ID A0A0D1JPC6_9MYCO Unreviewed; 403 AA.
AC A0A0D1JPC6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KIU14429.1};
GN ORFNames=TL10_24410 {ECO:0000313|EMBL:KIU14429.1};
OS Mycolicibacterium llatzerense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU14429.1, ECO:0000313|Proteomes:UP000032221};
RN [1] {ECO:0000313|EMBL:KIU14429.1, ECO:0000313|Proteomes:UP000032221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLUC14 {ECO:0000313|EMBL:KIU14429.1,
RC ECO:0000313|Proteomes:UP000032221};
RA Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium llatzerense and Mycobacterium immunogenum
RT recovered from brain abscess.";
RL Submitted (JAN-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|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:KIU14429.1}.
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DR EMBL; JXST01000044; KIU14429.1; -; Genomic_DNA.
DR RefSeq; WP_043394708.1; NZ_LXSC01000040.1.
DR AlphaFoldDB; A0A0D1JPC6; -.
DR STRING; 280871.TL10_24410; -.
DR PATRIC; fig|280871.6.peg.5060; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000032221; Unassembled WGS sequence.
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; 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; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR48083:SF2; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000032221}.
FT DOMAIN 132..227
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 243..395
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 403 AA; 43315 MW; 5CA725CACE393541 CRC64;
MAINLEIPRK LQAVVEKGHQ GAAEMLRPIS RKYDLAEHAY PAELDTLASL FEGIQESNAV
SIAGAGFSAS ESKSKHANIN GANMSALLNA LEVSWGDVAL LLTVPYQGLG NAAISAVATK
DQLAKWGKVW AAMAITEPSF GSDSAAVSTT AVLDGDEWVI NGEKIFVTAG SRATHIVVWA
TLDRSLGRAA IKSFCVPREH PGVIVERLEH KLGIKASDTA VIRFDNCRIP KDYLLGDPEI
KVDKGFGGVM ETFDNTRPMV AAMAVGVGRA ALEELRTILT DAGIEISYDK PAHAQSAPAA
EFLRMESDWE AAYLLSLRAA WQADNKIPNS KEASMSKAKA GRMGTDVTLK AVELAGTTGY
SEEPLLEKWA RDSKILDIFE GTQQIQQLVV ARRLLGLSSA QLK
//