ID A0A2V5JKY6_9MICC Unreviewed; 404 AA.
AC A0A2V5JKY6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:PYI38316.1};
GN ORFNames=CVS30_10970 {ECO:0000313|EMBL:PYI38316.1};
OS Arthrobacter psychrolactophilus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=92442 {ECO:0000313|EMBL:PYI38316.1, ECO:0000313|Proteomes:UP000247980};
RN [1] {ECO:0000313|EMBL:PYI38316.1, ECO:0000313|Proteomes:UP000247980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:PYI38316.1,
RC ECO:0000313|Proteomes:UP000247980};
RA Liu Q., Xin Y.-H.;
RT "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT glacialis sp. nov.";
RL Submitted (MAY-2018) 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:PYI38316.1}.
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DR EMBL; QJVC01000010; PYI38316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5JKY6; -.
DR OrthoDB; 9770681at2; -.
DR Proteomes; UP000247980; 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; PS00072; ACYL_COA_DH_1; 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:UP000247980}.
FT DOMAIN 34..139
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 145..238
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 254..397
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 404 AA; 44306 MW; B46EF223C45808B8 CRC64;
MISSKGMPVS KAAVDLNNLP YADGDFYGFE QLLSEKERER LQEIRDFLAK EVKPIAVDCW
NRGEFPMELI PKLAEANLMS PVRNQGYSNV FAGIVHAEFT RADASIATFM GVHDGLFTGS
IEALASEEQK AAWLPDIYAM KKIGAFGLTE PLGGSDVAGG TRTTAVRDGD NWILNGAKRW
IGNATFSDWV VIYARDLADN QVKAFMVDTK LPGYTATKIE NKISLRTVQN ADIVLDNVVV
PHEFKLAGAN SFRDTNKVLK VTRLAVAWQA VGQQLAAFDV ARRYAVERQQ FGRPIASFQM
VQDQLVQMLG NTVSSMGMMV RLAQLEDQGV AKDEQSALAK AFTTARMRET VAMGRNLLGG
NGIVTDYEMA KIFADAEAIY SYEGTYEINT LVTGRAITGI SAIV
//
