ID K5BD91_MYCHD Unreviewed; 396 AA.
AC K5BD91;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Acyl-CoA dehydrogenase FadE17 {ECO:0000313|EMBL:VCT92328.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:VCT92328.1};
DE SubName: Full=Acyl-CoA dehydrogenase, N-terminal domain protein {ECO:0000313|EMBL:EKF21306.1};
GN ORFNames=C731_4722 {ECO:0000313|EMBL:EKF21306.1}, MHAS_04055
GN {ECO:0000313|EMBL:VCT92328.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF21306.1, ECO:0000313|Proteomes:UP000006265};
RN [1] {ECO:0000313|EMBL:EKF21306.1, ECO:0000313|Proteomes:UP000006265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 {ECO:0000313|EMBL:EKF21306.1}, and DSM 44199 / CIP
RC 105218 / JCM 12690 / 3849 {ECO:0000313|Proteomes:UP000006265};
RX PubMed=23209251; DOI=10.1128/JB.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
RN [2] {ECO:0000313|EMBL:VCT92328.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mhassiacum {ECO:0000313|EMBL:VCT92328.1};
RA Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA Castillo E.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000268660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC {ECO:0000313|Proteomes:UP000268660};
RX PubMed=30701245; DOI=10.1128/mra.01522-18;
RA Sanchez M., Blesa A., Sacristan-Horcajada E., Berenguer J.;
RT "Complete genome sequence of Mycolicibacterium hassiacum DSM 44199.";
RL Microbiol. Resour. Announc. 8:e01522-e01522(2019).
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; AMRA01000150; EKF21306.1; -; Genomic_DNA.
DR EMBL; LR026975; VCT92328.1; -; Genomic_DNA.
DR RefSeq; WP_005632353.1; NZ_LR026975.1.
DR AlphaFoldDB; K5BD91; -.
DR STRING; 1122247.GCA_000379865_03601; -.
DR KEGG; mhas:MHAS_04055; -.
DR PATRIC; fig|1122247.3.peg.4521; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 3964153at2; -.
DR Proteomes; UP000006265; Unassembled WGS sequence.
DR Proteomes; UP000268660; Chromosome 1.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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 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:UP000006265}.
FT DOMAIN 8..121
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 125..218
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 231..391
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 396 AA; 43246 MW; 64E1ED469274144B CRC64;
MDLNDSPAEA RFRARLRAWL ADTLPTLPWP EPADMHERRR FWSVWQRKLF DAGFAGLSWP
AEYGGAGADA KIKAIFNEEL DRAGAPDRLN IIGEDFAGPT IVAFGTDEQK RRYLEPILKG
DEIWCQLFSE PESGSDLASL RTTATKVDGG WKINGQKIWT SRAQIADNAI LLARTGGGER
HKGITYFLVS MASPGITVRP LAHMLGEAEF NEVFLDDVFV PDGNVVGAVD GGWKVAMATL
SFERVGIATG RVNTTRAVAD LVDQIKRGTT DDGRPLAADP LVRQRIADLY GRALTHYLIG
QRVITGAASG EPPGPVTSIG KLYFCPLVED IADFGLELTD FGGQFGLDEA GRDDTDPEQQ
RWLRLAYQAR GTAIAGGSTF IQRNIAAERV LGMPRG
//
