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Database: UniProt
Entry: A0A0Q8AKC1_9MICO
LinkDB: A0A0Q8AKC1_9MICO
Original site: A0A0Q8AKC1_9MICO 
ID   A0A0Q8AKC1_9MICO        Unreviewed;       390 AA.
AC   A0A0Q8AKC1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KQZ83297.1};
GN   ORFNames=ASD56_13425 {ECO:0000313|EMBL:KQZ83297.1};
OS   Microbacterium sp. Root166.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736478 {ECO:0000313|EMBL:KQZ83297.1, ECO:0000313|Proteomes:UP000051650};
RN   [1] {ECO:0000313|Proteomes:UP000051650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root166 {ECO:0000313|Proteomes:UP000051650};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ83297.1, ECO:0000313|Proteomes:UP000051650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root166 {ECO:0000313|EMBL:KQZ83297.1,
RC   ECO:0000313|Proteomes:UP000051650};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQZ83297.1}.
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DR   EMBL; LMGL01000003; KQZ83297.1; -; Genomic_DNA.
DR   RefSeq; WP_055966628.1; NZ_LMGL01000003.1.
DR   AlphaFoldDB; A0A0Q8AKC1; -.
DR   STRING; 1736478.ASD56_13425; -.
DR   Proteomes; UP000051650; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; IPR013107; Acyl-CoA_DH_C.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_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:SF25; ACYL-COA DEHYDROGENASE YDBM-RELATED; 1.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051650}.
FT   DOMAIN          16..85
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          246..369
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   390 AA;  41571 MW;  48C5410EA5BCD75F CRC64;
     MSDFDPRAFL PDDLLERIRE RAPIHDRDNT FPDADLAELR EAGYLAMLVP RELGGGGLGL
     AAASALQQRL AGAAPATALA VNMHLVWTGV AKVLADRGID DLRFVQEGAA SGEVFAFGIS
     EAGNDLVLFG SGTDAAPQPD GGYAFTGTKI FTSLAPVWTQ LGLHGLDTVS PDGPKMVYAF
     VSRSEEAEGR VVTADDWDTL GMRGTQSRTT RLRGAVAPAE RVARRIDPGP NPDPLVFGIF
     SVFEILLASV YTGIARRALS LAVEAAGART SKRTGKPYAQ DPDIRRRIAD MAVAYDALPP
     QLAALARDVD ELADHGPRWF SLLAGLKHRA VTAAKEIVDE AVLVAGGSSY FSSHELGRLY
     RDVLAGLFHP SDPESARSTV ATAWLGPLED
//
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