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Database: UniProt
Entry: A0A0D1JPC6_9MYCO
LinkDB: A0A0D1JPC6_9MYCO
Original site: A0A0D1JPC6_9MYCO 
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
//
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