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Database: UniProt
Entry: A0A138ABP7_9ACTN
LinkDB: A0A138ABP7_9ACTN
Original site: A0A138ABP7_9ACTN 
ID   A0A138ABP7_9ACTN        Unreviewed;       402 AA.
AC   A0A138ABP7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KXP07830.1};
GN   ORFNames=AXK60_09400 {ECO:0000313|EMBL:KXP07830.1};
OS   Tsukamurella pseudospumae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=239498 {ECO:0000313|EMBL:KXP07830.1, ECO:0000313|Proteomes:UP000070258};
RN   [1] {ECO:0000313|Proteomes:UP000070258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15929 {ECO:0000313|Proteomes:UP000070258};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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}.
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:KXP07830.1}.
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DR   EMBL; LSRF01000055; KXP07830.1; -; Genomic_DNA.
DR   RefSeq; WP_068571747.1; NZ_LSRF01000055.1.
DR   AlphaFoldDB; A0A138ABP7; -.
DR   STRING; 239498.AXK60_09400; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000070258; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:InterPro.
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; IPR045008; ACX4-like.
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; PTHR43188; ACYL-COENZYME A OXIDASE; 1.
DR   PANTHER; PTHR43188:SF1; ACYL-COENZYME A OXIDASE 4, PEROXISOMAL; 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.
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|RuleBase:RU362125}.
FT   DOMAIN          29..139
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          144..236
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          249..395
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   402 AA;  44150 MW;  9D2BBD531452C35B CRC64;
     MSDRLTADLA EGIARARDTD YLNMNALLTE DERVLLAKVR VFGDRELLPI VNDYWERGEF
     PHEILPKLAA LNIVGDTMSG YGTTPMSAVG QGLVSYELGR LDGSIGTFMG VHVGLAMQSI
     YQLGSEEQRQ RWLPPMAALE KVGAFALTEP DHGSDSVALE STATLDGDTW ILNGRKRWPG
     NATWCDVIVV FARDTADGTV KGFVVEKDDP GYSATKIDGK VSLRMVQNAD IVLDEVRVPD
     DRRLVHCNGF PDVAKVLMGT RNMVAWSSAG HAVAAYEIAL TYAQRRIQFG QPIAQRQLIQ
     SQLVQMLADV TAMQLYCIRL GRLLDEGEVT DTMAALAKYY CSVKARDVCR QARDILGGNG
     ITLEFHVMRH LCDMEALVTY EGTAEIQSLI VGREVTGSGA FV
//
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