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Database: UniProt
Entry: A0A1H8KNU4_9MICO
LinkDB: A0A1H8KNU4_9MICO
Original site: A0A1H8KNU4_9MICO 
ID   A0A1H8KNU4_9MICO        Unreviewed;       392 AA.
AC   A0A1H8KNU4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:TFB95062.1};
GN   ORFNames=E3O10_01060 {ECO:0000313|EMBL:TFB95062.1};
OS   Cryobacterium luteum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=1424661 {ECO:0000313|EMBL:TFB95062.1, ECO:0000313|Proteomes:UP000297654};
RN   [1] {ECO:0000313|EMBL:TFB95062.1, ECO:0000313|Proteomes:UP000297654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hh15 {ECO:0000313|EMBL:TFB95062.1,
RC   ECO:0000313|Proteomes:UP000297654};
RA   Liu Q., Xin Y.-H.;
RT   "Genomics of glacier-inhabiting Cryobacterium strains.";
RL   Submitted (MAR-2019) 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:TFB95062.1}.
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DR   EMBL; SOFF01000004; TFB95062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8KNU4; -.
DR   STRING; 1424661.SAMN05216281_12030; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000297654; 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          26..129
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          133..226
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          244..385
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   392 AA;  42292 MW;  5777D3117D26E2E9 CRC64;
     MTFELLGSDF FGYENLLTAP ERAAIVKLRA YLEAEVRPIA NGCWDRAEFP TQIIKPLAEL
     GLYSFGWDET RPFENSAVFR GFVALELARV DASVSTFVGV QNGLAAGSLA ACGSAKQRAE
     WIPRLASGEI VGAFGLTEPL SGSDAAQGLR TTATRSGDSW TLNGAKRWIG NATFSDVTII
     WAKDTADNQV KGFIVPTDTA GYSATKIEGK ISLRAVQNAD ITLTDVVVPE SLRLQNANSF
     KDTAKVLRAT RAEVSWAAVG NAIGAYDAAV AYSKQREQFG KAIGGHQLVQ DLLVKSLGNI
     TASLGMVVRV SQLHDEGVQR DEHSALTKAY TTSRMRESVA WCRELFGGNG VTLEYNVARH
     FADAEAIYSY EGTQEMNTLI VGRTITGQAA FV
//
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