ID A0A1X1T469_9MYCO Unreviewed; 412 AA.
AC A0A1X1T469;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:BBZ38039.1};
GN ORFNames=AWC00_18100 {ECO:0000313|EMBL:ORV39384.1}, MCNS_11020
GN {ECO:0000313|EMBL:BBZ38039.1};
OS Mycobacterium conspicuum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=44010 {ECO:0000313|EMBL:BBZ38039.1, ECO:0000313|Proteomes:UP000467385};
RN [1] {ECO:0000313|EMBL:ORV39384.1, ECO:0000313|Proteomes:UP000193407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44136 {ECO:0000313|EMBL:ORV39384.1,
RC ECO:0000313|Proteomes:UP000193407};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBZ38039.1, ECO:0000313|Proteomes:UP000467385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14738 {ECO:0000313|EMBL:BBZ38039.1,
RC ECO:0000313|Proteomes:UP000467385};
RX PubMed=31287781;
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
RN [3] {ECO:0000313|EMBL:BBZ38039.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 14738 {ECO:0000313|EMBL:BBZ38039.1};
RA Matsumoto Y., Motooka D., Nakamura S.;
RL Submitted (FEB-2020) 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; AP022613; BBZ38039.1; -; Genomic_DNA.
DR EMBL; LQOR01000038; ORV39384.1; -; Genomic_DNA.
DR STRING; 44010.AWC00_18100; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000193407; Unassembled WGS sequence.
DR Proteomes; UP000467385; Chromosome.
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 CDD; cd00567; ACAD; 1.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF42; SHORT-CHAIN SPECIFIC ACYL-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 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|RuleBase:RU362125}.
FT DOMAIN 55..144
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 149..244
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 256..406
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 412 AA; 46855 MW; D73814995A7C8CFD CRC64;
MDFALPEHLP GLLAEMDAFI EREIAPLQAE NMQYFDQRRE HARTDWDNDG IPTAEWEELL
AEMRRRADRA GWLRYGLPAS LGGRDGTNVD MAVIREHLAH KGLGLHNDLQ NESSIVGNFP
QVIMMERFGT DEQRSVWSEA LITGQRSMAF GLTEPQHGSD ATWLETYAKP DGDSWVINGS
KRFNTGVHRA THDLIFARTS GEPGQARGIT AFLVPTDADG FNVPYYWWTF NMPTDHGEVE
LTDVRVPADA VLGEVDRGLE VAQTFLHENR IRQAASSLGA AQYCIDRAAD YAAKRVVFGK
PLSVNQAVQW PLAELQTEAQ MVRLLVHYAA WHLDRDHHME VSDKVSMANY RANRLVCDAA
DRAMQIFGGL GYSRHEPFEH IYRHHRRYRI TEGAEEIQIR RVAQRLFKFG TK
//
