ID I4BT11_MYCCN Unreviewed; 381 AA.
AC I4BT11;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AFM20418.1};
GN OrderedLocusNames=Mycch_5799 {ECO:0000313|EMBL:AFM20418.1};
OS Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OG Plasmid pMYCCH.01 {ECO:0000313|EMBL:AFM20418.1,
OG ECO:0000313|Proteomes:UP000006057}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM20418.1, ECO:0000313|Proteomes:UP000006057};
RN [1] {ECO:0000313|EMBL:AFM20418.1, ECO:0000313|Proteomes:UP000006057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB4 {ECO:0000313|EMBL:AFM20418.1,
RC ECO:0000313|Proteomes:UP000006057};
RC PLASMID=pMYCCH.01 {ECO:0000313|EMBL:AFM20418.1,
RC ECO:0000313|Proteomes:UP000006057};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of plasmid 1 of Mycobacterium chubuense NBB4.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP003054; AFM20418.1; -; Genomic_DNA.
DR RefSeq; WP_014805688.1; NC_018022.1.
DR AlphaFoldDB; I4BT11; -.
DR KEGG; mcb:Mycch_5799; -.
DR PATRIC; fig|710421.3.peg.5789; -.
DR HOGENOM; CLU_018204_0_3_11; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000006057; Plasmid pMYCCH.01.
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; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125}; Plasmid {ECO:0000313|EMBL:AFM20418.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006057}.
FT DOMAIN 12..121
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 125..220
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..381
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 381 AA; 42084 MW; 10E881AA4FC2E784 CRC64;
MSSPISPWMN AELLELRDLA AKFFSAELAP HANRFADQHH VDRELWNRAG ELGLLCMSIP
EEYGGGGGTF AHEAVVLEEQ ARIGDSSWGA GLHSGIVAHY ILQYATEELR AQWLPKMASG
EMIGAIAMTE PGTGSDLQSV KTKALLDGDE YVITGSKTFI TNGQQADLII VVAKTDPSQG
AAGISLIAVE ADRVGFRRGK VLDKIGQRGQ DTSELFFDEV RVPRSHLLGQ AEGQGFIQLM
TQLPQERLIV AVGAVAAMEL ALEQTLKYTR EREAFGRPVF GFQNTKFTLA EAATETRIAR
VFLDYCIDLH LAGQLDVQTV AMAKWWTTER AMKVLDDCMQ LHGGYGYMTE YPISRLWVDQ
RVQKIYAGTN EVMKEIISRS L
//
