; WP_047314798.1; NZ_LDPT01000009.1.
DR AlphaFoldDB; A0A0I9Y8R4; -.
DR STRING; 1202450.B586_03060; -.
DR PATRIC; fig|29311.18.peg.4218; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000036334; 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; 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; IPR006089; Acyl-CoA_DH_CS.
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.
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 Reference proteome {ECO:0000313|Proteomes:UP000036334}.
FT DOMAIN 33..180
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 192..293
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 312..464
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 599 AA; 65855 MW; 4981C51B94A9DE6B CRC64;
MYEYDVEPAD RLPFCTAEKA QRYRTDNYRG AVGRNWYRTD PTLQFTMAYY LQPDELAFAE
PHLTRIGELM GGPVARWAEE TDRNPPRLDR YDRWGHDISR VTMPASFTQA RRAVLDAQQT
LRSEAQAAKL SSSLPLFASN YLLNQADIGM GCALGTGGGM VQSLVAAYAP PDVREHVLAK
FDSGEWAGQT AQLLTERTGG SDLGALETTA RRAAEGGDAW LLNGVKWFAS NCAGEAFVVL
AKPEGAPDST RGVATFLVLR TRRDGSRNGV RVRRLKDKLG TRSVASGEVE FVDAEAFLLS
EKPSGDTGPA DGKGLGRMME LTNAARLGIA LFGLGNARRA LVESLCYARQ RRAFGGPLID
KPLMRRKLSE LIVDVEAALA LVFDCTGATN HRQPRNRRQR IAVPVTKLKV CRLGITAASD
AIEIHGGNGY IEDWPVARLL RDAQVNTIWE GPDNILCLDV RRGIEQTRAH ETLLARLHDA
ISVSDDTEDG GDTTRLVAER LDDLDAAITA WTKLDREVAE ARLFPLAQFM GDVYAGALLT
EQAAWEQATR GSDRKALVAR LYARRHLADR GPLRGIDADS DEALERFDEL VDGAFTPRV
//
