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Database: UniProt
Entry: A0A0D4C183_9MICC
LinkDB: A0A0D4C183_9MICC
Original site: A0A0D4C183_9MICC 
ID   A0A0D4C183_9MICC        Unreviewed;       383 AA.
AC   A0A0D4C183;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AJT42452.1};
GN   ORFNames=UM93_14830 {ECO:0000313|EMBL:AJT42452.1};
OS   Psychromicrobium lacuslunae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Psychromicrobium.
OX   NCBI_TaxID=1618207 {ECO:0000313|EMBL:AJT42452.1, ECO:0000313|Proteomes:UP000061839};
RN   [1] {ECO:0000313|EMBL:AJT42452.1, ECO:0000313|Proteomes:UP000061839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHBB 11108 {ECO:0000313|EMBL:AJT42452.1,
RC   ECO:0000313|Proteomes:UP000061839};
RX   PubMed=25908143;
RA   Kiran S., Swarnkar M.K., Pal M., Thakur R., Tewari R., Singh A.K.,
RA   Gulati A.;
RT   "Complete Genome Sequencing of Protease-Producing Novel Arthrobacter sp.
RT   Strain IHBB 11108 Using PacBio Single-Molecule Real-Time Sequencing
RT   Technology.";
RL   Genome Announc. 3:0-0(2015).
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}.
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DR   EMBL; CP011005; AJT42452.1; -; Genomic_DNA.
DR   RefSeq; WP_045076309.1; NZ_CP011005.1.
DR   AlphaFoldDB; A0A0D4C183; -.
DR   STRING; 1618207.UM93_14830; -.
DR   KEGG; ari:UM93_14830; -.
DR   PATRIC; fig|1618207.4.peg.3020; -.
DR   HOGENOM; CLU_018204_0_3_11; -.
DR   OrthoDB; 2769798at2; -.
DR   Proteomes; UP000061839; Chromosome.
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; 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; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; ISOVALERYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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.
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:UP000061839}.
FT   DOMAIN          10..123
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          127..221
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          233..381
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   383 AA;  42030 MW;  E0C2ED81F64127A4 CRC64;
     MVLSRKLYQE EHEQFREIVR AFVEEYARPN VERWQQEGKV DRWLFTAAAE AGILGFSIPE
     EFGGGGSDDF RFNAVMGEEL ARHPVSDGMA GIALSNDIVI PYFLDLTNDE QKSRWLPGIA
     RGELITAVAM TEPGTGSDLA GIRTKAVRDG DDYIVNGSKI FISNGQNADL VVTAVRTSDD
     PHKGLSLLVI EGSSEGFFRG KNLEKIGLHA QDTSELIFDN VRVPAANLLG AEGAGFLGLM
     KNLPQERLSI AAAGVAASEG ILERTITYVK ERQAFGKSIG SFQNTRFELV EMHTAVQASR
     AYIDECITQH TAGKLSAVDA AAAKWWTTEQ LVNTVNRCLQ LHGGYGYMLE YRIAQDYLDA
     RITTIYGGTT EIMKEIVGRD LGL
//
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