ID K5BI11_MYCHD Unreviewed; 731 AA.
AC K5BI11;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Acyl-CoA dehydrogenase FadE34 {ECO:0000313|EMBL:VCT92883.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:VCT92883.1};
DE SubName: Full=Acyl-CoA dehydrogenase, N-terminal domain protein {ECO:0000313|EMBL:EKF25511.1};
GN ORFNames=C731_0470 {ECO:0000313|EMBL:EKF25511.1}, MHAS_04618
GN {ECO:0000313|EMBL:VCT92883.1};
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:EKF25511.1, ECO:0000313|Proteomes:UP000006265};
RN [1] {ECO:0000313|EMBL:EKF25511.1, ECO:0000313|Proteomes:UP000006265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 {ECO:0000313|EMBL:EKF25511.1}, 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:VCT92883.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mhassiacum {ECO:0000313|EMBL:VCT92883.1};
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 -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; AMRA01000013; EKF25511.1; -; Genomic_DNA.
DR EMBL; LR026975; VCT92883.1; -; Genomic_DNA.
DR RefSeq; WP_005624103.1; NZ_LR026975.1.
DR AlphaFoldDB; K5BI11; -.
DR STRING; 1122247.GCA_000379865_02626; -.
DR KEGG; mhas:MHAS_04618; -.
DR PATRIC; fig|1122247.3.peg.450; -.
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:InterPro.
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; 2.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 2.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 2.
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:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000313|EMBL:VCT92883.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006265}.
FT DOMAIN 6..95
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 218..343
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 377..469
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 473..566
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 579..725
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 731 AA; 78733 MW; 4D005817174FA940 CRC64;
MPIAITTEHN DLADSVRSLV ARVAPSEVLH EALETPIPNP PPYWKAAAEQ GLQGLHLAES
VGGQGFGILE LAIVIAEFGY GAVPGPFVPS VIASALIAAH DPADPRLAGL ASGETIAAYA
IESGLTATRT GDKLVIRGEV RAVPAAAQAS LLVLPVAIDS GEEWVVLDAD QVEIEPVQSV
DPLRPVAHVR VNAVEVGEDR VLSDLSRAHA RALVSTLLSA ECIGVARWAT DTASEYAKIR
EQFGRPIGKF QAVKHKCAEM IADTERATAA VWDAAQALDE LADKSAEETG FEFAAAVAAT
LAIDAVLHCT QDCIQVHGGI GFTWEHDTNV YYRRALGLAA AFGRRGEYPQ RVVDLATSTG
MRRLGIKLDP DTEKLRAEIR AEIDAIKAIP DDKERVVALA EGGWVVPHLP RPWGRGASPV
EQIIIAQEFQ DAKVERPNMG IASWLIPSVV AYGTEEQKQR FLPPTLRGEM IWCQLFSEPG
AGSDLASLTT KATKVEGGWR ITGQKIWTTG AQYSHWGMLL ARTDPDAPKH KGITYFLLDM
SSEGVEVKPL RELTGNAMFN TVFLDDVFVP DELVLGEVNR GWEVSRTTLT AERVSIGSSE
PPFLPNLNRF VEFIRDGHFD QVAKHQAGHL IAEGHAAKVL NMRSTLLTLA GGDPMPAAAI
GKLLSMRTGQ KYAEFVVASF GTEGAVGDPN ELTGRWAEFL LASRATTIYG GTSEVQLNII
AERLLGLPRD L
//
